Journal articles on the topic 'Salivary peptide'
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1
Ito, Seiki, Toshimitsu Suzuki, Takeshi Momotsu, Satoko Isemura, Eiichi Saitoh, Kazuo Sanada, and Akira Shibata. "Presence of salivary Protein C and salivary peptide P-C-like immunoreactivity in the laryngo-tracheo-bronchial glands." Acta Endocrinologica 108, no. 1 (January 1985): 130–34. http://dx.doi.org/10.1530/acta.0.1080130.
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Abstract. An indirect immunofluorescence technique using antisera aganist salivary peptide P-C and against salivary Protein C was carried out on the laryngeal, tracheal and bronchial glands to examine whether salivary peptide P-C-like immunoreactivity, recently demonstrated in the serous cells of the human salivary glands, was also present in those of laryngeal, tracheal and bronchial glands and to ascertain whether salivary peptide P-C is a fragment of salivary Protein C or not. Salivary peptide P-C-like immunoreactivity was present in the serous cells of the human laryngeal, tracheal and bronchial glands. Observation of serial sections immunostained with two kinds of antisera revealed that cells reacting with antisera against salivary peptide P-C were identical to those reacting with antisera against salivary Protein C pre-incubated with salivary peptide P-C. The finding implied that salivary peptide P-C and salivary Protein C, originally isolated from human saliva, were also present in the serous cells of tissues other than the salivary glands. Furthermore, analysis of the primary structure of salivary peptide P-C and salivary Protein C together with the present morphological finding suggests that salivary peptide P-C is a COOH-terminal fragment of salivary Protein C. Thus, salivary Protein C and salivary peptide P-C may play some role in the function of the serous cells of the salivary and laryngo-tracheobronchial glands.
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Nicolodi, Maria, and Elena Del Bianco. "Sensory Neuropeptides (Substance P, Calcitonin Gene-Related Peptide) and Vasoactive Intestinal Polypeptide in Human Saliva: Their Pattern in Migraine and Cluster Headache." Cephalalgia 10, no. 1 (February 1990): 39–50. http://dx.doi.org/10.1046/j.1468-2982.1990.1001039.x.
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Substance P, calcitonin gene-related peptide and vasoactive intestinal polypeptide-like immunoreactivities have been evaluated in the saliva of 15 subjects suffering from migraine without aura and 16 control subjects. All three peptides were also measured in the symptomatic/non-symptomatic side saliva sampled from 10 cluster headache sufferers during the cluster period, 5 cluster headache sufferers out of the cluster period, as well as in the right and left side saliva of 18 control subjects. The most interesting result gives a clear difference in common migraine and cluster headache salivary vasoactive intestinal polypeptide-like immunoreactivity contents. In fact, these are enhanced during cluster headache attack and decreased during migraine attack when compared with the interictal period vasoactive intestinal polypeptide-like immunoreactivity levels. Another remarkable finding concerns the significant increase of substance P-like immunoreactivity and calcitonin gene-related peptide-like immunoreactivity levels, from basal values, in the saliva sampled during both migraine and cluster headache attacks. Control subjects showed a calcitonin gene-related peptide-like immunoreactivity and substance P-like immunoreactivity salivary contents significantly higher than migraine sufferers' saliva sampled in basal conditions. Conversely, calcitonin gene-related peptide-like immunoreactivities levels in controls were lower than in cluster headache sufferers' saliva obtained during intervals. Finally, during cluster headache attacks the enhancement of substance P-like immunoreactivity and vasoactive intestinal polypeptide-like immunoreactivity salivary contents interest the non-symptomatic side, whereas the symptomatic side salivary substance P-like immunoreactivity and vasoactive intestinal poly-peptide-like immunoreactivity contents remain unchanged. These findings do not allow any final conclusion. However, this biochemical evaluation indicates relevant changes of the salivary neuropeptides in diseases, such as migraine and cluster headache, in which pain transmission is surely involved.
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Ito, Seiki, Toshimitsu Suzuki, Tooru Izumi, Takeshi Momotsu, Satoko Isemura, Eiichi Saitoh, Kazuo Sanada, and Akira Shibata. "Intracellular localization of salivary peptide P-C-like immunoreactivity in the human pancreatic B-cells." Acta Endocrinologica 108, no. 1 (January 1985): 119–29. http://dx.doi.org/10.1530/acta.0.1080119.
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Abstract. In order to clarify the intracellular localization of salivary peptide P-C-like immunoreactivity in human pancreatic B-cells, an immunohistochemical study at electron microscopic levels was carried out by the protein A-gold technique using antisera against insulin and salivary peptide P-C. Both salivary peptide P-C-like immunoreactivity and insulin-like immunoreactivity were present only in the insulin secretory granules of the pancreatic B-cells. However, the former immunoreactivity was lacking in many insulin secretory granules of foetal pancreatic B-cells while the latter immunoreactivity was seen in all insulin secretory granules. Salivary peptide P-C-like immunoreactivity was not found in the other kinds of cells in the islets. In a previous immunohistochemical study at light microscopic level, salivary peptide P-C-like immunoreactivity appeared in a few pancreatic B-cells at about the 16th week of gestation, in an increasing number during gestation, and was seen in all pancreatic B-cells a few months after birth. The present finding together with the above results suggest that absence of salivary peptide P-C-like immunoreactivity in some foetal pancreatic B-cells may be due to the underdevelopment of salivary peptide P-C-like immunoreactivity in each insulin secretory granule. From the examination of cross-reactivity of antisera against salivary peptide P-C to other kinds of salivary peptides and salivary Protein C, and from the results of an indirect immunofluorescence technique using three kinds of antisera including antisera against salivary peptide P-C, salivary peptide P-B and salivary Protein C, it was thought that salivary peptide P-C-like immunoreactivity in human pancreatic B-cells belongs neither to salivary Protein C nor to salivary peptide P-B nor to salivary peptide P-E, but either to salivary peptide P-C itself or to an unknown substance which has common antigenic determinants with salivary peptide P-C, salivary peptide P-B and salivary Protein C. Salivary peptide P-C-like immunoreactivity was not found in the pancreatic B-cells of other mammals. Thus, although a new substance other than insulin is present in the insulin secretory granules of the human pancreatic B-cells, its pathophysiological function remains unclear.
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Veenstra, Jan A. "The salivary gland salivation stimulating peptide from Locusta migratoria (Lom-SG-SASP) is not a typical neuropeptide." PeerJ 5 (July 26, 2017): e3619. http://dx.doi.org/10.7717/peerj.3619.
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The salivary gland salivation stimulating peptide was identified from the salivary glands of the migratory locust by its ability to stimulate cAMP production in the same tissue. The gene coding for this peptide has recently been identified and been shown to code for a precursor consisting of a signal peptide, several copies of the peptide separated by Lys–Arg doublets and a few other peptides. These data are consistent with it being a neuropeptide. However, antiserum raised to this peptide labels the acini of the salivary glands while RT-PCR only gives positive results in the salivary gland, but not in any ganglion of the central nervous system. Thus, this peptide is not a typical neuropeptide as previously assumed.
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Morris, Katherine E., Chris D. St. Laurent, Ryan S. Hoeve, Jim Wickware, Paul Forsythe, Ron Mathison, and A. Dean Befus. "The sympathetic nervous system regulates the release of anti-inflammatory peptides from salivary glands (93.18)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 93.18. http://dx.doi.org/10.4049/jimmunol.182.supp.93.18.
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Abstract Chronic and acute stress have profound effects on inflammation. In rats, allergic inflammation is regulated by the sympathetic nervous system acting on salivary glands. Human asthma is frequently accompanied by salivary gland inflammation. Salivary gland dysfunction in stressed individuals could enhance asthma severity. Salivary gland prohormone SMR1 (submandibular rat-1) is cleaved into two peptides that are anti-inflammatory in rats, mice, dogs, sheep, cats, and human cells in pulmonary inflammation, food allergy, septic shock, pancreatitis, and spinal cord injury. We hypothesized that modulation of the autonomic nervous system would change the expression, processing, and secretion of SMR1 and its peptides. Rats were injected with saline, isoproterenol, or pilocarpine, or the superior cervical ganglion was excised. Saliva, blood, and tissues were collected and analyzed for SMR1. Adrenergic stimulation caused the majority of SMR1 into be secreted into saliva in 60 min. Removal of the superior cervical ganglion that innervates the salivary glands changed SMR1 protein levels in the salivary glands. SMR1 secretion into saliva in response to acute stress may provide a large pool of SMR1-derived peptide products that mediate anti-inflammatory responses locally and systemically. This research is funded by AllerGen NCE.
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Yi, Ting Chun, and Shabbir Moochhala. "Mini-Review Article – Current Opinion on Salivary Biomarkers as a Measurement for Stress and Fatigue." Open Biomarkers Journal 6, no. 1 (May 17, 2013): 9–14. http://dx.doi.org/10.2174/1875318301306010009.
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Salivary biomarkers have been increasingly popular in stress research as saliva is easily produced and collection is non-invasive and not limited by geographical distance or lack of infrastructure. Several salivary biomarkers have been utilized in stress research, for instance, salivary cortisol, salivary amylase and salivary immunoglobulin A. Despite being sensitive to changes in fatigue, they have limitations such as inter-individual variability, and interactions with other constituents that may confound the results. Recently, Hyperion Biotechnology has developed the Fatigue Biomarker Index (FBI), which is a measurement of the changes in concentration of salivary peptides with fatigue. The FBI has been shown to be an accurate and objective biomarker of fatigue, and has huge potential for use in various fields and industries. This article will review some of the previous and current salivary biomarkers of stress, as well as critically appraise the new salivary peptide test in terms of its accuracy, application and access.
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Tao, Renchuan, Richard J. Jurevic, Kimberly K. Coulton, Marjorie T. Tsutsui, Marilyn C. Roberts, Janet R. Kimball, Norma Wells, Jeffery Berndt, and Beverly A. Dale. "Salivary Antimicrobial Peptide Expression and Dental Caries Experience in Children." Antimicrobial Agents and Chemotherapy 49, no. 9 (September 2005): 3883–88. http://dx.doi.org/10.1128/aac.49.9.3883-3888.2005.
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ABSTRACT Dental caries is a major worldwide oral disease problem in children. Although caries are known to be influenced by dietary factors, the disease results from a bacterial infection; thus, caries susceptibility may be affected by host factors such as salivary antimicrobial peptides. This study aimed to determine a possible correlation between caries prevalence in children and salivary concentrations of the antimicrobial peptides human beta-defensin-3 (hBD-3), the cathelicidin LL37, and the alpha-defensins HNP1-3 (a mixture of HNP1, 2, 3). Oral examinations were performed on 149 middle school children, and unstimulated whole saliva was collected for immunoassays of the three peptides and for assay of caries-causing bacteria in saliva. The median salivary levels of hBD-3, LL37, and HNP1-3 were in the microgram/ml range but were highly variable in the population. While levels of LL37 and hBD-3 did not correlate with caries experience, the median HNP1-3 levels were significantly higher in children with no caries than in children with caries. Children with high caries levels did not have high levels of salivary Streptococcus mutans, and the HNP1-3 level was not correlated with salivary S. mutans. By immunohistochemistry we localized HNP1-3 in submandibular salivary duct cells. HNPs are also released by neutrophils into the gingival crevicular fluid. Both sources may account for their presence in saliva. Low salivary levels of HNP1-3 may represent a biological factor that contributes to caries susceptibility. This observation could lead to new ways to screen for caries susceptibility and to new means of assessing the risk for this common oral problem.
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Yasuda, Takuya, Koichiro Tahara, and Tetsuji Sawada. "Detection of salivary citrullinated cytokeratin 13 in healthy individuals and patients with rheumatoid arthritis by proteomics analysis." PLOS ONE 17, no. 3 (March 23, 2022): e0265687. http://dx.doi.org/10.1371/journal.pone.0265687.
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The immune response to citrullinated peptides in the mucosa has been suggested to play an important role in the transition from pre-onset rheumatoid arthritis (RA) to clinically evident RA. Although there are reports indicating the presence of anti-citrullinated peptide antibodies in the saliva, few studies have reported citrullinated peptide detection in human saliva. This study aimed to identify citrullinated peptides in human saliva and discuss their clinical significance. Saliva samples were collected from 11 patients with RA and from 20 healthy individuals. Citrullinated peptides were detected using an anti-modified citrulline (AMC) antibody. Saliva from the healthy individuals was subjected to two-dimensional protein electrophoresis to isolate citrullinated peptides, which were analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and mass spectrometry by peptide mass fingerprinting. The results were corroborated by immunoprecipitation (IP)-western blotting. The signal intensities of the bands precipitated with anti-cytokeratin 13 (CK13) and AMC antibodies were quantified. The signal intensity ratio of the band produced by the AMC antibody was divided by that of the band produced by the anti-CK13 antibody to calculate the citrullinated CK13 (Cit-CK13) ratio. A citrullinated peptide band corresponding to a molecular weight of approximately 50 kDa was detected in the saliva of healthy individuals, and identified as CK13 via mass spectrometry and IP-western blotting. No significant difference was observed between the salivary Cit-CK13 ratios of patients with RA and healthy participants (p = 0.605). This is the first study to show that Cit-CK13 is present in human saliva, and that there is no significant difference between the Cit-CK13 ratios of patients with RA and healthy individuals, suggesting that salivary Cit-CK13 content and RA development may not be associated. The physiological and pathological roles of Cit-CK13 in the oral cavity, and its responsiveness to mucosal immunity, remain unknown and will be the subject of further investigation.
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Ito, Seiki, Toshimitsu Suzuki, Satoko Isemura, Kazuo Sanada, Hiroyuki Anaguchi, Hirohiko Shimizu, Toshihiro Maruyama, and Akira Shibata. "'Salivary peptide P-C' of human pancreatic B-cells shares only partly immunoreactivity with salivary peptide P-C indicating a new B-cell protein which is different from insulin." Acta Endocrinologica 120, no. 1 (January 1989): 62–68. http://dx.doi.org/10.1530/acta.0.1200062.
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Abstract. Salivary peptide P-C like immunoreactivity, originally isolated from human whole saliva has later been found in the human pancreatic B-cells. In the present work an indirect immunofluorescence technique using monoclonal antibodies against isolated salivary peptide P-C was applied to Bouin fixed pancreas and parotid glands to study the possible identity of the two substances. Positive P-C immunofluroescence was found in the serous cells of parotid glands but not in pancreatic B-cells, suggesting that pancreatic P-C substance is not salivary peptide P-C itself, but a substance sharing the common antigenic site with salivary peptide P-C. To examine this, an indirect immunofluorescence technique using polyclonal P-C antisera pre-absorbed with six kinds of synthetic fragments (1–22, 23–44, 23–29, 30–44, 30–38 and 38–44) of salivary peptide P-C was applied to the human pancreas. The result showed that pancreatic P-C substance was a substance which shares the common antigenic site with the 38–44 amino acid residue of salivary peptide P-C. Western blot analysis using extracts of human pancreata further showed that pancreatic P-C substance is not a precursor of insulin but a protein with molecular weight of 11 500 dalton, indicating the presence of a new protein in the insulin secretory granules of human pancreatic B-cells.
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Hamada, Tomoyuki, Masatsugu Kawashima, Haruo Watanabe, Junji Tagami, and Hidenobu Senpuku. "Molecular Interactions of Surface Protein Peptides of Streptococcus gordonii with Human Salivary Components." Infection and Immunity 72, no. 8 (August 2004): 4819–26. http://dx.doi.org/10.1128/iai.72.8.4819-4826.2004.
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ABSTRACT Oral streptococci play a large role in dental biofilm formation, and several types interact as early colonizers with the enamel salivary pellicle to form the primary biofilm, as well as to incorporate other bacteria on tooth surfaces. Interactions of surface molecules of individual streptococci with the salivary pellicle on the tooth surface have an influence on the etiological properties of an oral biofilm. To elucidate the molecular interactions of streptococci with salivary components, binding between surface protein (SspB and PAg) peptides of Streptococcus gordonii and Streptococcus sobrinus were investigated by utilizing BIAcore biosensor technology. The analogous peptide [change of T at position 400 to K in SspB(390-402), resulting in the SspB(390-T400K-402) peptide] from S. gordonii showed the greatest response for binding to salivary components and inhibited the binding of Streptococcus sanguis by more than 50% in a competitive inhibition assay in a comparison with other SspB and PAg peptides. This peptide also bound to the high-molecular-weight protein complex of salivary components and the agglutinin (gp340/DMBT1) peptide (scavenger receptor cysteine-rich domain peptide 2 [SRCRP 2]). In addition, the SspB(390-T400K-402) peptide was visualized by two surface positive charges in connection with the positively charged residues, in which lysine was a key residue for binding. Therefore, the region containing lysine may have binding activity in S. gordonii and S. sanguis, and the SRCRP 2 region may function as a receptor for the binding. These findings may provide useful information regarding the molecular mechanism of early biofilm formation by streptococci on tooth surfaces.
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Bachrach, G., G. Chaushu, M. Zigmond, E. Yefenof, A. Stabholz, J. Shapira, J. Merrick, and S. Chaushu. "Salivary LL-37 Secretion in Individuals with Down Syndrome is Normal." Journal of Dental Research 85, no. 10 (October 2006): 933–36. http://dx.doi.org/10.1177/154405910608501012.
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Antimicrobial peptides play an important role in the innate immune response. Deficiency in salivary LL-37 antimicrobial peptide has been implicated in periodontitis in patients with morbus Kostman syndrome. Down syndrome is associated with periodontitis, diminished salivary flow, and salivary immunoglobulin deficiency. In the present study, levels of LL-37 and its hCAP18 precursor were measured in saliva samples from young individuals with Down syndrome and compared with levels in those from age-matched healthy controls. LL-37 and human cathelicidin antimicrobial protein (hCAP18) were detected in whole but not in parotid saliva. hCAP18 was more abundant than LL-37. The concentrations of salivary hCAP18 and LL-37 were found to be higher in individuals with Down syndrome than in healthy controls, but their secretion rates were similar. We concluded that, while the adaptive immunity of individuals with Down syndrome is impaired at the oral mucosa, the secretion rate of the LL-37 component of the innate immune system is normal.
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Lamkin, Mark S., and Frank G. Oppenheim. "Structural Features of Salivary Function." Critical Reviews in Oral Biology & Medicine 4, no. 3 (April 1993): 251–59. http://dx.doi.org/10.1177/10454411930040030101.
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Saliva plays an important role in the maintenance of oral health by exhibiting multiple host defense functions. These include homeostatic processes, lubrication, antimicrobial activity, and the control of demineralization/remineralization of teeth. Biochemical studies of saliva and salivary secretions established that specific salivary proteins are responsible for these defense functions. Because some of these salivary proteins have been characterized extensively, including their primary structures, it has become feasible to explore their structure/function relationships. Acidic proline-rich proteins (PRPs), for example, exhibit high affinity to hydroxyapatite, inhibit crystal growth of calcium phosphate salts from solutions supersaturated with respect to hydroxyapatite, bind calcium ions, and interact with several oral bacteria on adsorption to hydroxyapatite. Statherins, histatins, and cystatins also exhibit affinities to mineral surfaces, inhibit calcium phosphate precipitation, and play a role in maintaining the integrity of teeth. Furthermore, histatins exhibit both antibacterial and antifungal activities. Approaches to identifying the functional domains of these salivary proteins include functional assays of enzymatically digested proteins and peptides, synthetic peptides and peptide analogues, and chemically modified proteins as well as biophysical studies of native proteins or peptides. Such studies have demonstrated that the fungicidal activities of histatins reside in the middle portion of the polypeptide chain, whereas the hydroxyapatite binding domains of PRPs and statherin reside in the phosphorylated amino-terminal regions. Identification of functional domains is vital in understanding the mechanisms of action and this information can be exploited in the development of therapeutic agents.
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Almoudi, Manal Mohamed, Alaa Sabah Hussein, Mohamed Ibrahim Abu-Hassan, Bahruddin Saripudin, and Mohd Shawal Firdaus Mohamad. "The Association of Early Childhood Caries with Salivary Antimicrobial Peptide LL37 and Mutans Streptococci." Journal of Clinical Pediatric Dentistry 45, no. 5 (November 1, 2021): 330–36. http://dx.doi.org/10.17796/1053-4625-45.5.7.
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Purpose: This study aims to determine the relation of salivary LL37 level and mutans streptococci levels in early childhood caries (ECC). Study design: A case-control study was performed in children ≤71 months old. Unstimulated whole saliva was collected and the level of salivary LL37 was measured using an enzyme-linked immunosorbent assay kit. The mutans streptococci oral bacteria were isolated from saliva and identified using a modified SB-20 culture medium (SB-20M). Data were analyzed using descriptive statistics, bivariate, and Spearman’s rank correlation analysis. Results: The was a variability of salivary LL37 level among the children and the level was significantly associated with age and races. The median (IQR) value of salivary LL37 in caries-free (CF) children was significantly higher 393.50 (580.55) ng/mL compared to 172.50 (234.65) ng/mL in the ECC group. The ECC children exhibited a significantly higher count of S. mutans and S. sobrinus compared to the CF children. An inverse weak correlation between salivary LL37 and dmft was also observed. Conclusions: The low salivary LL37 level and higher S. mutans and S. sobrinus count in ECC supported the protective role of salivary LL37 against dental caries. Further studies are required to explore the definite relation between salivary LL37 levels and dental caries.
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Hormdee, Doosadee, Saengsome Prajaneh, Amonrujee Kampichai, Ranuch Tak, and Ponlatham Chaiyarit. "Prolonged Suppressive Effects of Periodontitis on Salivary TFF3 Production." European Journal of Dentistry 13, no. 02 (May 2019): 193–98. http://dx.doi.org/10.1055/s-0039-1693949.
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Abstract Objective As a follow-up to our previous study that demonstrated decreased salivary trefoil factor family 3 (TFF3) peptide levels in chronic periodontitis patients, this current study aimed to observe the effects of nonsurgical periodontal treatment on salivary TFF3 peptides in patients with periodontal diseases. Materials and Methods Eighty-seven volunteers that comprised of 30 individuals with healthy periodontium, 31 with gingivitis, and 26 with chronic periodontitis were considered for the study. Prior to periodontal treatment, a general periodontal examination was performed along with collection of saliva samples from each volunteer. Nonsurgical periodontal treatments were provided to patients with gingivitis and periodontitis. Two weeks post-treatment, saliva samples were recollected, and the periodontal status was re-evaluated. Salivary TFF3 concentrations were measured by enzyme-linked immunosorbent assay. Statistical Analysis Mann–Whitney U test was used when the investigated data were not normally distributed. Chi-squared test was used when dealing with categorical data. Kruskal–Wallis test with post-hoc corrections was used to compare data among the three investigated groups. Two-tailed p < 0.05 was considered as statistically significant. Results Prior to the periodontal treatment, salivary TFF3 concentrations in patients with gingivitis and periodontitis were significantly lower than those with healthy periodontium. Two weeks post-treatment, increased levels of salivary TFF3 were observed in patients with gingivitis, whereas the concentrations decreased in patients with chronic periodontitis. Conclusion This study demonstrated the effects of periodontal disease on the production of salivary TFF3 peptides. Interestingly, nonsurgical periodontal treatment also affected the recovery of salivary TFF3 peptides but varied in their outcomes between gingivitis and periodontitis patients.
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Ribeiro, J. M. "Characterization of a vasodilator from the salivary glands of the yellow fever mosquito Aedes aegypti." Journal of Experimental Biology 165, no. 1 (April 1, 1992): 61–71. http://dx.doi.org/10.1242/jeb.165.1.61.
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Salivary gland homogenates and oil-induced saliva of the mosquito Aedes aegypti dilate the rabbit aortic ring and contract the guinea pig ileum. The vasodilatory activity is endothelium-dependent, heat-stable, sensitive to both trypsin and chymotrypsin treatments, and both smooth muscle activities cross-desensitize to the tachykinin peptide substance P. Both bioactivities co-elute when salivary gland homogenates are fractionated by reversed-phase HPLC. Molecular sieving chromatography indicates a relative molecular mass of 1400. A monoclonal antibody specific to the carboxy terminal region of tachykinins reacts with material in the posterior part of the central lobe of paraformaldehyde-fixed salivary glands. The presence of a vasodilatory peptide of the tachykinin family in the salivary glands of A. aegypti is proposed and its role in blood feeding is discussed.
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Hoffmann, Werner. "Salivary Trefoil Factor Family (TFF) Peptides and Their Roles in Oral and Esophageal Protection: Therapeutic Potential." International Journal of Molecular Sciences 22, no. 22 (November 12, 2021): 12221. http://dx.doi.org/10.3390/ijms222212221.
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Human saliva is a complex body fluid with more than 3000 different identified proteins. Besides rheological and lubricating properties, saliva supports wound healing and acts as an antimicrobial barrier. TFF peptides are secreted from the mucous acini of the major and minor salivary glands and are typical constituents of normal saliva; TFF3 being the predominant peptide compared with TFF1 and TFF2. Only TFF3 is easily detectable by Western blotting. It occurs in two forms, a disulfide-linked homodimer (Mr: 13k) and a high-molecular-mass heterodimer with IgG Fc binding protein (FCGBP). TFF peptides are secretory lectins known for their protective effects in mucous epithelia; the TFF3 dimer probably has wound-healing properties due to its weak motogenic effect. There are multiple indications that FCGBP and TFF3-FCGBP play a key role in the innate immune defense of mucous epithelia. In addition, homodimeric TFF3 interacts in vitro with the salivary agglutinin DMBT1gp340. Here, the protective roles of TFF peptides, FCGBP, and DMBT1gp340 in saliva are discussed. TFF peptides are also used to reduce radiotherapy- or chemotherapy-induced oral mucositis. Thus, TFF peptides, FCGBP, and DMBT1gp340 are promising candidates for better formulations of artificial saliva, particularly improving wound healing and antimicrobial effects even in the esophagus.
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Kapas, S., K. Pahal, A. T. Cruchley, E. Hagi-Pavli, and J. P. Hinson. "Expression of Adrenomedullin and its Receptors in Human Salivary Tissue." Journal of Dental Research 83, no. 4 (April 2004): 333–37. http://dx.doi.org/10.1177/154405910408300412.
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Adrenomedullin is a multifunctional peptide produced by a wide range of different cells and tissues. This study was designed to investigate whether adrenomedullin is present in human saliva and in salivary glands. It was expected that saliva may contain high concentrations of adrenomedullin, which has antimicrobial activity in vitro, which may have functional implications in the oral cavity. Saliva from the submandibular and parotid glands contained higher concentrations of adrenomedullin than did the circulation, but lower concentrations than in whole saliva. This suggests that oral epithelium may contribute the majority of the adrenomedullin peptide found in saliva. Specific adrenomedullin receptors were found in cell lines from the submandibular (HSG) and parotid (HSY) salivary glands. These findings suggest a paracrine/autocrine role for adrenomedullin in these tissues; however, the concentration of adrenomedullin in saliva was insufficient to suggest a significant antimicrobial action in the healthy oral cavity.
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Morris, K. E., C. D. St. Laurent, R. S. Hoeve, P. Forsythe, M. R. Suresh, R. D. Mathison, and A. D. Befus. "Autonomic nervous system regulates secretion of anti-inflammatory prohormone SMR1 from rat salivary glands." American Journal of Physiology-Cell Physiology 296, no. 3 (March 2009): C514—C524. http://dx.doi.org/10.1152/ajpcell.00214.2008.
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The autonomic nervous system regulates the secretion of bioactive proteins and peptides from salivary glands that can be important in systemic physiological responses. The prohormone submandibular rat-1, which is highly expressed in rat submandibular glands, can be cleaved to produce polypeptides with analgesic and anti-inflammatory activities. Human genes related to submandibular rat-1 have conserved biological functions and are potentially important in pain suppression, erectile function, and inflammation. In this study we describe the differential expression and posttranslational modification of submandibular rat-1 protein in salivary glands, the urogenital tract, lung, blood, and saliva in male Sprague-Dawley and Brown Norway rats. Submandibular rat-1 protein is secreted into saliva after the administration of β-adrenergic or cholinergic agonists. Removal of the sympathetic ganglion that innervates the salivary glands results in increased levels of submandibular rat-1 protein in salivary glands. The secretion of submandibular rat-1 in response to physiological stress may provide a large pool of submandibular rat-1-derived peptide products that can promote analgesia and decrease inflammation locally and systemically. This pathway may be conserved among mammals and may constitute an important anti-inflammatory and analgesic response to stress.
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Rowzee, Anne M., Niamh X. Cawley, John A. Chiorini, and Giovanni Di Pasquale. "Glucagon-Like Peptide-1 Gene Therapy." Experimental Diabetes Research 2011 (2011): 1–5. http://dx.doi.org/10.1155/2011/601047.
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Glucagon-like peptide 1 (GLP-1) is a small peptide component of the prohormone, proglucagon, that is produced in the gut. Exendin-4, a GLP-1 receptor agonist originally isolated from the saliva ofH. suspectumor Gila monster, is a peptide that shares sequence and functional homology with GLP-1. Both peptides have been demonstrated to stimulate insulin secretion, inhibit glucagon secretion, promote satiety and slow gastric emptying. As such, GLP-1 and Exendin-4 have become attractive pharmaceutical targets as an adjunctive therapy for individuals with type II diabetes mellitus, with several products currently available clinically. Herein we summarize the cell biology leading to GLP-1 production and secretion from intestinal L-cells and the endocrine functions of this peptide and Exendin-4 in humans. Additionally, gene therapeutic applications of GLP-1 and Exendin-4 are discussed with a focus on recent work using the salivary gland as a gene therapy target organ for the treatment of diabetes mellitus.
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Smith, Daniel J., William F. King, Leigh A. Barnes, Debra Trantolo, Donald L. Wise, and Martin A. Taubman. "Facilitated Intranasal Induction of Mucosal and Systemic Immunity to Mutans Streptococcal Glucosyltransferase Peptide Vaccines." Infection and Immunity 69, no. 8 (August 1, 2001): 4767–73. http://dx.doi.org/10.1128/iai.69.8.4767-4773.2001.
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ABSTRACT Synthetic peptide vaccines which are derived from functional domains of Streptococcus mutans glucosyltransferases (GTF) have been shown to induce protective immunity in Sprague-Dawley rats after subcutaneous injection in the salivary gland region. Since mucosal induction of salivary immunity would be preferable in humans, we explored methods to induce mucosal antibody in the rat to the GTF peptide vaccines HDS and HDS-GLU after intranasal administration. Several methods of facilitation of the immune response were studied: the incorporation of peptides in bioadhesive poly(d,l-lactide-coglycolide) (PLGA) microparticles, the use of monoepitopic (HDS) or diepitopic (HDS-GLU) peptide constructs, or the use of mucosal adjuvants. Salivary immunoglobulin A (IgA) responses were not detected after intranasal administration of diepitopic HDS-GLU peptide constructs in alum or after incorporation into PLGA microparticles. However, significant primary and secondary salivary IgA and serum IgG antibody responses to HDS were induced in all rats when cholera holotoxin (CT) or a detoxified mutant Escherichia coli heat-labile enterotoxin (R192G LT) were intranasally administered with HDS peptide constructs in PLGA. Coadministration of LT with HDS resulted in predominantly IgG2a responses in the serum, while coadministration with CT resulted in significant IgG1 and IgG2a responses to HDS. Serum IgG antibody, which was induced to the HDS peptide construct by coadministration with these adjuvants, also bound intact mutans streptococcal GTF in an enzyme-linked immunosorbent assay and inhibited its enzymatic activity. Thus, immune responses which are potentially protective for dental caries can be induced to peptide-based GTF vaccines after mucosal administration if combined with the CT or LT R192G mucosal adjuvant.
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Smith, P. H., and B. B. Toms. "Immunocytochemical localization of insulin- and glucagonlike peptides in rat salivary glands." Journal of Histochemistry & Cytochemistry 34, no. 5 (May 1986): 627–32. http://dx.doi.org/10.1177/34.5.3517146.
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An avidin-biotin immunocytochemical technique was used to localize cells containing an insulin- or glucagon-like peptide in the major salivary glands of Sprague-Dawley rats. Cells with insulin-like staining were observed in the intercalated ducts of both the parotid and submandibular glands, but none were found in the sublingual gland. A discrete population of cells with intense glucagon-like immunostaining was associated with the acini of all three major salivary glands. This immunostaining only followed use of a glucagon antiserum with N-terminal specificity and not after incubation of tissues with an anti-glucagon serum having C-terminal specificity. These results suggest that rat salivary glands may contain peptides potentially capable of influencing substrate metabolism. In addition, the present findings indicate that the glucagon-like peptide found in salivary glands has a greater immunocytochemical similarity to glicentin (gut-type glucagon) and/or glucagon precursors than to the 3500 molecular weight pancreatic glucagon.
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Nogueira, R. D., W. F. King, G. Gunda, S. Culshaw, M. A. Taubman, R. O. Mattos-Graner, and D. J. Smith. "Mutans Streptococcal Infection Induces Salivary Antibody to Virulence Proteins and Associated Functional Domains." Infection and Immunity 76, no. 8 (May 12, 2008): 3606–13. http://dx.doi.org/10.1128/iai.00214-08.
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ABSTRACTThe interplay between mucosal immune responses to natural exposure to mutans streptococci and the incorporation and accumulation of these cariogenic microorganisms in oral biofilms is unclear. An initial approach to explore this question would be to assess the native secretory immunity emerging as a consequence ofStreptococcus mutansinfection. To this end, we analyzed salivary immunoglobulin A (IgA) antibody to mutans streptococcal glucosyltransferase (Gtf) and glucan binding protein B (GbpB) and to domains associated with enzyme function and major histocompatibility complex (MHC) class II binding in two experiments. Salivas were collected from approximately 45-day-old Sprague-Dawley rats, which were then infected withS. mutansSJ32. Infection was verified and allowed to continue for 2 to 2.5 months. Salivas were again collected following the infection period. Pre- and postinfection salivas were then analyzed for IgA antibody activity using peptide- or protein-coated microsphere Luminex technology.S. mutansinfection induced significant levels of salivary IgA antibody to Gtf (P< 0.002) and GbpB (P< 0.001) in both experiments, although the levels were usually far lower than the levels achieved when mucosal immunization is used. Significantly (P< 0.035 toP< 0.001) elevated levels of postinfection salivary IgA antibody to 6/10 Gtf peptides associated with either enzyme function or MHC binding were detected. The postinfection levels of antibody to two GbpB peptides in the N-terminal region of the six GbpB peptides assayed were also elevated (P< 0.031 andP< 0.001). Interestingly, the patterns of the rodent response to GbpB peptides were similar to the patterns seen in salivas from young children during their initial exposure toS. mutans.Thus, the presence of a detectable postinfection salivary IgA response to mutans streptococcal virulence-associated components, coupled with the correspondence between rat and human mucosal immune responsiveness to naturally presented Gtf and GbpB epitopes, suggests that the rat may be a useful model for defining mucosal responses that could be expected in humans. Under controlled infection conditions, such a model could prove to be helpful for unraveling relationships between the host response and oral biofilm development.
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Amano, Atsuo, Satoshi Shizukuishi, Hiroshi Horie, Shigenobu Kimura, Ichijiro Morisaki, and Shigeyuki Hamada. "Binding of Porphyromonas gingivalisFimbriae to Proline-Rich Glycoproteins in Parotid Saliva via a Domain Shared by Major Salivary Components." Infection and Immunity 66, no. 5 (May 1, 1998): 2072–77. http://dx.doi.org/10.1128/iai.66.5.2072-2077.1998.
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ABSTRACT Porphyromonas gingivalis, a putative periodontopathogen, can bind to human saliva through its fimbriae. We previously found that salivary components from the submandibular and sublingual glands bind to P. gingivalis fimbriae and that acidic proline-rich protein (PRP) and statherin function as receptor molecules for fimbriae. In this study, we investigated the fimbria-binding components in parotid saliva. Fractionated human parotid saliva by gel-filtration chromatography was immobilized onto nitrocellulose membranes for the overlay assay following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The salivary components on the membrane were allowed to interact with fimbriae purified fromP. gingivalis ATCC 33277, and the interacted fimbriae were probed with anti-fimbria antibodies. The fimbriae were shown to bind to two forms of proline-rich glycoproteins (PRGs) as well as to acidic PRPs and statherin. Moreover, fimbriae bound to several components of smaller molecular size which appeared to be acidic PRP variants and basic PRPs. Fimbriae bound strongly to the purified PRGs adsorbed onto hydroxyapatite (HAP) beads. In contrast, PRGs in solution failed to inhibit the fimbrial binding to the immobilized PRGs on the HAP beads. These findings suggest that the appearance of binding site(s) of PRGs can be ascribed to their conformational changes. We previously identified the distinct segments within PRP and statherin molecules that are involved in fimbrial binding. The peptides analogous to the binding regions of PRP and statherin (i.e., PRP-C and STN-C) markedly inhibit the binding of fimbriae to PRP and statherin immobilized on the HAP beads, respectively. The PRP-C significantly inhibited the binding of fimbriae to PRG-coated HAP beads as well as to PRP on HAP beads. The peptide did not affect the binding of fimbriae to statherin, whereas the STN-C showed no effect on the fimbrial binding to PRPs or PRGs. In the overlay assay, the PRP-C clearly diminished the interactions between the fimbriae and the various salivary components, including PRPs, the PRGs, and the components with smaller molecular sizes but not statherin. These results strongly suggest that fimbriae bind to salivary components (except statherin) via common peptide segments. It is also suggested that fimbriae bind to saliva through the two distinct binding domains of receptory salivary components: (i) PRGs and PRPs and (ii) statherin.
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Aidoukovitch, Alexandra, Sara Bodahl, Ellen Tufvesson, and Bengt-Olof Nilsson. "Desquamated Epithelial Cells of Unstimulated Human Whole Saliva Express Both EGF Transcript and Protein." International Journal of Dentistry 2022 (December 17, 2022): 1–9. http://dx.doi.org/10.1155/2022/3194703.
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Objective. The aim of this study was to investigate if desquamated oral epithelial cells (DOECs) express the epidermal growth factor (EGF) and if these cells thereby may contribute to salivary EGF contents. Background. DOECs have recently been shown to harbor the antimicrobial peptide LL-37, proposing that they may also store other biologically important salivary peptides/proteins. The EGF peptide is a growth factor which plays a critical role to maintain epithelial integrity and promote epithelial healing. The EGF is produced by salivary glands, but it is not known whether DOECs contain the EGF and thereby contribute to salivary EGF levels. Materials and Methods. DOECs were isolated from unstimulated whole saliva collected from four healthy volunteers. EGF protein expression was determined in cell lysates by dot blot and ELISA. Cellular distribution of cytokeratin, the proliferation marker Ki67, and EGF immunoreactivity were assessed by immunocytochemistry. EGF gene expression was investigated by qPCR. Expression of EGF transcript and protein in DOECs was compared to that in the human cultured keratinocyte cell line (HaCaT) cells. Results. EGF protein expression was detected in DOEC cell lysates by both dot blot and ELISA. Strong cytoplasmic EGF immunoreactivity was observed in DOECs, although some cells showed only a weak immunoreactive signal for EGF. Moreover, DOECs, besides containing EGF protein, also expressed transcript for EGF. Interestingly, ELISA analysis revealed that EGF protein contents were higher in DOECs than in HaCaT cells. ELISA analysis also disclosed that EGF concentration was about 10 times higher in whole saliva compared to DOECs. EGF transcript expression was about 50% lower in HaCaT cells stimulated with high (10%) compared to low (0.1%) concentration of fetal bovine serum, representing growth-stimulated and growth-restricted conditions, respectively, implying that growth-stimulus exerts negative feedback on EGF gene activity in HaCaT cells. Conclusion. Here, we show for the first time that DOECs express the EGF, arguing that these cells contribute to salivary EGF contents and hence may play a role in gingival epithelial repair and wound healing.
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Dekker, Rebecca L., Terry A. Lennie, Debra K. Moser, Craig S. Miller, Jeffrey L. Ebersole, Misook L. Chung, Charles L. Campbell, Alison Bailey, and Elizabeth G. Tovar. "Salivary Biomarkers, Oral Inflammation, and Functional Status in Patients With Heart Failure." Biological Research For Nursing 19, no. 2 (September 20, 2016): 153–61. http://dx.doi.org/10.1177/1099800416665197.
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Aims: To describe correlations and agreement between salivary and serum B-type natriuretic peptide (BNP), C-reactive protein (CRP), interleukin (IL)-6, and IL-10 and determine which biomarkers predict worse functional class in patients with heart failure (HF). Methods: Serum and saliva were collected from 75 hospitalized patients with HF (57 ± 12 years, 43% female, New York Heart Association [NYHA] Classes I [4%], II [43%], and III [53%]). Oral inflammation was rated as good, fair, or poor. Spearman’s ρ and Bland–Altman were used to determine correlations and agreement of the salivary and serum forms of each biomarker. Logistic regressions were used to determine which biomarkers predicted worse NYHA functional class, controlling for depression, body mass index, smoking, and oral inflammation. Results: Median biomarker concentrations were as follows: BNP (serum 361 pg/ml, saliva 9 pg/ml), CRP (serum 13 ng/ml, saliva 25.6 ng/ml), IL-6 (serum 19.3 pg/ml, saliva 10.5 pg/ml), and IL-10 (serum 64.1 pg/ml, saliva 4.7 pg/ml). There was a moderate-to-strong correlation for serum–salivary CRP, weak correlation for serum–salivary IL-6, and no correlations for serum–salivary BNP and IL-10. The Bland–Altman test showed good salivary–serum agreement for all biomarkers, but as serum concentrations rose, salivary measures underestimated serum levels. Visible oral inflammation was the only predictor of worse NYHA class.
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Situ, Hongsa, and Libuse A. Bobek. "In Vitro Assessment of Antifungal Therapeutic Potential of Salivary Histatin-5, Two Variants of Histatin-5, and Salivary Mucin (MUC7) Domain 1." Antimicrobial Agents and Chemotherapy 44, no. 6 (June 1, 2000): 1485–93. http://dx.doi.org/10.1128/aac.44.6.1485-1493.2000.
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ABSTRACT Human salivary histatin-5 (Hsn-5) is a 24-residue peptide that possesses potent antifungal activity in vitro. The MUC7gene encodes human salivary low-molecular-weight mucin (MG2). The candidacidal activity of MUC7 domain 1 (MUC7 D1, the N-terminal 51 amino acid residues of MUC7) in vitro has also been demonstrated. In this study, we have investigated the antifungal therapeutic potential of Hsn-5, its two variants, R12I/K17N and R12I/H21L, and MUC7 D1. First, these peptides were tested for activities against different clinically important fungi. We found them to possess broad-spectrum antifungal activities; specifically, most exhibited excellent in vitro activity against eight clinically important fungal strains tested, including Candida albicansand Candida glabrata and their azole-resistant counterparts and Cryptococcus neoformans and its amphotericin B-resistant counterpart. These findings also suggest that the mechanism of action of both Hsn-5 and MUC7 D1 for these fungi is different from that of amphotericin B or azole antifungal agents. Second, we examined the stability of these peptides in whole human saliva and human serum. In saliva, the Hsn-5 variants R12I/K17N and R12I/H21L and MUC7 D1 degraded at a lower rate than Hsn-5. In human serum, MUC7 D1 was also more stable than Hsn-5; both peptides were more stable in serum than in saliva. Third, we examined the cytotoxicity of these peptides using human erythrocytes and two human cell lines (KB and HSG). No (or very low) hemolytic activity was observed with any of the four peptides, even at the highest protein concentration tested (200 μM), while amphotericin B caused 100% hemolysis at only 12.5 μM. The toxic effects of Hsn-5 and MUC7 D1 toward KB and HSG cells were also much lower than that of amphotericin B as measured by trypan blue exclusion. Together, these findings indicate that the investigated peptides possess high antifungal therapeutic potential, in particular for the treatment of drug-resistant fungal strains associated with immunocompromised (particularly human immunodeficiency virus-infected) patients. The same peptides could also be used as components of artificial saliva for patients with salivary dysfunction.
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Messenger, B., MN Clifford, and LM Morgan. "Glucose-dependent insulinotropic polypeptide and insulin-like immunoreactivity in saliva following sham-fed and swallowed meals." Journal of Endocrinology 177, no. 3 (June 1, 2003): 407–12. http://dx.doi.org/10.1677/joe.0.1770407.
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Gastrointestinal peptides, including insulin, glucagon and glucose-dependent insulinotropic polypeptide (GIP) have previously been reported in salivary glands. Recent evidence has suggested they might influence postprandial macronutrient metabolism. This study therefore investigated and compared postprandial hormone concentrations in saliva and plasma to determine whether their secretion was influenced by oral food stimuli. In a within-subject randomised cross-over comparison of hormone concentrations in plasma and saliva following a mixed meal, 12 subjects were given two 1708 kJ mixed meals. On one occasion the meal was chewed and swallowed (swallowed meal), on the other it was chewed and expectorated (sham-fed meal). Salivary and plasma levels of immunoreactive insulin, GIP and glucagon-like peptide-1 (GLP-1), total protein, alpha-amylase, glucose and non-esterified fatty acid were measured before and for 90 min following the meals. Saliva total protein and alpha-amylase rose following both meals, indicating that the stimulus for salivary protein release is related to the presence of food in the mouth. GLP-1 was not detected in saliva. Fasting salivary insulin levels were lower in saliva than plasma (28+/-6 vs 40+/-25 pmol/l respectively). Both increased following the swallowed meal but the rise in saliva was slower and less marked than in plasma (peak levels 96+/-18 and 270+/-66 pmol/l for saliva and plasma respectively, P<0.01). Both were unchanged following the sham-fed meal. GIP was detected in saliva. Fasting GIP levels were significantly higher in saliva than plasma (183+/-23 compared with 20+/-7 pmol/l, P<0.01). They decreased in saliva following both swallowed and sham-fed meals to nadirs of 117+/-17 and 71+/-12 pmol/l respectively, but rose following the swallowed meal to peak levels of 268+/-66 pmol/l. These findings are consistent with insulin in saliva being an ultrafiltrate of that circulating in blood, but GIP in saliva being the product of local salivary gland synthesis, whose secretion is influenced, directly or indirectly, by oral stimuli. The function of salivary GIP is unknown, but we speculate that it may play a role in the regulation of gastric acid secretion in the fasting state.
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Huang, Chun-Ming, Justin W. Torpey, Yu-Tseung Liu, Yun-Ru Chen, Katherine E. Williams, Elizabeth A. Komives, and Richard L. Gallo. "A Peptide with a ProGln C Terminus in the Human Saliva Peptidome Exerts Bactericidal Activity against Propionibacterium acnes." Antimicrobial Agents and Chemotherapy 52, no. 5 (February 19, 2008): 1834–36. http://dx.doi.org/10.1128/aac.01347-07.
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ABSTRACT Nine proline-rich peptides ending with a proline-glutamine C terminus in a salivary peptidome were sequenced by matrix-assisted laser desorption ionization time of flight time of flight tandem mass spectrometry. A GPPPQGGRPQ peptide binds gram-positive Propionibacterium acnes and considerably inhibits bacterial growth. The peptide exhibiting innate immunity may be applied for treatment of various P. acnes-associated human diseases.
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Suzuki, Yosuke, Hiroki Itoh, Kohei Amada, Ryota Yamamura, Yuhki Sato, and Masaharu Takeyama. "Significant Increase in Salivary Substance P Level after a Single Oral Dose of Cevimeline in Humans." International Journal of Peptides 2013 (March 24, 2013): 1–6. http://dx.doi.org/10.1155/2013/284765.
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Cevimeline is a novel muscarinic acetylcholine receptor agonist currently being developed as a therapeutic agent for xerostomia. We examined the effects of cevimeline on salivary and plasma levels of substance-P- (SP-), calcitonin-gene-related-peptide- (CGRP-), and vasoactive-intestinal-polypeptide- (VIP-) like immunoreactive substances (ISs) in humans. An open-labeled crossover study was conducted on seven healthy volunteers. Saliva volume was measured, and saliva and venous blood samples were collected before and 30–240 min after a single oral dose of cevimeline or placebo. Salivary and plasma levels of SP-, CGRP-, and VIP-IS were measured using a highly sensitive enzyme immunoassay. A single oral dose of cevimeline resulted in significant increases in salivary but not plasma SP-IS level compared to placebo. Cevimeline administration did not alter the salivary or plasma levels of CGRP-IS or VIP-IS compared to placebo. Significant increases in salivary volume were observed after cevimeline administration compared to placebo. A significant correlation was observed between the total release of SP-IS and that of salivary volume. These findings suggest an association of SP with the enhancement of salivary secretion by cevimeline.
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Stie, Mai Bay, Johan Ring Gätke, Ioannis S. Chronakis, Jette Jacobsen, and Hanne Mørck Nielsen. "Mucoadhesive Electrospun Nanofiber-Based Hybrid System with Controlled and Unidirectional Release of Desmopressin." International Journal of Molecular Sciences 23, no. 3 (January 27, 2022): 1458. http://dx.doi.org/10.3390/ijms23031458.
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The sublingual mucosa is an attractive route for drug delivery, although challenged by a continuous flow of saliva that leads to a loss of drug by swallowing. It is of great benefit that drugs absorbed across the sublingual mucosa avoid exposure to the harsh environment of the gastro-intestinal lumen; this is especially beneficial for drugs of low physicochemical stability such as therapeutic peptides. In this study, a two-layered hybrid drug delivery system was developed for the sublingual delivery of the therapeutic peptide desmopressin. It consisted of peptide-loaded mucoadhesive electrospun chitosan/polyethylene oxide-based nanofibers (mean diameter of 183 ± 20 nm) and a saliva-repelling backing film to promote unidirectional release towards the mucosa. Desmopressin was released from the nanofiber-based hybrid system (approximately 80% of the loaded peptide was released within 45 min) in a unidirectional manner in vitro. Importantly, the nanofiber–film hybrid system protected the peptide from wash-out, as demonstrated in an ex vivo flow retention model with porcine sublingual mucosal tissue. Approximately 90% of the loaded desmopressin was retained at the surface of the ex vivo porcine sublingual mucosa after 15 min of exposure to flow rates representing salivary flow.
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Gorr, Sven-Ulrik, Mahsa Abdolhosseini, Anuradha Shelar, and Julie Sotsky. "Dual host-defence functions of SPLUNC2/PSP and synthetic peptides derived from the protein." Biochemical Society Transactions 39, no. 4 (July 20, 2011): 1028–32. http://dx.doi.org/10.1042/bst0391028.
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PSP (parotid secretory protein)/SPLUNC2 (short palate, lung and nasal epithelium clone 2) is expressed in human salivary glands and saliva. The protein exists as an N-glycosylated and non-glycosylated form and both appear to induce agglutination of bacteria, a major antibacterial function for salivary proteins. Both forms of PSP/SPLUNC2 bind LPS (lipopolysaccharide), suggesting that the protein may also play an anti-inflammatory role. Based on the predicted structure of PSP/SPLUNC2 and the location of known antibacterial and anti-inflammatory peptides in BPI (bactericidal/permeability-increasing protein) and LBP (LPS-binding protein), we designed GL13NH2 and GL13K, synthetic peptides that capture these proposed functions of PSP/SPLUNC2. GL13NH3 agglutinates bacteria, leading to increased clearance by macrophages and reduced spread of infection in a plant model. GL13K kills bacteria with a minimal inhibitory concentration of 5–10 μg/ml, kills bacteria in biofilm and retains activity in 150 mM NaCl and 50% saliva. Both peptides block endotoxin action, but only GL13K appears to bind endotoxin. The peptides do not cause haemolysis, haemagglutination in serum, inhibit mammalian cell proliferation or induce an inflammatory response in macrophages. These results suggest that the GL13NH2 and the modified peptide GL13K capture the biological activity of PSP/SPLUNC2 and can serve as lead compounds for the development of novel antimicrobial and anti-inflammatory peptides.
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LIGTENBERG, Antoon J. M., Floris J. BIKKER, Jolanda M. A. DE BLIECK-HOGERVORST, Enno C. I. VEERMAN, and Arie V. NIEUW AMERONGEN. "Binding of salivary agglutinin to IgA." Biochemical Journal 383, no. 1 (September 24, 2004): 159–64. http://dx.doi.org/10.1042/bj20040265.
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SAG (salivary agglutinin), which is identical to gp-340 (glycoprotein-340) from the lung, is encoded by DMBT1 (deleted in malignant brain tumours 1). It is a member of the SRCR (scavenger receptor cysteine-rich) superfamily and contains 14 SRCR domains, 13 of which are highly similar. SAG in saliva is partially complexed with IgA, which may be necessary for bacterial binding. The goal of the present study was to characterize the binding of purified SAG to IgA. SAG binds to a variety of proteins, including serum and secretory IgA, alkaline phosphatase-conjugated IgGs originating from rabbit, goat, swine and mouse, and lactoferrin and albumin. Binding of IgA to SAG is calcium dependent and is inhibited by 0.5 M KCl, suggesting that electrostatic interactions are involved. Binding of IgA was destroyed after reduction of SAG, suggesting that the protein moiety is involved in binding. To pinpoint further the binding domain for IgA on SAG, a number of consensus-based peptides of the SRCR domains and SRCR interspersed domains were designed and synthesized. ELISA binding studies with IgA indicated that only one of the peptides tested, comprising amino acids 18–33 (QGRVEVLYRGSWGTVC) of the 109-amino-acid SRCR domain, exhibited binding to IgA. This domain is identical to the domain of SAG that is involved in binding to bacteria. Despite this similar binding site, IgA did not inhibit binding of Streptococcus mutans to SAG or peptide. These results show that the binding of IgA to SAG is specifically mediated by a peptide sequence on the SRCR domains.
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Oho, Takahiko, Floris J. Bikker, Arie V. Nieuw Amerongen, and Jasper Groenink. "A Peptide Domain of Bovine Milk Lactoferrin Inhibits the Interaction between Streptococcal Surface Protein Antigen and a Salivary Agglutinin Peptide Domain." Infection and Immunity 72, no. 10 (October 2004): 6181–84. http://dx.doi.org/10.1128/iai.72.10.6181-6184.2004.
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ABSTRACT The peptide domain of salivary agglutinin responsible for its interaction with cell surface protein antigen (PAc) of Streptococcus mutans or bovine lactoferrin was found in the same peptide, scavenger receptor cysteine-rich domain peptide 2 (SRCRP2). Inhibition studies suggest that PAc and lactoferrin, of which residues 480 to 492 seem important, competitively bind to the SRCRP2 domain of salivary agglutinin.
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Niemi, Liza Danielsson, and Ingegerd Johansson. "Salivary Statherin Peptide-Binding Epitopes of Commensal and Potentially Infectious Actinomyces spp. Delineated by a Hybrid Peptide Construct." Infection and Immunity 72, no. 2 (February 2004): 782–87. http://dx.doi.org/10.1128/iai.72.2.782-787.2004.
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ABSTRACT Adhesion of microorganisms to host receptor molecules such as salivary statherin molecules is a common event in oral microbial colonization. Here we used a hybrid peptide construct (with both a hydroxyapatite-binding portion and a test peptide portion) to map the interaction of Actinomyces species (and Candida albicans) with statherin. Adhesion to hybrid peptides and truncated statherin variants revealed three binding types, types I to III. (i) Type I strains of rat, hamster, and human infection origins bound C-terminal-derived QQYTF and PYQPQY peptides. The QQYTF peptide inhibited statherin binding for some strains but not for others. (ii) Type II strains of human and monkey tooth origins bound middle-region-derived YQPVPE and QPLYPQ peptides. Neither strain was inhibited by soluble peptides. (iii) Type III strains of human infection origins (and C. albicans) did not bind to either statherin-derived peptides or truncated statherin. Moreover, the type I strains inhibited by QQYTF were also inhibited by TF and QAATF peptides and were detached from statherin by the same peptides. In conclusion, it is suggested that commensal and potentially infectious microorganisms bind middle or C-terminal statherin differently and that other microbes might require discontinuous epitopes.
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Mathison, R. D., A. D. Befus, and J. S. Davison. "A novel submandibular gland peptide protects against endotoxic and anaphylactic shock." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 273, no. 3 (September 1, 1997): R1017—R1023. http://dx.doi.org/10.1152/ajpregu.1997.273.3.r1017.
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Submandibular glands release peptides and proteins that, through exocrine and endocrine actions, facilitate tissue repair in the oral cavity, gastrointestinal tract, and more distal sites such as liver. It has been shown that salivary gland factors also modulate inflammatory responses, because we found that removal of the submandibular glands increases the hypotensive responses to endotoxin. From this observation we proposed that these glands contain a factor that regulates cardiovascular response to shock. With the use of classical peptide isolation procedures, a heptapeptide (TDIFEGG) called submandibular gland peptide T was identified in rat submandibular glands. A synthetic form of this peptide reduced endotoxic shock in sialadenectomized rats by 50% at doses as low as 1 microgram/kg and prevented allergen-induced hypotension by 90% in rats with intact salivary glands at a dose of 100 micrograms/kg. This novel peptide is probably generated from a prohormone, submandibular gland rat 1 protein, a product of the VCSA1 gene. These data indicate that submandibular glands participate in the regulation of systemic homeostasis.
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Londono-Renteria, Berlin, Papa M. Drame, Jehidys Montiel, Ana M. Vasquez, Alberto Tobón-Castaño, Marissa Taylor, Lucrecia Vizcaino, and Audrey E. Lenhart. "Identification and Pilot Evaluation of Salivary Peptides from Anopheles albimanus as Biomarkers for Bite Exposure and Malaria Infection in Colombia." International Journal of Molecular Sciences 21, no. 3 (January 21, 2020): 691. http://dx.doi.org/10.3390/ijms21030691.
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Insect saliva induces significant antibody responses associated with the intensity of exposure to bites and the risk of disease in humans. Several salivary biomarkers have been characterized to determine exposure intensity to Old World Anopheles mosquito species. However, new tools are needed to quantify the intensity of human exposure to Anopheles bites and understand the risk of malaria in low-transmission areas in the Americas. To address this need, we conducted proteomic and bioinformatic analyses of immunogenic candidate proteins present in the saliva of uninfected Anopheles albimanus from two separate colonies—one originating from Central America (STECLA strain) and one originating from South America (Cartagena strain). A ~65 kDa band was identified by IgG antibodies in serum samples from healthy volunteers living in a malaria endemic area in Colombia, and a total of five peptides were designed from the sequences of two immunogenic candidate proteins that were shared by both strains. ELISA-based testing of human IgG antibody levels against the peptides revealed that the transferrin-derived peptides, TRANS-P1, TRANS-P2 and a salivary peroxidase peptide (PEROX-P3) were able to distinguish between malaria-infected and uninfected groups. Interestingly, IgG antibody levels against PEROX-P3 were significantly lower in people that have never experienced malaria, suggesting that it may be a good marker for mosquito bite exposure in naïve populations such as travelers and deployed military personnel. In addition, the strength of the differences in the IgG levels against the peptides varied according to location, suggesting that the peptides may able to detect differences in intensities of bite exposure according to the mosquito population density. Thus, the An. albimanus salivary peptides TRANS-P1, TRANS-P2, and PEROX-P3 are promising biomarkers that could be exploited in a quantitative immunoassay for determination of human-vector contact and calculation of disease risk.
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Jeandel, L., E. Morrier, and S. Heisler. "Atrial natriuretic peptide stimulates submandibular gland synthesis and secretion of cGMP." American Journal of Physiology-Endocrinology and Metabolism 257, no. 5 (November 1, 1989): E675—E680. http://dx.doi.org/10.1152/ajpendo.1989.257.5.e675.
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Binding of atrial natriuretic peptide (ANP) to rat submandibular gland and its effect on guanosine 3',5'-cyclic monophosphate (cGMP) formation and salivary secretion were investigated. Membranes rapidly and specifically bound 125I-ANP. Binding was inhibited by unlabeled ANP (IC50 approximately 1.6 nM), but not by atriopeptin I, other COOH- and NH2-terminal deleted ANP fragments, or agents such as pilocarpine or substance P. Scatchard analysis revealed a single class of high-affinity sites (dissociation constant 0.74 +/- 0.25 nM; maximal binding capacity 20.5 +/- 6.3 pmol/mg protein). Intravenous infusion of ANP with pilocarpine caused a significant dose-dependent increase in the levels of cGMP detected in plasma and saliva. Because salivary cGMP may have originated in plasma, the effect of ANP on cGMP formation was evaluated in dispersed cells. ANP evoked a concentration-dependent increase in both cGMP synthesis and secretion (EC50 approximately 1.7 x 10(-8) M). The atrial peptide did affect basal or l-isoproterenol-stimulated adenosine 3',5'-cyclic monophosphate synthesis in dispersed cells. When infused by itself and/or with pilocarpine, ANP did not alter the rate of spontaneous or pilocarpine-induced salivary flow, secretion of chloride, or protein release. The data demonstrate the presence of guanylate cyclase-coupled ANP receptors in submandibular gland; the atrial peptide, however, does not exert an effect of the secretory function of the gland.
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Valenzuela, Jesus G., Ivo M. B. Francischetti, Van My Pham, Mark K. Garfield, Thomas N. Mather, and José M. C. Ribeiro. "Exploring the sialome of the tick Ixodes scapularis." Journal of Experimental Biology 205, no. 18 (September 15, 2002): 2843–64. http://dx.doi.org/10.1242/jeb.205.18.2843.
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SUMMARY To attempt description of the set of mRNA and protein (sialome) expressed in the salivary glands of the tick Ixodes scapularis, we randomly sequenced 735 clones of a full-length salivary gland cDNA library of this arthropod and performed Edman degradation of protein bands from salivary gland homogenates (SGH) and saliva separated by SDS-PAGE. The sequences were grouped into 410 clusters, of which 383 are not associated with known I. scapularis sequences. 15- and 17-protein bands from PAGE yielded amino-terminal information on the saliva and salivary gland gels,respectively. We attributed 19 of these sequences to translation products of the cDNA library. Full-length sequences were obtained for 87 clones. Among these protein sequences are several protease inhibitors of distinct classes,metalloproteases, novel proteins with histamine-binding domains, and several peptide families of unknown function displaying different conserved cysteine residues, many of which contain single Kunitz domains. This work provides information into the diversity of messages expressed in the salivary glands of I. scapularis, describes novel sequences that may be responsible for known biological activites, indicates further biological activities that may be present in I. scapularis saliva and identifies novel vaccine targets that may be used in Lyme disease prevention.
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Dai, Chaobin, Bin Zhang, Yunyang Liao, Qicai Liu, Feiguang Wu, Xiaoting Lv, Kai Zeng, and Xiaofeng Zhu. "CALCB rs3829222 T/T Genotype and Low Expression of CALCB Are High-Risk Factors for Adenoid Cystic Carcinoma of Salivary Gland." Disease Markers 2021 (June 12, 2021): 1–5. http://dx.doi.org/10.1155/2021/5546858.
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Objectives. To investigate the relationship between polymorphisms of calcitonin-related peptide gene II (beta-calcitonin gene-related peptide (βCGRP), CALCB) and serum CGRP levels in salivary adenoid cystic carcinoma. Materials and Methods. Using the polymerase chain reaction (PCR) technique, the full-length amplification and genotype analysis of CALCB genes were performed in 39 patients with adenoid cystic carcinoma of salivary gland and 158 normal controls. The gene frequencies of major genotype of CALCB in adenoid cystic carcinoma of salivary gland and normal control group were analyzed. Enzyme-linked immunosorbent assay (ELISA) was used to evaluate serum calcitonin gene-related peptide (CGRP) and its concentration of alpha and beta subtypes. Results. Univariate logistic regression analysis showed that the CALCB rs2839222 T/T genotype was closely related to the occurrence of salivary adenoid cystic carcinoma, with a correlation coefficient of 3.89. Conclusions. The serum CGRP concentration in the salivary adenoid cystic carcinoma group was 1.56 times that of the normal control group. The αCGRP subtype was significant, which was 3.02 times that of the normal control. The polymorphism of βCGRP gene is associated with genetic susceptibility to salivary adenoid cystic carcinoma, and serum CGRP and βCGRP can be used as novel markers of salivary adenoid cystic carcinoma.
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Alkhateeb, Alaa A., Lloyd A. Mancl, Richard B. Presland, Marilynn L. Rothen, and Donald L. Chi. "Unstimulated Saliva-Related Caries Risk Factors in Individuals with Cystic Fibrosis: A Cross-Sectional Analysis of Unstimulated Salivary Flow, pH, and Buffering Capacity." Caries Research 51, no. 1 (November 16, 2016): 1–6. http://dx.doi.org/10.1159/000450658.
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Salivary flow rate, pH, and buffering capacity are associated with dental caries, but studies from the cystic fibrosis (CF) literature are inconclusive regarding these salivary factors and caries. The aim of this study was to evaluate these factors and their associations with dental caries in individuals with CF. Unstimulated whole saliva was collected from individuals aged 6-20 years at Seattle Children's Hospital CF Clinic, USA (n = 83). Salivary flow rate was measured in milliliters per minute. Salivary pH was assessed using a laboratory pH meter. Buffering capacity was assessed by titration with HCl. The outcome measure was caries prevalence, defined as the number of decayed, missing, or filled primary and permanent tooth surfaces. Spearman's rank correlation coefficient and the t test were used to test for bivariate associations. Multiple variable linear regression models were used to (1) run confounder-adjusted analyses and (2) assess for potential interactions. There was no significant association between salivary flow rate or buffering capacity and caries prevalence. There was a significant negative association between salivary pH and caries prevalence, but this association was no longer significant after adjusting for age. There was no significant interaction between salivary flow rate and buffering capacity or between antibiotic use and the 3 salivary factors. Our results indicate that unstimulated salivary factors are not associated with dental caries prevalence in individuals with CF. Future studies should investigate other potential saliva-related caries risk factors in individuals with CF such as cariogenic bacteria levels, salivary host defense peptide levels, and medication use.
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Rittschof, D., C. M. Kratt, and A. S. Clare. "Gastropod predation sites: the role of predator and prey in chemical attraction of the hermit crab Clibanarius vittatus." Journal of the Marine Biological Association of the United Kingdom 70, no. 3 (August 1990): 583–96. http://dx.doi.org/10.1017/s0025315400036602.
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Gastropod shells are essential to most hermit crabs. Shell availability limits hermit crab populations. Shells provide protection and the degree of shell-fit controls crab growth and fecundity. Crabs locate new gastropod shells from a distance under water by molecules released from gastropod flesh during predation events. Here we test the hypothesis that the salivary glands of the predatory gastropod are the source of enzymes that digest muscle proteins and release peptide attractants. We describe the anatomy of both the acinous salivary glands and the tubular accessory salivary glands of Busycon contrarium which are similar to those of B. carica. The salivary gland ducts empty at the mouth, suggesting a role in the primary digestion of food. We show that gastropod muscle proteins, extracted by salt solutions with the ionic strength of sea water and purified by precipitation in low ionic strength can be digested by gastropod salivary gland enzymes to generate peptides attractive to the hermit crab, Clibanarius vittatus, in field assays.
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Ahmed, Araz, Alessandro Gulino, Simita Amayo, Walter Arancio, Ada Maria Florena, Beatrice Belmonte, Abdo Jurjus, Angelo Leone, and Isabelle Miletich. "Natriuretic peptide system expression in murine and human submandibular salivary glands: a study of the spatial localisation of ANB, BNP, CNP and their receptors." Journal of Molecular Histology 51, no. 1 (November 13, 2019): 3–13. http://dx.doi.org/10.1007/s10735-019-09849-5.
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Abstract The natriuretic peptide (NP) system comprises of three ligands, the Atrial Natriuretic Peptide (ANP), Brain Natriuretic peptide (BNP) and C-type Natriuretic peptide (CNP), and three natriuretic peptide receptors, NPRA, NPRB and NPRC. Here we present a comprehensive study of the natriuretic peptide system in healthy murine and human submandibular salivary glands (SMGs). We show CNP is the dominant NP in mouse and human SMG and is expressed together with NP receptors in ducts, autonomic nerves and the microvasculature of the gland, suggesting CNP autocrine signalling may take place in some of these glandular structures. These data suggest the NP system may control salivary gland function during homeostasis through the regulation of electrolyte re-absorption, neural stimulation and/or blood vessel wall contraction/relaxation. We also show abnormal expression of NPRA in the stroma of a subset of human SMGs resected from patients diagnosed with oral squamous cell carcinoma (OSCC) of non-salivary gland origin. This finding warrants further research to investigate a possible correlation between early OSCC invasion and NPRA overexpression.
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Belstrøm, Daniel, Rosa R. Jersie-Christensen, David Lyon, Christian Damgaard, Lars J. Jensen, Palle Holmstrup, and Jesper V. Olsen. "Metaproteomics of saliva identifies human protein markers specific for individuals with periodontitis and dental caries compared to orally healthy controls." PeerJ 4 (September 14, 2016): e2433. http://dx.doi.org/10.7717/peerj.2433.
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BackgroundThe composition of the salivary microbiota has been reported to differentiate between patients with periodontitis, dental caries and orally healthy individuals. To identify characteristics of diseased and healthy saliva we thus wanted to compare saliva metaproteomes from patients with periodontitis and dental caries to healthy individuals.MethodsStimulated saliva samples were collected from 10 patients with periodontitis, 10 patients with dental caries and 10 orally healthy individuals. The proteins in the saliva samples were subjected to denaturing buffer and digested enzymatically with LysC and trypsin. The resulting peptide mixtures were cleaned up by solid-phase extraction and separated online with 2 h gradients by nano-scale C18reversed-phase chromatography connected to a mass spectrometer through an electrospray source. The eluting peptides were analyzed on a tandem mass spectrometer operated in data-dependent acquisition mode.ResultsWe identified a total of 35,664 unique peptides from 4,161 different proteins, of which 1,946 and 2,090 were of bacterial and human origin, respectively. The human protein profiles displayed significant overexpression of the complement system and inflammatory markers in periodontitis and dental caries compared to healthy controls. Bacterial proteome profiles and functional annotation were very similar in health and disease.ConclusionsOverexpression of proteins related to the complement system and inflammation seems to correlate with oral disease status. Similar bacterial proteomes in healthy and diseased individuals suggests that the salivary microbiota predominantly thrives in a planktonic state expressing no disease-associated characteristics of metabolic activity.
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Helmerhorst, Eva J., Ingrid M. Reijnders, Wim van ’t Hof, Ina Simoons-Smit, Enno C. I. Veerman, and Arie V. Nieuw Amerongen. "Amphotericin B- and Fluconazole-ResistantCandida spp., Aspergillus fumigatus, and Other Newly Emerging Pathogenic Fungi Are Susceptible to Basic Antifungal Peptides." Antimicrobial Agents and Chemotherapy 43, no. 3 (March 1, 1999): 702–4. http://dx.doi.org/10.1128/aac.43.3.702.
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ABSTRACT The present study shows that a number of basic antifungal peptides, including human salivary histatin 5, a designed histatin analog designated dhvar4, and a peptide from frog skin, PGLa, are active against amphotericin B-resistant Candida albicans,Candida krusei, and Aspergillus fumigatusstrains and against a fluconazole-resistant Candida glabrata isolate.
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Ghamari, Mahboob, Vahid Hosseininaveh, Ali Darvishzadeh, and Khalil Talebi. "Biochemical characterisation of the tissue degrading enzyme, collagenase, in the spined soldier bug, Podisus maculiventris (Hemiptera: Pentatomidae)." Journal of Plant Protection Research 54, no. 2 (July 8, 2014): 164–70. http://dx.doi.org/10.2478/jppr-2014-0026.
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Abstract Podisus maculiventris (Say) is a generalist predator attacking many insect species from different orders. The bug injects saliva into its prey's body. The ingested hemolymph and liquefied internal tissues pass through the bug's alimentary tract. Collagenase working on peptide bonds of collagen and basement membrane proteins, leads to the disintegration of the prey's internal organs. As yet, there is an almost complete lack of knowledge on the collagenase activity in P. maculiventris. The collagenase activity of the salivary glands and midgut was optimum at pH 8.0 which was congruent with the optimal pH of the total proteolytic activity of the salivary glands. More collagenolytic activity was determined in the posterior lobe of the salivary glands and anterior midgut. Significant inhibition of collagenolytic activity by ethylenediaminetetraacetic acid (EDTA) revealed the enzyme is a metalloproteinase. The collagenase activity notably decreased when the bug went hungry. The salivary gland collagenase is a vital enzyme in extra-oral digestion and facilitates the action of other digestive enzymes. The midgut collagenase may be involved in the digestion of the ingested muscle fibers. The collagenase probably acts as an intoxicating agent in the saliva (venom) of P. maculiventris. Paralysing toxins are present in the salivary gland secretion.
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Gohel, Vishal, Judith A. Jones, and Carolyn J. Wehler. "Salivary biomarkers and cardiovascular disease: a systematic review." Clinical Chemistry and Laboratory Medicine (CCLM) 56, no. 9 (August 28, 2018): 1432–42. http://dx.doi.org/10.1515/cclm-2017-1018.
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Abstract Background: The purpose of this systematic review is to summarize the literature examining associations between salivary biomarkers and cardiovascular disease (CVD) status. Contents: An advanced search was conducted using MeSH terms related to salivary biomarkers and CVD, and entered into the PubMed, Web of Science, and Google Scholar search databases. Four hundred and thirty-three records were narrowed to 22 accepted articles. Included titles were assessed for quality using the Newcastle-Ottawa scale, and ranked into categories of low, moderate, or high. Summary: A total of 40 salivary biomarkers were analyzed among accepted articles. The most studied markers were salivary creatine kinase isoform MB, C-reactive protein (CRP), matrix metalloproteinase-9, troponin I, myeloperoxidase, myoglobin, and brain natriuretic peptide. Salivary CRP provided the most consistent trends. Statistically significant increases of salivary CRP were present with CVD in every study that analyzed it. The remaining six markers demonstrated varying patterns. Outlook: Existing studies provide insufficient data to draw definitive conclusions. Current research shows that there is an association between some salivary biomarkers and CVD, but the details of existing studies are conflicting. Despite inconclusive results, the diagnostic potential of saliva shows promise as a non-invasive means of cardiovascular risk assessment.
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Armistead, Jennifer S., Iain B. H. Wilson, Toin H. van Kuppevelt, and Rhoel R. Dinglasan. "A role for heparan sulfate proteoglycans in Plasmodium falciparum sporozoite invasion of anopheline mosquito salivary glands." Biochemical Journal 438, no. 3 (August 26, 2011): 475–83. http://dx.doi.org/10.1042/bj20110694.
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HS (heparan sulfate) has been shown to be an important mediator of Plasmodium sporozoite homing and invasion of the liver, but the role of this glycosaminoglycan in mosquito vector host–sporozoite interactions is unknown. We have biochemically characterized the function of AgOXT1 (Anopheles gambiae peptide-O-xylosyltransferase 1) and confirmed that AgOXT1 can modify peptides representing model HS and chondroitin sulfate proteoglycans in vitro. Moreover, we also demonstrated that the mosquito salivary gland basal lamina proteoglycans are modified by HS. We used RNA interference-mediated knockdown of HS biosynthesis in A. gambiae salivary glands to determine whether Plasmodium falciparum sporozoites that are released from mosquito midgut oocysts use salivary gland HS as a receptor for tissue invasion. Our results suggest that salivary gland basal lamina HS glycosaminoglycans only partially mediate midgut sporozoite invasion of this tissue, and that in the absence of HS, the presence of other surface co-receptors is sufficient to facilitate parasite entry.
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Sekine, Shinichi, Kosuke Kataoka, Muneo Tanaka, Hideki Nagata, Toru Kawakami, Kenichi Akaji, Saburo Aimoto, and Satoshi Shizukuishi. "Active domains of salivary statherin on apatitic surfaces for binding to Fusobacterium nucleatum cells." Microbiology 150, no. 7 (July 1, 2004): 2373–79. http://dx.doi.org/10.1099/mic.0.27107-0.
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Fusobacterium nucleatum can bind to saliva-coated tooth surfaces. However, the nature of the domains of salivary protein that interact with F. nucleatum remains unclear. The ability of individual proteins in human submandibular-sublingual saliva (HSMSL) to bind F. nucleatum cells was examined by dot blot assay; statherin displayed the strongest binding activity. Statherin binding sites were determined based on binding of 125I-labelled F. nucleatum to statherin-coated hydroxyapatite (sHAP) beads via inhibition assays using synthetic analogous peptide fragments of whole statherin. Analogous peptides corresponding to residues 19–26 and 32–39 of statherin inhibited binding by 77 % and 68 %, respectively. Synthetic peptides were also prepared by serial deletions of individual residues from N- and C-termini of the peptides GPYQPVPE (aa 19–26) and QPYQPQYQ (aa 32–39). The inhibitory effects of peptides YQPVPE (aa 21–26) and PYQPQYQ (aa 33–39) were very similar to those of GPYQPVPE and QPYQPQYQ, respectively. However, additional deletion of residues resulted in significant reduction of the inhibitory effect. Alanine-scan analysis of YQPVPE revealed that all tested peptides retained inhibitory activity; only YAPVPE exhibited significantly decreased inhibitory activity. These findings suggest that YQPVPE and PYQPQYQ may represent the minimal active segments of statherin for binding to F. nucleatum; moreover, Gln may be a key amino acid in the active segment.
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Floden, Angela M., Mona Sohrabi, Suba Nookala, Jay J. Cao, and Colin K. Combs. "Salivary Aβ Secretion and Altered Oral Microbiome in Mouse Models of AD." Current Alzheimer Research 17, no. 12 (February 22, 2021): 1133–44. http://dx.doi.org/10.2174/1567205018666210119151952.
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Background: Beta amyloid (Aβ) peptide containing plaque aggregations in the brain are a hallmark of Alzheimer’s Disease (AD). However, Aβ is produced by cell types outside of the brain suggesting that the peptide may serve a broad physiologic purpose. Objective: Based upon our prior work documenting expression of amyloid β precursor protein (APP) in intestinal epithelium we hypothesized that salivary epithelium might also express APP and be a source of Aβ. Methods: To begin testing this idea, we compared human age-matched control and AD salivary glands to C57BL/6 wild type, AppNL-G-F , and APP/PS1 mice. Results: Both male and female AD, AppNL-G-F , and APP/PS1 glands demonstrated robust APP and Aβ immunoreactivity. Female AppNL-G-F mice had significantly higher levels of pilocarpine stimulated Aβ 1-42 compared to both wild type and APP/PS1 mice. No differences in male salivary Aβ levels were detected. No significant differences in total pilocarpine stimulated saliva volumes were observed in any group. Both male and female AppNL-G-F but not APP/PS1 mice demonstrated significant differences in oral microbiome phylum and genus abundance compared to wild type mice. Male, but not female, APP/PS1 and AppNL-G-F mice had significantly thinner molar enamel compared to their wild type counterparts. Conclusion: These data support the idea that oral microbiome changes exist during AD in addition to changes in salivary Aβ and oral health.
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Ryan, J., T. Mantle, S. McQuaid, and D. C. Costigan. "Salivary insulin-like growth factor-I originates from local synthesis." Journal of Endocrinology 135, no. 1 (October 1992): 85—NP. http://dx.doi.org/10.1677/joe.0.1350085.
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ABSTRACT Insulin-like growth factor-I (IGF-I) is a GH-dependent growth factor found in its highest concentrations in plasma. It is also measurable in saliva. The origins of salivary IGF-I concentrations were studied. Intracardial administration of Sprague–Dawley rats with 125I-labelled IGF-I and subsequent analysis of plasma and saliva samples by exclusion gel chromatography and SDS-PAGE, followed by autoradiography, demonstrated the apparent inability of IGF-I to cross from the plasma pool through to saliva. 125I-Labelled IGF-I was not chromatographed immediately before injection, resulting in administration of free iodide along with the iodinated peptide. This free iodide was demonstrable in saliva, indicating that movement of substances from plasma to saliva was measurable using the levels of 125I activity administered. Free iodide in saliva was not contributed to by 125I-labelled IGF-I degradation since 125I-labelled IGF-I was shown to be stable in saliva over 24 h. These data indicated that IGF-I in saliva is produced locally. Identification of a 4·7 kb IGF-I mRNA transcript in rat parotid salivary gland was consistent with IGF-I synthesis within that tissue. Journal of Endocrinology (1992) 135, 85–90