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1
Liang, Yifan, Shin-ichi Ikeda, Junhan Chen, Yan Zhang, Kazuno Negishi, Kazuo Tsubota, and Toshihide Kurihara. "Myopia Is Suppressed by Digested Lactoferrin or Holo-Lactoferrin Administration." International Journal of Molecular Sciences 24, no. 6 (March 18, 2023): 5815. http://dx.doi.org/10.3390/ijms24065815.
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Myopia is becoming a leading cause of vision impairment. An effective intervention is needed. Lactoferrin (LF) is a protein that has been reported to inhibit myopia progression when taken orally. This study looked at the effects of different forms of LF, such as native LF and digested LF, on myopia in mice. Mice were given different forms of LF from 3 weeks of age, and myopia was induced with minus lenses from 4 weeks of age. Results showed that mice given digested LF or holo-LF had a less elongated axial length and thinned choroid, compared to those given native-LF. Gene expression analysis also showed that the groups given native-LF and its derivatives had lower levels of certain cytokines and growth factors associated with myopia. These results suggest that myopia can be more effectively suppressed by digested LF or holo-LF than native-LF.
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León-Sicairos, Nidia, Magda Reyes-López, Cynthia Ordaz-Pichardo, and Mireya de la Garza. "Microbicidal action of lactoferrin and lactoferricin and their synergistic effect with metronidazole inEntamoeba histolyticaThis paper is one of a selection of papers published in this Special Issue, entitled 7th International Conference on Lactoferrin: Structure, Function, and Applications, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 3 (June 2006): 327–36. http://dx.doi.org/10.1139/o06-060.
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Lactoferrin (Lf), in its iron-free form, has been shown to inhibit the growth of pathogenic microorganisms. In the light of new agents to control amoebiasis, the microbicidal activity of human and bovine Lf and bovine lactoferricin (bLfcin, fragment 4–14), and of each combined with metronidazole, the main drug used in amoebiasis, was evaluated in trophozoites of Entamoeba histolytica. Both lactoferrins and bLfcin were able to kill amoebas in a concentration-dependent manner. This killing effect was modulated according to the culture age, pH, and temperature. Parasites obtained from the stationary phase were more susceptible to Lf than those from the early exponential phase. The effect of Lf and its derived peptide, bLfcin, was prevented by both Fe2+and Fe3+. However, the divalent cations Mg2+and Ca2+prevented the killing effect of Lf but not of bLfcin. A synergistic amoebicidal effect was found between metronidazole and human Lf, bovine Lf, or bLfcin. These data suggest that Lf and bLfcin might be used in amoebiasis if they are administered with a low dose of metronidazole to diminish the toxicity of this drug. Thus, Lf and bLfcin are therapeutically potential candidates for use as antiamoebics in patients.
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Hoek, K. S., J. M. Milne, P. A. Grieve, D. A. Dionysius, and R. Smith. "Antibacterial activity in bovine lactoferrin-derived peptides." Antimicrobial Agents and Chemotherapy 41, no. 1 (January 1997): 54–59. http://dx.doi.org/10.1128/aac.41.1.54.
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Several peptides sharing high sequence homology with lactoferricin B (Lf-cin B) were generated from bovine lactoferrin (Lf) with recombinant chymosin. Two peptides were copurified, one identical to Lf-cin B and another differing from Lf-cin B by the inclusion of a C-terminal alanine (lactoferricin). Two other peptides were copurified from chymosin-hydrolyzed Lf, one differing from Lf-cin B by the inclusion of C-terminal alanyl-leucine and the other being a heterodimer linked by a disulfide bond. These peptides were isolated in a single step from chymosin-hydrolyzed Lf by membrane ion-exchange chromatography and were purified by reverse-phase high-pressure liquid chromatography (HPLC). They were characterized by N-terminal Edman sequencing, mass spectrometry, and antibacterial activity determination. Pure lactoferricin, prepared from pepsin-hydrolyzed Lf, was purified by standard chromatography techniques. This peptide was analyzed against a number of gram-positive and gram-negative bacteria before and after reduction of its disulfide bond or cleavage after its single methionine residue and was found to inhibit the growth of all the test bacteria at a concentration of 8 microM or less. Subfragments of lactoferricin were isolated from reduced and cleaved peptide by reverse-phase HPLC. Subfragment 1 (residues 1 to 10) was active against most of the test microorganisms at concentrations of 10 to 50 microM. Subfragment 2 (residues 11 to 26) was active against only a few microorganisms at concentrations up to 100 microM. These antibacterial studies indicate that the activity of lactoferricin is mainly, but not wholly, due to its N-terminal region.
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Takakura, Natsuko, Hiroyuki Wakabayashi, Hiroko Ishibashi, Susumu Teraguchi, Yoshitaka Tamura, Hideyo Yamaguchi, and Shigeru Abe. "Oral Lactoferrin Treatment of Experimental Oral Candidiasis in Mice." Antimicrobial Agents and Chemotherapy 47, no. 8 (August 2003): 2619–23. http://dx.doi.org/10.1128/aac.47.8.2619-2623.2003.
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ABSTRACT We assessed the potential of lactoferrin (LF), a multifunctional milk protein, for treatment of oral candidiasis with immunosuppressed mice, which have local symptoms characteristic of oral thrush. Oral administration of bovine LF in drinking water starting 1 day before the infection significantly reduced the number of Candida albicans in the oral cavity and the score of lesions on the tongue on day 7 after the inoculation. The symptomatic effect of LF was confirmed by macroscopic and microscopic observations of the tongue's surface. Similar effects were also observed upon administration of LF pepsin hydrolysate, but not lactoferricin B, an antimicrobial peptide of LF. The anticandidal activity of LF was evident on administration either in drinking water or by intragastric intubation with a stomach tube. These results suggest that the effect of LF in this oral candidiasis model is not due to direct antifungal action. In conclusion, LF could have potential as a food component supporting antifungal drug treatment.
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Caccavo, Domenico, Antonella Afeltra, Salvatore Pece, Giuseppe Giuliani, Marina Freudenberg, Chris Galanos, and Emilio Jirillo. "Lactoferrin-Lipid A-Lipopolysaccharide Interaction: Inhibition by Anti-Human Lactoferrin Monoclonal Antibody AGM 10.14." Infection and Immunity 67, no. 9 (September 1, 1999): 4668–72. http://dx.doi.org/10.1128/iai.67.9.4668-4672.1999.
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ABSTRACT Lactoferrin (LF) is a glycoprotein that exerts both bacteriostatic and bactericidal activities. The interaction of LF with lipopolysaccharide (LPS) of gram-negative bacteria seems to play a crucial role in the bactericidal effect. In this study, we evaluated, by means of an enzyme-linked immunosorbent assay, the binding of biotinylated LF to the S (smooth) and R (rough) (Ra, Rb, Rc, Rd1, Rd2, and Re) forms of LPS and different lipid A preparations. In addition, the effects of two monoclonal antibodies (AGM 10.14, an immunoglobulin G1 [IgG1] antibody, and AGM 2.29, an IgG2b antibody), directed against spatially distant epitopes of human LF, on the LF-lipid A or LF-LPS interaction were evaluated. The results showed that biotinylated LF specifically binds to solid-phase lipid A, as this interaction was prevented in a dose-dependent fashion by either soluble uncoupled LF or lipid A. The binding of LF to S-form LPS was markedly weaker than that to lipid A. Moreover, the rate of LF binding to R-form LPS was inversely related to core length. The results suggest that the polysaccharide O chain as well as oligosaccharide core structures may interfere with the LF-lipid A interaction. In addition, we found that soluble lipid A also inhibited LF binding to immobilized LPS, demonstrating that, in the whole LPS structure, the lipid A region contains the major determinant recognized by LF. AGM 10.14 inhibited LF binding to lipid A and LPS in a dose-dependent fashion, indicating that this monoclonal antibody recognizes an epitope involved in the binding of LF to lipid A or some epitope in its close vicinity. In contrast, AGM 2.29, even in a molar excess, did not prevent the binding of LF to lipid A or LPS. Therefore, AGM 10.14 may represent a useful tool for neutralizing selectively the binding of LF to lipid A. In addition, the use of such a monoclonal antibody could allow better elucidation of the consequences of the LF-lipid A interaction.
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Miyazawa, K., C. Mantel, L. Lu, D. C. Morrison, and H. E. Broxmeyer. "Lactoferrin-lipopolysaccharide interactions. Effect on lactoferrin binding to monocyte/macrophage-differentiated HL-60 cells." Journal of Immunology 146, no. 2 (January 15, 1991): 723–29. http://dx.doi.org/10.4049/jimmunol.146.2.723.
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Abstract Lactoferrin (LF) has been implicated in a number of functions including the negative regulation of myelopoiesis in vitro and in vivo, an effect mediated by suppression of cytokine release from monocytes/macrophages. This suppression is abrogated by bacterial LPS. In the present study, HL-60 cells were induced to differentiate to monocytes/macrophages by 12-O-tetradecanoyl phorbol-13-acetate, and LF-binding assays were performed. After differentiation, HL-60 cells showed a twofold increase of LF-binding sites with no difference in the specificity or affinity of LF between pre- and post-differentiated cells. CD11a, CD11b, and CD11c Ag, which have been associated with specific binding sites for LPS on monocytes/macrophages, were also increased three- to fourfold after differentiation. With the use of this system, the effect of LPS on LF binding was studied. At 37 degrees C, LPS enhanced LF binding on HL-60 cells, especially after differentiation. Conversely, at 4 degrees C, LPS inhibited LF binding. There was little effect of temperature on LF binding in the absence of LPS. In the presence of polymyxin B sulfate, the enhanced LF binding by LPS was abrogated. Also, pretreatment with mAbCD11 and/or mAb5D3, which are associated with or directed against candidate LPS receptors, reduced LF binding. Cross-linking studies using an iodinated, photoactivatable LPS derivative ([125I]ASD-LPS) demonstrated directly the specific binding of LPS to LF. These data indicate a dichotomous nature of LF binding on monocyte/macrophage-differentiated HL-60 cells--one being mediated by specific LF receptors whereas the other is apparently mainly via LPS receptors after formation of an LF-LPS complex. These interactions, for which a model is proposed, help to explain the mechanism behind LPS abrogation of the myelopoietic suppressive effects of LF, and a situation that probably occurs during bacterial infection.
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Lopez, Veronica, Shannon L. Kelleher, and Bo Lönnerdal. "Lactoferrin receptor mediates apo- but not holo-lactoferrin internalization via clathrin-mediated endocytosis in trophoblasts." Biochemical Journal 411, no. 2 (March 27, 2008): 271–78. http://dx.doi.org/10.1042/bj20070393.
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LfR [Lf (lactoferrin) receptor] is expressed in most mammalian tissues, including placental trophoblasts, and is presumed to mediate the internalization of Lf. However, the physiological significance of trophoblast LfR is not understood. Using the CT (cytotrophoblast) cell model BeWo, we demonstrated that transfection with LfR siRNA (small interfering RNA) significantly decreased apo- but not holo-Lf uptake compared with mock-transfected controls and that apo- but not holo-Lf significantly increased MMP (matrix metalloproteinase)-2 activity. As Lf functionality is related to the presence (holo-Lf) or absence (apo-Lf) of iron within the Lf molecule, our results suggest that apo-Lf may play a role in cellular invasion. Moreover, we detected LfR (∼105 kDa) in association with the plasma membrane, and ligand blotting confirmed that Lf binds to a LfR of ∼105 kDa. Apo-Lf treatment significantly increased LfR abundance at the plasma membrane and internalization probably occurs via clathrin-mediated endocytosis through early and recycling endosomes, as LfR was co-localized with EEA1 (early endosome antigen 1) and TfR (transferrin receptor) using confocal microscopy, and hypertonic medium (0.4 M sucrose) significantly inhibited apo-Lf internalization. In summary, our data demonstrate that apo- but not holo-Lf is internalized by LfR and suggest that, following internalization via LfR, apo-Lf plays a role in CT invasiveness by inducing MMP-2 activity. Moreover, LfR facilitates apo-Lf uptake specifically through clathrin-mediated endocytosis into early endosomes and potentially into a recycling pathway. Taken together, our data provide a new dimension in understanding ligand-dependant function that may be directly related to the ability of LfR to selectively internalize apo- but not holo-Lf.
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Drozhzhyna, G. I., and T. A. Veliksar. "Lactoferrin: Invisible Eye Defender." International scientific-practical journal Ophthalmology, no. 1 (12) (2021): 73–84. http://dx.doi.org/10.30702/ophthalmology31032021-12.1.73-84/048.8.
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The main protective proteins that are synthesized by eye cells are lactoferrin (Lf), lysozyme, immunoglobulin-A, and tear lipocalins. It has been proven that Lf is contained in biological fluids and mucous membranes of various organs; this highlights the importance of this protein in the first line of defense from pathogenic microorganisms. Lf is a non-heme iron-binding chelating glycoprotein from the transferrin family. Lf carries out bactericidal, fungicidal, antiviral, antioxidant and transport functions, prevents the formation of free radicals, inhibits lipid peroxidation, activates enzymes of the antioxidant system. Lf is contained in tears in the highest concentration (about 2 mg/ml, 25% of tear proteins), the average concentration is 1.42 mg/ml. Lf is an important component providing homeostasis of the ocular surface, modulates the activity of T-lymphocytes and macrophages in infections, prevents the multiplication of pathogenic microflora, the development of inflammation, protects the integrity of the cornea, promotes healing from microtraumas, controls the level of iron in the lacrimal fluid, and protects against toxins. These properties of Lf open up prospects for its application in the treatment of chronic diseases of the ocular surface and, in particular, dry eye disease. Lf concentration in tears decreases during sleep, with age, in dry eye disease, keratitis and conjunctivitis, when using contact lenses, that increase the risk of developing eye infections. The first results of the application of ophthalmic drops Lacto (NOVAX® PHARMA) showed good tolerance and therapeutic efficacy in the treatment of inflammatory diseases of the ocular surface. Keywords: lactoferrin, tear, antimicrobial, immunomodulatory, anti-inflammatory properties, ocular surface.
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Icriverzi, Madalina, Valentina Dinca, Magdalena Moisei, Robert W. Evans, Mihaela Trif, and Anca Roseanu. "Lactoferrin in Bone Tissue Regeneration." Current Medicinal Chemistry 27, no. 6 (March 16, 2020): 838–53. http://dx.doi.org/10.2174/0929867326666190503121546.
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: Among the multiple properties exhibited by lactoferrin (Lf), its involvement in bone regeneration processes is of great interest at the present time. A series of in vitro and in vivo studies have revealed the ability of Lf to promote survival, proliferation and differentiation of osteoblast cells and to inhibit bone resorption mediated by osteoclasts. Although the mechanism underlying the action of Lf in bone cells is still not fully elucidated, it has been shown that its mode of action leading to the survival of osteoblasts is complemented by its mitogenic effect. Activation of several signalling pathways and gene expression, in an LRPdependent or independent manner, has been identified. Unlike the effects on osteoblasts, the action on osteoclasts is different, with Lf leading to a total arrest of osteoclastogenesis. : Due to the positive effect of Lf on osteoblasts, the potential use of Lf alone or in combination with different biologically active compounds in bone tissue regeneration and the treatment of bone diseases is of great interest. Since the bioavailability of Lf in vivo is poor, a nanotechnology- based strategy to improve the biological properties of Lf was developed. The investigated formulations include incorporation of Lf into collagen membranes, gelatin hydrogel, liposomes, loading onto nanofibers, porous microspheres, or coating onto silica/titan based implants. Lf has also been coupled with other biologically active compounds such as biomimetic hydroxyapatite, in order to improve the efficacy of biomaterials used in the regulation of bone homeostasis. : This review aims to provide an up-to-date review of research on the involvement of Lf in bone growth and healing and on its use as a potential therapeutic factor in bone tissue regeneration.
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Liu, Zhen-Shu, and Po-Wen Chen. "Featured Prebiotic Agent: The Roles and Mechanisms of Direct and Indirect Prebiotic Activities of Lactoferrin and Its Application in Disease Control." Nutrients 15, no. 12 (June 15, 2023): 2759. http://dx.doi.org/10.3390/nu15122759.
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Lactoferrin (LF) is a glycoprotein found in mammalian milk, and lactoferricin is a peptide derived from LF hydrolysate. Both LF and lactoferricin (LFcin) have diverse functions that could benefit mammals. Bovine LF (BLF) and BLFcin exhibit a wide range of antimicrobial activities, but most probiotic strains are relatively resistant to their antibacterial effects. BLF and BLF hydrolysate can promote the growth of specific probiotics depending on the culture conditions, the dose of BLF or BLF-related peptides, and the probiotic strains used. BLF supplementation has been shown to modulate several central molecular pathways or genes in Lacticaseibacillus rhamnosus GG under cold conditions, which may explain the prebiotic roles of BLF. LF alone or in combination with selected probiotics can help control bacterial infections or metabolic disorders, both in animal studies and in human clinical trials. Various LF-expressing probiotics, including those expressing BLF, human LF, or porcine LF, have been developed to facilitate the combination of LFs with specific probiotics. Supplementation with LF-expressing probiotics has positive effects in animal studies. Interestingly, inactivated LF-expressing probiotics significantly improved diet-induced nonalcoholic fatty liver disease (NAFLD) in a mouse model. This review highlights the accumulated evidence supporting the use of LF in combination with selected LF-resistant probiotics or LF-expressing probiotics in the field.
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Lepanto, Maria Stefania, Luigi Rosa, Rosalba Paesano, Piera Valenti, and Antimo Cutone. "Lactoferrin in Aseptic and Septic Inflammation." Molecules 24, no. 7 (April 3, 2019): 1323. http://dx.doi.org/10.3390/molecules24071323.
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Lactoferrin (Lf), a cationic glycoprotein able to chelate two ferric irons per molecule, is synthesized by exocrine glands and neutrophils. Since the first anti-microbial function attributed to Lf, several activities have been discovered, including the relevant anti-inflammatory one, especially associated to the down-regulation of pro-inflammatory cytokines, as IL-6. As high levels of IL-6 are involved in iron homeostasis disorders, Lf is emerging as a potent regulator of iron and inflammatory homeostasis. Here, the role of Lf against aseptic and septic inflammation has been reviewed. In particular, in the context of aseptic inflammation, as anemia of inflammation, preterm delivery, Alzheimer’s disease and type 2 diabetes, Lf administration reduces local and/or systemic inflammation. Moreover, Lf oral administration, by decreasing serum IL-6, reverts iron homeostasis disorders. Regarding septic inflammation occurring in Chlamydia trachomatis infection, cystic fibrosis and inflammatory bowel disease, Lf, besides the anti-inflammatory activity, exerts a significant activity against bacterial adhesion, invasion and colonization. Lastly, a critical analysis of literature in vitro data reporting contradictory results on the Lf role in inflammatory processes, ranging from pro- to anti-inflammatory activity, highlighted that they depend on cell models, cell metabolic status, stimulatory or infecting agents as well as on Lf iron saturation degree, integrity and purity.
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Krzyzowska, Malgorzata, Marcin Chodkowski, Martyna Janicka, Dominika Dmowska, Emilia Tomaszewska, Katarzyna Ranoszek-Soliwoda, Katarzyna Bednarczyk, Grzegorz Celichowski, and Jaroslaw Grobelny. "Lactoferrin-Functionalized Noble Metal Nanoparticles as New Antivirals for HSV-2 Infection." Microorganisms 10, no. 1 (January 5, 2022): 110. http://dx.doi.org/10.3390/microorganisms10010110.
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(1) Background: Lactoferrin has been recognized as a potent inhibitor of human herpetic viruses, such as herpes simplex type 1 (HSV-1) and 2 (HSV-2). In this work, we tested if silver and gold nanoparticles modified with lactoferrin (LF-Ag/AuNPs) can become novel microbicides with additional adjuvant properties to treat genital herpes infection. (2) Methods: The antiviral and cytotoxic activities of LF-Ag/AuNPs were tested in human skin HaCaT and vaginal VK-2-E6/E7 keratinocytes. Viral titers and immune responses after treatment with LF-Ag/AuNPs were tested in murine vaginal HSV-2 infection. (3) Results: LF-Ag/AuNPs inhibited attachment and entry of HSV-2 in human keratinocytes much better than lactoferrin. Furthermore, pretreatment with LF-AgNPs led to protection from infection. Infected mice treated intravaginally with LF-Ag/AuNPs showed lower virus titers in the vaginal tissues and spinal cords in comparison to treatment with lactoferrin. Following treatment, vaginal tissues showed a significant increase in CD8+/granzyme B + T cells, NK cells and dendritic cells in comparison to NaCl-treated group. LF-Ag/AuNPs-treated animals also showed significantly better expression of IFN-γ, CXCL9, CXCL10, and IL-1β in the vaginal tissues. (4) Conclusions: Our findings show that LF-Ag/AuNPs could become effective novel antiviral microbicides with immune-stimulant properties to be applied upon the mucosal tissues.
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Sharma, Ankita, Umesh K. Shandilya, Monika Sodhi, Ashok K. Mohanty, Pranay Jain, and Manishi Mukesh. "Evaluation of Milk Colostrum Derived Lactoferrin of Sahiwal (Bos indicus) and Karan Fries (Cross-Bred) Cows for Its Anti-Cancerous Potential." International Journal of Molecular Sciences 20, no. 24 (December 14, 2019): 6318. http://dx.doi.org/10.3390/ijms20246318.
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Lactoferrin (Lf) is an iron-binding glycoprotein protein known to have immune-modulatory role and recently, its anticancerous effect against different cancer cell types was emphasized. In the present investigation, a comparative evaluation of anticancer potential of colostrum-derived lactoferrin from Indian native zebu cow (Sahiwal, SAC), crossbred (Karan Fries, KFC) and commercially available (C-Lf) lactoferrin from exotic cow using cellular models was made. A protocol was standardized successfully to purify Lf protein from colostrum of both breeds using HPLC and purity was confirmed by LC–MS. A standardized dose of 750 µg/mL Lf was used to treat two cell types MDA-MB-231 and MCF-7 with Lf from three different sources; SAC-Lf, KFC-Lf and C-Lf for 48 h and 72 h. Different cellular parameters including cytotoxicity, viability, apoptosis and cell proliferation were determined. Comparatively, Lf from commercial source (C-Lf) had maximum effect in both cell types followed by SAC-Lf and KFC-Lf. Further, transcriptional changes in genes associated with apoptosis (Bax and Bcl-2), tumor progression (p53, p21, CD44 and NF-κβ) and survival (survivin) were evaluated in Lf treatment. The overall results strongly emphasized to the fact that Lf purified from cow colostrum has the capacity to inhibit the in vitro growth of cancerous cell lines albeit to a varied extent.
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Rosenmund, A., C. Kuyas, and A. Haeberli. "Oxidative radioiodination damage to human lactoferrin." Biochemical Journal 240, no. 1 (November 15, 1986): 239–45. http://dx.doi.org/10.1042/bj2400239.
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Oxidative iodination of human lactoferrin (Lf) as commonly performed by using the chloramine-T, the Iodogen or the lactoperoxidase method produces an unreliable tracer protein because of excessive and heterogeneous polymer formation. Before iodination a minor tetramer fraction may be demonstrable in iron-saturated Lf only. Iodination-induced polymerization of iron-poor as well as iron-saturated Lf occurs independently of the presence or absence of 10 mM-EDTA and the 125I-/Lf molar ratio used for iodination. 125I-Lf polymers are mainly covalently linked, as suggested by the lack of substantial dissociation in SDS/polyacrylamide-gel electrophoresis. Damage to the 125I-Lf monomer may be another consequence of oxidative iodination. This is demonstrated in SDS/polyacrylamide-gel electrophoresis where 50% of the radioactivity of apparently normal monomer (Mr 75,000) is displaced to a lower-Mr region (30,000-67,000) after reduction with dithiothreitol. Non-oxidative iodination by the Bolton-Hunter technique produces an antigenetically stable tracer that is not being subjected to polymerization and monomer degradation as judged by high-performance gel chromatography and SDS/polyacrylamide-gel electrophoresis with and without dithiothreitol treatment. It is concluded that oxidation in itself leads to covalent non-disulphide cross-linking between human Lf molecules and, possibly, to intramolecular peptide-bond breaking becoming unmasked under reducing conditions. In biological experiments with human 125I-Lf this problem should be carefully considered.
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Wang, Xiao, Xiumin Wang, Ya Hao, Da Teng, and Jianhua Wang. "Research and development on lactoferrin and its derivatives in China from 2011–2015." Biochemistry and Cell Biology 95, no. 1 (February 2017): 162–70. http://dx.doi.org/10.1139/bcb-2016-0073.
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Lactoferrin (Lf), a multifunctional glycoprotein, is an important antimicrobial and immune regulatory protein present in neutrophils and most exocrine secretions of mammals. Lactoferricin (Lfcin) is located in the N-terminal region of this protein. In this review, the current state of research into Lf and Lfcin in China is described. Searching with HistCite software in Web Sci located 118 papers published by Chinese researchers from 2011–2015, making China one of the top 3 producers of Lf research and development in the world. The biological functions of Lf and Lfcin are discussed, including antibacterial, antiviral, antifungal, anticarcinogenic, and anti-inflammatory activities; targeted drug delivery, induction of neurocyte, osteoblast, and tenocyte growth, and possible mechanisms of action. The preparation and heterologous expression of Lf in animals, bacteria, and yeast are discussed in detail. Five Lf-related food additive factories and 9 Lf-related health food production companies are certified by the China Food and Drug Administration (CFDA). The latest progress in the generation of transgenic livestock in China, the safety of the use of transgenic animals, and future prospects for the uses of Lf and Lfcin are also covered.
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Niaz, Bushra, Farhan Saeed, Awais Ahmed, Muhammad Imran, Abid Aslam Maan, Muhammad Kashif Iqbal Khan, Tabussam Tufail, Faqir Muhammad Anjum, Shahzad Hussain, and Hafiz Ansar Rasul Suleria. "Lactoferrin (LF): a natural antimicrobial protein." International Journal of Food Properties 22, no. 1 (January 1, 2019): 1626–41. http://dx.doi.org/10.1080/10942912.2019.1666137.
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Zhang, Yingqi, Chao Lu, and Jin Zhang. "Lactoferrin and Its Detection Methods: A Review." Nutrients 13, no. 8 (July 22, 2021): 2492. http://dx.doi.org/10.3390/nu13082492.
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Lactoferrin (LF) is one of the major functional proteins in maintaining human health due to its antioxidant, antibacterial, antiviral, and anti-inflammatory activities. Abnormal levels of LF in the human body are related to some serious diseases, such as inflammatory bowel disease, Alzheimer’s disease and dry eye disease. Recent studies indicate that LF can be used as a biomarker for diagnosis of these diseases. Many methods have been developed to detect the level of LF. In this review, the biofunctions of LF and its potential to work as a biomarker are introduced. In addition, the current methods of detecting lactoferrin have been presented and discussed. We hope that this review will inspire efforts in the development of new sensing systems for LF detection.
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Bialic, Kinga, Artur Bialic, Rafał Bakalarczyk, Paweł Majewski, Lucjan Bednarz, Karolina Szala-Czerwonka, Natalia Woś, Adrian Rejmer, Katarzyna Rojek, and Karolina Wijas. "Exploring the Potential of Lactoferrin in Neonatology and Obstetrics - Promising Advancements for Maternal and Infant Health." Journal of Education, Health and Sport 34, no. 1 (May 28, 2023): 34–50. http://dx.doi.org/10.12775/jehs.2023.34.01.003.
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Introduction and purpose:
Lactoferrin (Lf), a glycoprotein found in body fluids, plays a key role in many of the biological mechanisms that occur in the human body. Over the years, more and more studies have contributed to the expansion of the clinical applications of lactoferrin. In this article, we want to focus on using lactoferrin in Neonatology and Obstetrics. The applications of lactoferrin in obstetrics continue to expand, some of which include the prevention of preterm delivery (PTD) and anaemia in pregnant women. Lf also helps to reduce the incidence of necrotizing enterocolitis and sepsis in newborns by mobilising the immune system and participating in the defence against pathogens and has been under investigation as a potential therapeutic agent for genital infections. The aim of this review is to summarise the current state of knowledge, regarding lactoferrin's broad spectrum of action and to highlight its potential therapeutic applications in these contexts.
State of knowledge:
This article aims to review the current knowledge on the properties of the lactoferrin and its applications in medicine, especially neonatology and obstetrics. Studies available in the PubMed and Google Scholar databases were included in the analysis.
Conclusion:
While lactoferrin shows promise in improving neonatal and maternal health, additional research is required to fully understand its precise mechanisms of action and optimise its use as a therapeutic agent. There is also a need for further studies to assess the safety and efficacy of lactoferrin in a variety of patient populations. Despite the challenges, lactoferrin continues to be an intriguing subject of scientific research, with potential therapeutic benefits in various medical fields.
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Suzuki, Yasushi A., and Bo Lönnerdal. "Characterization of mammalian receptors for lactoferrin." Biochemistry and Cell Biology 80, no. 1 (February 1, 2002): 75–80. http://dx.doi.org/10.1139/o01-228.
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Lactoferrin (Lf) has been suggested to have several physiological functions. Specific binding of Lf, indicating the presence of Lf receptors (LfRs), has been observed in various types of mammalian cells such as lymphocytes, hepatocytes, and enterocytes. These LfRs are considered to function as a mediator for some of the functions of Lf. We here review current knowledge of mammalian LfRs characterized in different tissues. We also briefly present evidence for the existence of an LfR provided by our cloning of a human intestinal LfR (HLfR). The entire coding region of the HLfR was cloned by polymerase chain reaction (PCR), and a recombinant HLfR (rHLfR) was expressed in a baculovirus system. The rHLfR was purified by immobilized human Lf (HLf) affinity chromatography, indicating that the rHLfR retained the capacity to bind HLf. The gene was expressed at high levels in fetal small intestine and in adult heart but at lower levels in Caco-2 cells. In summary, we demonstrate the presence of a unique receptor-mediated mechanism for Lf, functioning in the small intestine of the newborn infant and possibly in other tissues of human adults.Key words: lactoferrin, lactoferrin receptor, mammalian receptor, human, mouse.
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McAbee, D. D. "Isolated rat hepatocytes acquire iron from lactoferrin by endocytosis." Biochemical Journal 311, no. 2 (October 15, 1995): 603–9. http://dx.doi.org/10.1042/bj3110603.
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The iron-binding protein lactoferrin (Lf) present in blood is metabolized by the liver. Isolated rat hepatocytes vigorously endocytose bovine Lf via recycling Ca2(+)-dependent binding sites, but the uptake of iron from Lf by hepatocytes has not been examined. In this study, isolated rat hepatocytes were incubated with radiolabelled bovine Lf (125I-Lf, 59Fe-Lf or 125I-59Fe-Lf) at 37 degrees C, then washed at 4 degrees C in the presence of dextran sulphate with either Ca2+ or EGTA to distinguish between total bound and internal radioactivity respectively. Cells internalized 125I-Lf protein and Lf-bound 59Fe at maximal endocytic rates of 1700 and 480 mol.cell-1.s-1 respectively. When Lf was normalized for 59Fe content, these endocytic rates were equivalent and reflected an uptake potential of at least 3400 mol of iron.cell-1.s-1. Cells prebound with 125I-59Fe-Lf to Ca2+(-)dependent sites at 4 degrees C internalized more than 80% of both 125I-Lf protein and Lf-bound 59Fe approx. 6 min after warming to 37 degrees C at similar rates (125I-Lf: k(in) = 0.276 min-1, 59Fe: k(in) = 0.303 min-1). Within 4 h at 37 degrees C, cells had released 25% or less internalized Lf protein in the form of acid-soluble 125I-by-products but retained all the Lf-delivered 59Fe. Hyperosmotic disruption of clathrin-dependent endocytosis blocked the uptake of 125I-Lf and Lf-bound 59Fe. Incubation of cells with 125I-59Fe-Lf and a 100 molar excess of diferric transferrin reduced slightly the endocytosis of 125I-Lf protein and 59Fe accumulation. Treatment of cells with the ferric chelator desferrioxamine did not alter uptake of 125I-Lf protein or Lf-bound 59Fe, but the ferrous chelator bathophenanthroline disulphonate slightly elevated endocytosis of 125I-Lf protein and Lf-bound 59Fe. These findings indicate that Lf does not release its bound iron before endocytosis. It was concluded from this study that hepatocytes take up iron from Lf at high rates by a process that requires endocytosis of Lf-iron complexes.
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Lassiter, M. O., A. L. Newsome, L. D. Sams, and R. R. Arnold. "Characterization of Lactoferrin Interaction with Streptococcus mutans." Journal of Dental Research 66, no. 2 (February 1987): 480–85. http://dx.doi.org/10.1177/00220345870660021601.
Full textAbstract:
Lactoferrin (LF) is an iron-binding glycoprotein common to exocrine secretions and the specific granules of neutrophils. Each molecule is capable of high-affinity coordinate-binding of two ferric ions with two bicarbonate or carbonic anions. The initial aspect of the present study was directed at determining the nature of anion involvement in LF bactericidal activity. It was found that selective anions were capable of inhibiting the expression of bactericidal activity by LF on S. mutans 10449. The ability to block LF expression was directly related to the capacity of the anion to serve as a coordinate ion in iron-binding by the transferrin molecules. These data support the hypothesis that the LF target site on the bacterial surface is anionic. There has been controversy in the literature regarding LF involvement in hydroxy radical generation. The second phase of these studies indicated that treatment of S. mutans with LF under anaerobic conditions abrogated the bactericidal effect of this molecule. LF-killing could be enhanced by the presence of thiocyanate and inhibited by catalase and lactoperoxidase; however, bovine serum albumin was equally effective as an inhibitor. The apparent requirement for oxygen in LF bactericidal effect on S. mutans is not inconsistent with a hydroxy radical mechanism.
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Elizarova, Anna, Alexey Sokolov, Valeria Kostevich, Ekaterina Kisseleva, Evgeny Zelenskiy, Elena Zakharova, Oleg Panasenko, et al. "Interaction of Lactoferrin with Unsaturated Fatty Acids: In Vitro and In Vivo Study of Human Lactoferrin/Oleic Acid Complex Cytotoxicity." Materials 14, no. 7 (March 25, 2021): 1602. http://dx.doi.org/10.3390/ma14071602.
Full textAbstract:
As shown recently, oleic acid (OA) in complex with lactoferrin (LF) causes the death of cancer cells, but no mechanism(s) of that toxicity have been disclosed. In this study, constitutive parameters of the antitumor effect of LF/OA complex were explored. Complex LF/OA was prepared by titrating recombinant human LF with OA. Spectral analysis was used to assess possible structural changes of LF within its complex with OA. Structural features of apo-LF did not change within the complex LF:OA = 1:8, which was toxic for hepatoma 22a cells. Cytotoxicity of the complex LF:OA = 1:8 was tested in cultured hepatoma 22a cells and in fresh erythrocytes. Its anticancer activity was tested in mice carrying hepatoma 22a. In mice injected daily with LF-8OA, the same tumor grew significantly slower. In 20% of animals, the tumors completely resolved. LF alone was less efficient, i.e., the tumor growth index was 0.14 for LF-8OA and 0.63 for LF as compared with 1.0 in the control animals. The results of testing from 48 days after the tumor inoculation showed that the survival rate among LF-8OA-treated animals was 70%, contrary to 0% rate in the control group and among the LF-treated mice. Our data allow us to regard the complex of LF and OA as a promising tool for cancer treatment.
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Bobreneva, I. V., and M. V. Rokhlova. "Lactoferrin: properties and application. A review." Theory and practice of meat processing 6, no. 2 (July 29, 2021): 128–34. http://dx.doi.org/10.21323/2414-438x-2021-6-2-128-134.
Full textAbstract:
The current state, prospects for using and priorities in studying multifunctional protein lactoferrin (LF) in the food industry are discussed. Over the last decades, the studies of iron-binding, antibacterial, antiviral and antiparasitic properties of this representative of transferrins have determined quite a wide sphere of its use. The data on the lactoferrin composition, structure and activity are presented. The authors describe the modern methods for lactoferrin extraction and production from dairy raw materials both in the domestic and foreign productions using chromatographic methods for extraction and membrane methods for production. The practical experience in its application for food production, in particular, for meat and fermented dairy products, child and sports nutrition is discussed. An effect of technological process parameters in food production on the LF activity is highlighted. The study analyses an influence of new processing technologies such as high pressure or pulsed electric field in combination with classic methods for thermal processing and drying on the structure and activity of lactoferrin in food. The reviewed studies show that the use of lactoferrin in the meat industry, especially, in finished meat products, has limitations. The data presented in the review suggest a need for searching ways of lactoferrin introduction into meat systems to obtain functional products. One of the top-priority method for LF incorporation into meat products is LF encapsulation as one of the production stages.
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Pawlik, Adrianna, Grażyna Sender, Magdalena Sobczyńska, Agnieszka Korwin-Kossakowska, Henryka Lassa, and Jolanta Oprządek. "Lactoferrin gene variants, their expression in the udder and mastitis susceptibility in dairy cattle." Animal Production Science 55, no. 8 (2015): 999. http://dx.doi.org/10.1071/an13389.
Full textAbstract:
Lactoferrin gene (LF) is regarded as one of the potential markers of mastitis susceptibility/resistance in dairy cattle. The study’s aim was therefore, to investigate the feasibility of two single nucleotide polymorphisms (SNP), placed in the 5′-flanking region and 3′-untranslated region of the LF gene, to serve as mastitis markers. The associations between these SNP and the expression of LF, both on mRNA and protein level, were estimated in the milk of Polish Holstein-Friesian cows. The relationships between polymorphisms and cows’ estimated breeding values (EBV) for somatic cell count were also calculated. It was shown that both polymorphisms have a significant impact on lactoferrin content in milk, and that LF+32 SNP is associated with the cow’s EBV for somatic cell count. No association between SNP chosen for the study and lactoferrin mRNA abundance in milk somatic cells was observed. We propose LF+32 SNP for a molecular marker of mastitis resistance in dairy cows.
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Terekhova, M. S., D. V. Grigorieva, I. V. Gorudko, I. V. Semak, A. V. Sokolov, O. M. Panasenko, and S. N. Cherenkevich. "Physicochemical properties of lactoferrin under oxidative/halogenative stress." Doklady of the National Academy of Sciences of Belarus 63, no. 2 (May 18, 2019): 189–97. http://dx.doi.org/10.29235/1561-8323-2019-63-2-189-197.
Full textAbstract:
Lactoferrin (Lf) was discovered in the thirties of the twentieth century. Since that time a number of useful properties of Lf (antibacterial, antiviral, pro- and anti-inflammatory, etc.) have been found. That’s why Lf became a promising candidate for pharmaceuticals use. The concentration of Lf strikingly increases in inflammatory focuses due to neutrophil degranulation. At the same time, activated neutrophils starts to generate reactive oxygen and halogen species (ROS and RHS), which leads to the development of oxidative/halogenative stress. In this work, using the fluorescence analysis we found the change of the Lf structure and properties in the inflammation conditions (under oxidatives/halogenative stress). We use two forms of Lf – human Lf, excreted from human milk, and recombinant Lf, excreted from milk of transgenic goats. It was established that the amino acids of Lf (decreasing the number of tryptophanils and primary amines) and protein restructuring undergo modification under the HOCl action, while H2O2 has no influence. These changes in the molecule under the HOCl treatment result in decreasing the iron-binding capacity of Lf.
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Li, Ya, Jie Li, Zheng Gong, Xiao-Hua Pan, Zi-Han Ma, Shu-Yan Ma, Hong-Min Wang, Hong-Liang Dong, Fang-Yuan Gong, and Xiao-Ming Gao. "M860, a Monoclonal Antibody against Human Lactoferrin, Enhances Tumoricidal Activity of Low Dosage Lactoferrin via Granzyme B Induction." Molecules 24, no. 20 (October 9, 2019): 3640. http://dx.doi.org/10.3390/molecules24203640.
Full textAbstract:
Lactoferrin (LF) is a soluble glycoprotein of the transferring family found in most biological fluids, functioning as a major first line defense molecule against infection in mammals. It also shows certain anti-tumor activity, but its clinical application in tumor therapy is limited because high dosage is required. In this study, we demonstrate that M860, a monoclonal antibody against human LF (hLF), could significantly increase the anti-tumor potential of low dosage hLF by forming LF-containing immune complex (IC). Human monocytes primed with LF-IC, but not hLF or M860 alone, or control ICs, showed strong tumoricidal activity on leukemia cell lines Jurkat and Raji through induction of secreted Granzyme B (GzB). LF-IC is able to colligate membrane-bound CD14 (a TLR4 co-receptor) and FcγRIIa (a low affinity activating Fcγ receptor) on the surface of human monocytes, thereby triggering the Syk-PI3K-AKT-mTOR pathway leading to GzB production. Our work identifies a novel pathway for LF-mediated tumoricidal activity and may extend the clinical application of LF in tumor therapy.
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Ochoa, Theresa J., and Stéphane V. Sizonenko. "Lactoferrin and prematurity: a promising milk protein?" Biochemistry and Cell Biology 95, no. 1 (February 2017): 22–30. http://dx.doi.org/10.1139/bcb-2016-0066.
Full textAbstract:
Lactoferrin (Lf) is the major whey protein in milk, with multiple beneficial health effects including direct antimicrobial activities, anti-inflammatory effects, and iron homeostasis. Oral Lf supplementation in human preterm infants has been shown to reduce the incidence of sepsis and necrotizing enterocolitis. In preclinical models of antenatal stress and perinatal brain injury, bovine Lf protected the developing brain from neuronal loss, improved connectivity, increased neurotrophic factors, and decreased inflammation. It also supported brain development and cognition. Further, Lf can prevent preterm delivery by reducing proinflammatory factors and inhibiting premature cervix maturation. We review here the latest research on Lf in the field of neonatology.
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Pulina, Maria O., Elena T. Zakharova, Alexei V. Sokolov, Mikhail M. Shavlovski, Mikhail G. Bass, Kirill V. Solovyov, Vladimir N. Kokryakov, and Vadim B. Vasilyev. "Studies of the ceruloplasmin-lactoferrin complex." Biochemistry and Cell Biology 80, no. 1 (February 1, 2002): 35–39. http://dx.doi.org/10.1139/o01-206.
Full textAbstract:
We have previously shown that iron-containing human lactoferrin (LF) purified from breast milk is able to form both in vitro and in vivo a complex with ceruloplasmin (CP), the copper-containing protein of human plasma. Here we present evidence that the CPLF complex is dissociated by high concentrations of NaCl, CaCl2, or EDTA, or by decreasing the pH to 4.7. In addition, DNA, bacterial lipopolysaccharide, and heparin can displace CP from its complex with LF. Antibodies to either of the two proteins also cause dissociation of the complex.Key words: lactoferrin, ceruloplasmin, ferroxidase.
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Jiang, Rulan, Yasushi A. Suzuki, Xiaogu Du, and Bo Lönnerdal. "Lactoferrin and the lactoferrin–sophorolipids-assembly can be internalized by dermal fibroblasts and regulate gene expression." Biochemistry and Cell Biology 95, no. 1 (February 2017): 110–18. http://dx.doi.org/10.1139/bcb-2016-0090.
Full textAbstract:
Lactoferrin (Lf) is an iron-binding multifunctional protein, mainly present in external secretions. Lf is known to penetrate skin and may thus exert its multiple functions in skin. Sophorolipids (SLs) are glycolipid biosurfactants, which have been shown to enhance absorption of commercial bovine Lf (CbLf) in model skin via forming an assembly with CbLf. In this study, uptake and post-internalization localization of bovine Lf (bLf), CbLf, and human Lf (hLf) with or without forming assemblies with SLs in human dermal fibroblasts (HDFn) were determined using 125I-labeled Lfs and confocal microscopy, respectively. Our results show that all 3 Lfs were internalized by HDFn; although SLs did not significantly affect the uptake of Lfs, it changed Lf localization by accumulating Lfs in the perinuclear region. Furthermore, microarrays were used to investigate transcriptional profiling in HDFn in response to CbLf, SLs, or CbLf–SLs-assembly treatments. Transcriptome profiling indicates that CbLf may play roles in the protection of skin from oxidative stress, immunomodulatory activities, and enhancement of wound healing. The assembly had similar effects but dramatically modulated the transcription of some genes. SLs alone modified signaling pathways related to lipid metabolism, as well as synthesis of sex hormones and vitamins. Thus, CbLf may exert beneficial effects on skin, and these effects may be modulated by SLs.
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Soboleva, Svetlana E., Sergey E. Sedykh, Ludmila I. Alinovskaya, Valentina N. Buneva, and Georgy A. Nevinsky. "Cow Milk Lactoferrin Possesses Several Catalytic Activities." Biomolecules 9, no. 6 (May 29, 2019): 208. http://dx.doi.org/10.3390/biom9060208.
Full textAbstract:
Lactoferrin (LF) is a Fe3+-binding glycoprotein, that was first recognized in milk and then in other epithelial secretions and barrier body fluids to which many different functions have been attributed to LF including protection from iron-induced lipid peroxidation, immunomodulation, cell growth regulation, DNA and RNA binding, as well as transcriptional activation, etc. The polyfunctional physiological role of LF is still unclear, but it has been suggested to be responsible for primary defense against microbial and viral infections. It was shown previously that human milk LF possesses several enzymatic activities: DNase, RNase, ATPase, phosphatase, and amylase. Analysis of human, cow, horse, buffalo and camel LF showed a highly conserved three-dimensional (3D) structure including only detail differences in the species. Recently, it was shown that similar to human cow LF possesses DNase and RNase activities. Using different methods here we have shown for the first time that LFs from the milk of seven cows of different breeds possess high peroxidase, protease, amylase, protease, and phosphatase activities. Protease activity of cow LFs was activated by Mg2+ and Ca2+ ions. In contrast to human LFs, ATPase activity was revealed only in three of seven cow LF preparations. The discovery that LF possesses these activities may contribute to understanding the multiple physiological functions of this extremely polyfunctional protein including its protective role against microbial and viral infections.
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Reyes-López, Magda, Gerardo Ramírez-Rico, Jesús Serrano-Luna, and Mireya de la Garza. "Activity of Apo-Lactoferrin on Pathogenic Protozoa." Pharmaceutics 14, no. 8 (August 15, 2022): 1702. http://dx.doi.org/10.3390/pharmaceutics14081702.
Full textAbstract:
Parasites and other eventually pathogenic organisms require the ability to adapt to different environmental conditions inside the host to assure survival. Some host proteins have evolved as defense constituents, such as lactoferrin (Lf), which is part of the innate immune system. Lf in its iron-free form (apo-Lf) and its peptides obtained by cleavage with pepsin are microbicides. Parasites confront Lf in mucosae and blood. In this work, the activity of Lf against pathogenic and opportunistic parasites such as Cryptosporidium spp., Eimeria spp., Entamoeba histolytica, Giardia duodenalis, Leishmania spp., Trypanosoma spp., Plasmodium spp., Babesia spp., Toxoplasma gondii, Trichomonas spp., and the free-living but opportunistic pathogens Naegleria fowleri and Acanthamoeba castellani were reviewed. The major effects of Lf could be the inhibition produced by sequestering the iron needed for their survival and the production of oxygen-free radicals to more complicated mechanisms, such as the activation of macrophages to phagocytes with the posterior death of those parasites. Due to the great interest in Lf in the fight against pathogens, it is necessary to understand the exact mechanisms used by this protein to affect their virulence factors and to kill them.
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Maneva, Ana, Borislava Taleva, and Lilia Maneva. "Lactoferrin-Protector against Oxidative Stress and Regulator of Glycolysis in Human Erythrocytes." Zeitschrift für Naturforschung C 58, no. 3-4 (April 1, 2003): 256–62. http://dx.doi.org/10.1515/znc-2003-3-420.
Full textAbstract:
Binding of lactoferrin (Lf) to its membrane receptors requires an electron for the reduction of Fe3+LF to Fe2+LF. It is possible that glyceraldehyde D3-phosphate dehydrogenase, a glycolytic enzyme part of the erythrocyte membrane, delivers that electron. Then Lf, obtaining an electron from the coenzyme NADH, might stimulate glycolysis, which requires the oxidised state of the coenzyme NAD+. Such possibility is supported by the finding that another extracellular e- acceptor - potassium ferricyanide activates glycolysis by the similar mechanism. Present results show that ferricyanide inhibited the specific 59Fe-lactoferrin binding to its erythrocyte membrane receptors. It may be assumed that ferricyanide competes with lactoferrin for an electron which leads to decrease of the binding of 59Fe-lactoferrin to its receptors. Lactoferrin (50 and 100 nm), similar to ferricyanide, increased the accumulation of lactate (respectively by 25% and 30%). These results support the assumption that ferricyanide and lactoferrin are final acceptors of a common electron transport chain connected with the regulation of glycolysis.We established an antioxidative effect of lactoferrin on erythrocytes, which was expressed as: a) an influence on content and on activity of intracellular antioxidants - namely an enhancement of the content of reduced glutathione; b) a decreased content both of products of lipid peroxidation (thiobarbituric acid reactive substances) and hemolysis under normal conditions and oxidative stress.Lactoferrin is capable to bind metal ions and thus to block their catalytic participation in the oxidative disturbances of the membrane. In most of our experiments there were no metal ions in the incubation mixtures (except those stimulating oxidative stress). Our results showed that Lf limited both the generation of thiobarbituric acid reactive substances and hemolysis in the absence of metal ions in the media, as well as in their presence. These facts suggest that probably the antioxidative property of lactoferrin is glycolysis stimulation, leading to increased formation of ATP, which is necessary to maintain the ion gradient, membrane potential and morphology of the erythrocyte.
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Nagashima, Daichi, Yukiko Ishibashi, Sachiko Kawaguchi, Megumi Furukawa, Masahiro Toho, Megumi Ohno, Takeaki Nitto, and Nobuo Izumo. "Human Recombinant Lactoferrin Promotes Differentiation and Calcification on MC3T3-E1 Cells." Pharmaceutics 15, no. 1 (December 25, 2022): 60. http://dx.doi.org/10.3390/pharmaceutics15010060.
Full textAbstract:
Lactoferrin (LF), known to be present in mammalian milk, has been reported to promote the proliferation of osteoblasts and suppress bone resorption by affecting osteoclasts. However, the mechanisms underlying the effects of human sources LF on osteoblast differentiation have not yet been elucidated, and almost studies have used LF from bovine sources. The presented study aimed to characterize the molecular mechanisms of bovine lactoferrin (IF-I) and human recombinant lactoferrin (LF-II) on MC3T3-E1 pre-osteoblast cells. MC3T3-E1 cells were treated with LF, ascorbic acid, and β-glycerophosphate (β-GP). Cell proliferation was analyzed using the MTT assay. Alkaline phosphatase activation and osteopontin expression levels were evaluated via cell staining and immunocytochemistry. The differentiation markers were examined using quantitative real-time PCR. The cell viability assay showed the treatment of 100 μg/mL LF significantly increased; however, it was suppressed by the simultaneous treatment of ascorbic acid and β-GP. Alizarin red staining showed that the 100 μg/mL treatment of LF enhanced calcification. Quantitative real-time PCR showed a significant increase in osterix expression. The results suggest that treatment with both LFs enhanced MC3T3-E1 cell differentiation and promoted calcification. The mechanisms of calcification suggest that LFs are affected by an increase in osterix and osteocalcin mRNA levels.
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Tran, Tuan Hiep, Phuong Thi Thu Tran, and Duy Hieu Truong. "Lactoferrin and Nanotechnology: The Potential for Cancer Treatment." Pharmaceutics 15, no. 5 (April 28, 2023): 1362. http://dx.doi.org/10.3390/pharmaceutics15051362.
Full textAbstract:
Lactoferrin (Lf)—a glycoprotein of the transferrin family—has been investigated as a promising molecule with diverse applications, including infection inhibition, anti-inflammation, antioxidant properties and immune modulation. Along with that, Lf was found to inhibit the growth of cancerous tumors. Owing to unique properties such as iron-binding and positive charge, Lf could interrupt the cancer cell membrane or influence the apoptosis pathway. In addition, being a common mammalian excretion, Lf offers is promising in terms of targeting delivery or the diagnosis of cancer. Recently, nanotechnology significantly enhanced the therapeutic index of natural glycoproteins such as Lf. Therefore, in the context of this review, the understanding of Lf is summarized and followed by different strategies of nano-preparation, including inorganic nanoparticles, lipid-based nanoparticles and polymer-based nanoparticles in cancer management. At the end of the study, the potential future applications are discussed to pave the way for translating Lf into actual usage.
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Furmanski, P., Z. P. Li, M. B. Fortuna, C. V. Swamy, and M. R. Das. "Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity." Journal of Experimental Medicine 170, no. 2 (August 1, 1989): 415–29. http://dx.doi.org/10.1084/jem.170.2.415.
Full textAbstract:
Lactoferrin (Lf), the major iron-binding component of milk, also a major constituent of the specific granules of neutrophils involved in antimicrobial activity and a glycoprotein thought to play a role in regulatory functions in the hematopoietic system as well as other physiologic activities, is shown to occur in three isoforms. One, Lf-alpha, binds iron; the other two, Lf-beta and Lf-gamma, express potent RNase activity, but do not bind iron. The three isoforms are very similar or identical in Mr, pI, partial proteolytic peptide patterns, NH2-terminal amino acid sequence, and reactivity with mAbs and polyclonal antisera against the RNase and Lf, respectively. The finding of structurally similar but enzymatically distinct forms of Lf may be related to the diverse functions of the molecule.
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Hu, Zhao, Zhao, Wang, and Zhu. "The Effects of the Combination of Oral Lactoferrin and Iron Injection on Iron Homestasis, Antioxidative Abilities and Cytokines Activities of Suckling Piglets." Animals 9, no. 7 (July 11, 2019): 438. http://dx.doi.org/10.3390/ani9070438.
Full textAbstract:
Iron deficiency is considered a common nutritional problem for suckling piglets. The aim of this study was to evaluate the effects of the combination of oral lactoferrin and iron injection on iron levels, antioxidant ability and cytokine activity in suckling piglets. A total of sixty suckling piglets taken from six sows (10 piglets per litter) with a similar parity were chosen. The lactoferrin (LF) group was orally administrated with lactoferrin solution (0.5 g/kg body weight per day) for a week, the CON group was orally administrated with the same dose of physiological saline. Each piglet (all groups) was given 100 mg of iron dextran (FeDex) by intramuscular injection at the third day of age. Six piglets (n = 6) from each group were euthanized on days 8 and 21. The oral lactoferrin improved the iron level of suckling piglets by increasing the concentrations of serum hemoglobin and hepatic iron on day 8. Gene expression of lactoferrin receptor (LFR) was significantly increased in the LF group piglets on day 8, while duodenal protein expression of the divalent metal transporter 1 (DMT1) was significantly reduced in the LF group on day 8. In addition, oral lactoferrin enhanced serum T-AOC activities and duodenal SOD activities on day 21. The LF piglets had a significantly increased serum concentration of IL-10 on day 8. These results indicated that a combination of oral lactoferrin and iron injection is a more effective method of improving the iron level by up-regulating the expression of the LFR gene, enhancing the antioxidant ability and modulating the cytokine activity in the suckling piglets.
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PAYNE, K. D., P. M. DAVIDSON, S. P. OLIVER, and G. L. CHRISTEN. "Influence of Bovine Lactoferrin on the Growth of Listeria monocytogenes." Journal of Food Protection 53, no. 6 (June 1, 1990): 468–72. http://dx.doi.org/10.4315/0362-028x-53.6.468.
Full textAbstract:
The influence of bovine lactoferrin (LF) and Apo-LF on growth of Listeria monocytogenes in Ultra-High Temperature (UHT) 2% fat milk was determined. The effect of LF was dependent upon both the degree of iron saturation and concentration. Before iron removal, LF was found to be approximately 52% saturated with iron; and at 23 and 46 mg/ml LF, minimal growth inhibition of L. monocytogenes was observed. Following dialysis, Apo-LF iron saturation was reduced to approximately 18%. At 15 and 30 mg/ml Apo-LF, a bacteriostatic effect against L. monocytogenes was observed. Inhibition of growth associated with Apo-LF was abolished when ferric ammonium citrate was added to saturate the iron binding sites of the Apo-LF.
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Sadchikov, P. E., I. L. Goldman, S. V. Razin, A. D. Chernousov, L. I. Alekseeva, and E. R. Sadchikova. "THE MOLECULAR MECHANISM OF LACTOFERRIN INFLUENCE ON BONE FORMATION." Osteoporosis and Bone Diseases 19, no. 3 (December 15, 2016): 12–22. http://dx.doi.org/10.14341/osteo2016312-22.
Full textAbstract:
In present critical review of systematized materials on the breakthrough achievements of the last decade - the discovery of the effect of protein lactoferrin (LF) on bone formation. It is shownthat LF increases the number of osteoblasts, stimulate their proliferation and differentiation, and prevents their destruction. Action of LF exceeds that of many other previously established bone-forming factors. LF increases the ability of osteoblasts to synthesize and mineralize bone matrix. Apparently, the effect of LF on bone anabolism ensured by the presence of specific receptors on osteoblasts. It was found that LF also inhibits the formation of osteoclasts. Experimental studies have demonstrated that LF prevents the destruction of bone tissue in ovariectomizedanimals and, thus, developing the type of postmenstrual osteoporosis in women. We get the first clinical studies demonstrating an increase in the period of healing of bone injuries while reducing the level of endogenous LF. Since molecular research establishes that the expression of the LF gene is regulated by estrogen, which reduces the development of postmenopausal osteoporosis (PMO) in women, there is a need to further investigate the relationship of these processes, which will help to create a basis for the management of bone formation.
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Arutyunova, Elena, Cory L. Brooks, Amanda Beddek, Michelle W. Mak, Anthony B. Schryvers, and M. Joanne Lemieux. "Crystal structure of the N-lobe of lactoferrin binding protein B from Moraxella bovis1 1This paper is an invited article as a result of a presentation at the International Lactoferrin Conference held in Mazatlan, Mexico (May 2011), and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 90, no. 3 (June 2012): 351–61. http://dx.doi.org/10.1139/o11-078.
Full textAbstract:
Lactoferrin (Lf) is a bi-lobed, iron-binding protein found on mucosal surfaces and at sites of inflammation. Gram-negative pathogens from the Neisseriaceae and Moraxellaceae families are capable of using Lf as a source of iron for growth through a process mediated by a bacterial surface receptor that directly binds host Lf. This receptor consists of an integral outer membrane protein, lactoferrin binding protein A (LbpA), and a surface lipoprotein, lactoferrin binding protein B (LbpB). The N-lobe of the homologous transferrin binding protein B, TbpB, has been shown to facilitate transferrin binding in the process of iron acquisition. Currently there is little known about the role of LbpB in iron acquisition or how Lf interacts with the bacterial receptor proteins. No structural information on any LbpB or domain is available. In this study, we express and purify from Escherichia coli the full-length LbpB and the N-lobe of LbpB from the bovine pathogen Moraxella bovis for crystallization trials. We demonstrate that M. bovis LbpB binds to bovine but not human Lf. We also report the crystal structure of the N-terminal lobe of LbpB from M. bovis and compare it with the published structures of TbpB to speculate on the process of Lf mediated iron acquisition.
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Hwang, Shen-An, Sydney Boyd, Marian Kruzel, and Jeffrey Actor. "Lactoferrin enhances BCG efficacy to protect against tuberculosis disease pathology (106.28)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 106.28. http://dx.doi.org/10.4049/jimmunol.186.supp.106.28.
Full textAbstract:
Abstract Lactoferrin (LF), an iron binding protein found primarily in mucosal secretions and granules of neutrophils, possesses immune modulatory properties that include enhancement of the delayed type hypersensitivity against BCG antigens. Lactoferrin admixed to BCG enhanced host protection upon subsequent challenge with Erdman MTB, demonstrated by decreased organ CFU and reduced granuloma lesions. Splenic recall responses showed immunization with BCG/LF increased IFN-γ production. Additionally, dendritic cells cultured with BCG/LF increased expression of MHC II and CD86 compared to BCG alone. This study examines optimization of LF adjuvant to enhance efficacy of BCG by examining multiple vaccination parameters. C57BL/6 mice were immunized with or without booster at 8 weeks with BCG, BCG/bovine LF (1, 10 100μg), BCG/human recombinant lactoferrin (rhLF) sialylated (1, 10μg), or BCG/rhLF non-sialylated (1, 10μg). 12 weeks post-vaccination, mice were aerosol challenged with Erdman MTB and monitored through 24 weeks. At 6 weeks, splenic recall responses against BCG were examined. Peak LF adjuvant activity was observed at doses greater than 10μg/mouse, assessed by decreased pulmonary pathology post-MTB challenge. Splenic recall responses from BCG/bLF immunized mice showed increased IFN-γ and IL-17 with a concurrent decrease in IL-10 compared to BCG vaccinated and non-immunized controls. No significant differences observed between sialylated and non-sialylated human recombinant LF.
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Regueiro, Uxía, Maite López-López, Rubén Varela-Fernández, Francisco Javier Otero-Espinar, and Isabel Lema. "Biomedical Applications of Lactoferrin on the Ocular Surface." Pharmaceutics 15, no. 3 (March 7, 2023): 865. http://dx.doi.org/10.3390/pharmaceutics15030865.
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Lactoferrin (LF) is a first-line defense protein with a pleiotropic functional pattern that includes anti-inflammatory, immunomodulatory, antiviral, antibacterial, and antitumoral properties. Remarkably, this iron-binding glycoprotein promotes iron retention, restricting free radical production and avoiding oxidative damage and inflammation. On the ocular surface, LF is released from corneal epithelial cells and lacrimal glands, representing a significant percentage of the total tear fluid proteins. Due to its multifunctionality, the availability of LF may be limited in several ocular disorders. Consequently, to reinforce the action of this highly beneficial glycoprotein on the ocular surface, LF has been proposed for the treatment of different conditions such as dry eye, keratoconus, conjunctivitis, and viral or bacterial ocular infections, among others. In this review, we outline the structure and the biological functions of LF, its relevant role at the ocular surface, its implication in LF-related ocular surface disorders, and its potential for biomedical applications.
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Gajda-Morszewski, Przemysław, and Małgorzata Brindell. "Lactoferrin as a Potent Natural Supplement Exhibiting a Synergistic Effect with Drugs in Antimicrobial and Anticancer Therapies." Current Protein & Peptide Science 22, no. 9 (September 2021): 629–40. http://dx.doi.org/10.2174/1389203722666211011113932.
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: For many years, natural products have played a crucial role in drug discovery and drug design as a source of active agents or as inspiration. Lactoferrin (Lf), a glycoprotein found in milk and mammalian secretions, has been extensively studied in recent years, and numerous antimicrobial, anti-inflammatory, and anticancer properties of Lf have been demonstrated in the literature. The use of lactoferrin as a co-agent or supplement to enhance the beneficial effect of drugs, or to reduce their side effects, arouses the interest of many researchers, especially since Lf is a well-studied, biocompatible, cheap, and easily accessible protein. In this mini-review, we focus on the elucidation of the role of Lf in antimicrobial or anticancer therapies, pointing to the possible mechanism underlying the determined synergism between Lf and commonly used drugs.
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Mikulic, Nadja, Mary A. Uyoga, Edith Mwasi, Nicole U. Stoffel, Christophe Zeder, Simon Karanja, and Michael B. Zimmermann. "Iron Absorption is Greater from Apo-Lactoferrin and is Similar Between Holo-Lactoferrin and Ferrous Sulfate: Stable Iron Isotope Studies in Kenyan Infants." Journal of Nutrition 150, no. 12 (September 4, 2020): 3200–3207. http://dx.doi.org/10.1093/jn/nxaa226.
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ABSTRACT Background Whether lactoferrin (Lf) binds iron to facilitate its absorption or to sequester iron from potential enteropathogens remains uncertain. Bovine Lf is added to many infant formulas, but previous studies in infants reported that Lf had no effect on or inhibited iron absorption. The effects of the apo (iron-free) or the holo (iron-loaded) forms of Lf on iron absorption are unclear. Objectives Our objective was to compare iron absorption from a maize-based porridge containing: 1) labeled ferrous sulfate (FeSO4) alone; 2) labeled FeSO4 given with bovine apo-Lf; and 3) intrinsically labeled bovine holo-Lf. Methods In a crossover study, we measured iron absorption in Kenyan infants (n = 25; mean ± SD age 4.2 ± 0.9 months; mean ± SD hemoglobin 109 ± 11 g/L) from maize-based test meals containing: 1) 1.5 mg of iron as 54Fe-labeled FeSO4; 2) 1.42 mg of iron as 58Fe-labeled FeSO4, given with 1.41 g apo-Lf (containing 0.08 mg iron); and 3) 1.41 g holo-Lf carrying 1.5 mg iron as 57Fe. The iron saturation levels of apo- and holo-Lf were 0.56% and 47.26%, respectively primary outcome was fractional iron absorption (FIA), assessed by erythrocyte incorporation of isotopic labels. Results The FIA from the meal containing apo-Lf + FeSO4 (geometric mean, 9.8%; −SD and +SD, 5.4% and 17.5%) was higher than from the meals containing FeSO4 (geometric mean, 6.3%; −SD and +SD, 3.2% and 12.6%; P = 0.002) or holo-Lf (geometric mean, 5.0%; −SD and +SD, 2.8% and 8.9%; P <0.0001). There was no significant difference in FIA when comparing the meals containing holo-Lf versus FeSO4 alone (P = 0.24). Conclusions The amount of iron absorbed from holo-Lf was comparable to that of FeSO4, and the addition of apo-Lf to a test meal containing FeSO4 significantly increased (+56%) iron absorption. These findings suggest that Lf facilitates iron absorption in young infants. Because Lf binds iron with high affinity, it could be a safe way to provide iron to infants in low-income countries, where iron fortificants can adversely affect the gut microbiome and cause diarrhea. This study was registered at clinicaltrials.gov as NCT03617575.
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PEJLER, Gunnar. "Lactoferrin regulates the activity of heparin proteoglycan-bound mast cell chymase: characterization of the binding of heparin to lactoferrin." Biochemical Journal 320, no. 3 (December 15, 1996): 897–903. http://dx.doi.org/10.1042/bj3200897.
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Rat mast cell protease 1 (RMCP-1) is a secretory granule serine protease (chymase) that is recovered in vivo in a macromolecular complex with heparin proteoglycan (PG). We have previously shown that heparin activates RMCP-1 and that RMCP-1, when bound to heparin PG, is largely resistant to inhibition by a variety of macromolecular protease inhibitors. In the search for alternative mechanisms in the regulation of RMCP-1 activity, we hypothesized that heparin antagonists, by interfering with the RMCP-1/heparin PG interaction, might influence the activity of heparin-bound mast cell chymase. In the present study, lactoferrin (LF), a heparin-binding protein, was assessed for RMCP-1 inhibiting activity. LF proved to decrease the activity of heparin PG-associated RMCP-1, although a portion of the enzyme activity was resistant to regulation. The mechanism of regulation was shown to involve the displacement of RMCP-1 from heparin PG, and LF caused an approx. 6-fold increase in the apparent Km of the RMCP-1–heparin PG complex for the chromogenic substrate S-2586. The interaction of LF with heparin was characterized. Pig mucosal heparin and endogenous heparin PG were equally effective in binding LF, whereas heparan sulphate bound with lower affinity. None of dermatan sulphate, chondroitin sulphate or hyaluronan were effective in binding LF. Further, the 6-O-, 2-O- and N-sulphate groups in heparin were of approximately equal importance for binding. Octasaccharides were the smallest heparin oligosaccharides showing significant binding to LF.
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Zorina, V. N. "Pattern of lactoferrin anti-influenza virus inhibitory activity." Russian Journal of Infection and Immunity 10, no. 1 (April 7, 2020): 49–54. http://dx.doi.org/10.15789/2220-7619-pol-1156.
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Active antigenic drift allows the influenza virus to partially or completely avoid recognition by the immune system. For treatment, inhibitors of the proton-selective ion channel M2 and inhibitors of neuraminidase are used, which have undesirable side effects and provoke the emergence of treatment-resistant strains of the virus. This justifies the need to search for new therapeutic agents. Lactoferrin (LF) is a glycoprotein with a molecular mass of 75—80 kDa, capable for binding metal ions. The highest concentrations of LF are detected in colostrum and milk, a significant amount is deposited in neutrophil granules. The structure of the LF domains of human milk, cow, goat, pig, horse, camel, buffalo is homologous. LF interacts with both specific receptors and endocytosis receptors (LRP), Toll-like, signal receptors on the surface of various cell types. Lactoferrin of humans and animals has a high antiviral activity. This glycoprotein modulates the immune system, including the humoral and cellular immune responses, and regulates redox reactions. However, literature data on the role of this protein in the prevention and treatment of influenza are few. LF inhibitory activity against influenza A and B viruses has been described, including H1N1, H5N1, H7N1, H3N2 strains. It has been established that LF binds virus hemagglutinin, preventing interaction with the cell, blocks programmed cell death through interaction with caspase 3 for preventing the spread of the virus at the later stages of the infection, and blocks virus assembly. Peptides synthesized on the basis of LF C-domain structure demonstrate high inhibitory activity against virus. The use of LF as an adjuvant for vaccines is more effective than of aluminum oxide. Further study of LF effects on influenza virus and on the immune response during infection is necessary to develop new methods of prevention and treatment.
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Wang, Ye, Alaa Bekhit, Susan Mason, and James Morton. "Lactoferrin Isolation and Hydrolysis from Red Deer (Cervus elaphus) Milk and the Antibacterial Activity of Deer Lactoferrin and Its Hydrolysates." Foods 9, no. 11 (November 21, 2020): 1711. http://dx.doi.org/10.3390/foods9111711.
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Lactoferrin (Lf) and other whey proteins have been isolated from red deer milk for the first time using a three-step anion and cation exchange chromatography protocol. The separated deer Lf was subject to in vitro gastric and duodenal digestions to generate peptides. The purity of the deer Lf and its hydrolysis products were analyzed by SDS-PAGE. The antibacterial activity of the deer Lf and its hydrolysates were investigated and was compared to cow counterpart. Gastric and duodenal digested deer Lf had strong bactericidal activity against E. coli ATCC 25922 with minimum inhibition concentration (MIC) of 280 µM and 402 µM, respectively. These results suggest that deer milk contains bioactive whey proteins and can generate bioactive peptides, which can benefit human health by inhibiting food-borne pathogenic bacteria.
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Li, Yu-Qi, and Chuang Guo. "A Review on Lactoferrin and Central Nervous System Diseases." Cells 10, no. 7 (July 17, 2021): 1810. http://dx.doi.org/10.3390/cells10071810.
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Central nervous system (CNS) diseases are currently one of the major health issues around the world. Most CNS disorders are characterized by high oxidative stress levels and intense inflammatory responses in affected tissues. Lactoferrin (Lf), a multifunctional iron-binding glycoprotein, plays a significant role in anti-inflammatory, antibacterial, antiviral, reactive oxygen species (ROS) modulator, antitumor immunity, and anti-apoptotic processes. Previous studies have shown that Lf is abnormally expressed in a variety of neurological diseases, especially neurodegenerative diseases. Recently, the promotion of neurodevelopment and neuroprotection by Lf has attracted widespread attention, and Lf could be exploited both as an active therapeutic agent and drug nanocarrier. However, our understanding of the roles of Lf proteins in the initiation or progression of CNS diseases is limited, especially the roles of Lf in regulating neurogenesis. This review highlights recent advances in the understanding of the major pharmacological effects of Lf in CNS diseases, including neurodegenerative diseases, cerebrovascular disease, developmental delays in children, and brain tumors.
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Florian, Paula, Alina Macovei, Livia Sima, Norica Nichita, Inger Mattsby-Baltzer, and Anca Roseanu. "Endocytosis and trafficking of human lactoferrin in macrophage-like human THP-1 cells1This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 90, no. 3 (June 2012): 449–55. http://dx.doi.org/10.1139/o11-090.
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Different cell types have been reported to internalize lactoferrin (Lf) by specific or nonspecific receptors. Our studies focused on the endocytic pathway of human Lf in macrophage-like THP-1 cells. Lactoferrin was found to be internalized by THP-1 cells differentiated with phorbol myristate acetate. Incubation of cells with chlorpromazine and dansylcadaverine, inhibitors of clathrin-dependent endocytosis, led to a 50% inhibition of Lf internalization compared with untreated cells. Bafilomycin A1 and NH4Cl treatment also resulted in 40%–60% inhibition, respectively, suggesting that the internalization of Lf may partly be mediated by acidic endosome-like organelles. Endocytic uptake of Lf was also cholesterol-dependent, as shown by methyl-β-cyclodextrin or nystatin treatment of the cells prior to internalization. Partial colocalization of Lf and EEA-1, a marker specific for early endosomes, could be observed. Colocalization of Lf with a specific endoplasmic reticulum marker was also detected. Our results suggest that Lf is internalized mainly by the clathrin-dependent pathway in THP-1 cells and targets the ER. The physiological consequences of this intracellular trafficking will be the subject of future investigations.
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Liu, Zhen-Shu, Chuen-Fu Lin, Chung-Pei Lee, Min-Chi Hsieh, Hung-Fu Lu, Ying-Fang Chen, Yu-We Ku, and Po-Wen Chen. "A Single Plasmid of Nisin-Controlled Bovine and Human Lactoferrin Expressing Elevated Antibacterial Activity of Lactoferrin-Resistant Probiotic Strains." Antibiotics 10, no. 2 (January 27, 2021): 120. http://dx.doi.org/10.3390/antibiotics10020120.
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Lactoferrin (LF) is a multifunctional protein found in mammals, and it shows broad-spectrum antimicrobial activity. To improve the functional properties of specific probiotics in order to provide both the beneficial characteristics of lactic acid bacteria and the biological activity of LF, cDNAs of bovine LF (BLF), human LF (HLF), or porcine LF (PLF) were cloned into a nisin-inducible plasmid. These were then transformed into the selected eight probiotics, which are LF-resistant hosts. Expression of recombinant LFs (rLFs) was analyzed via SDS-PAGE and Western blot analysis. Although the selected host strains may not contain the nisRK genes (NisK, the sensor kinase; NisR, the regulator protein), the components of autoregulation, a low level of LFs expression can be successfully induced by using nisin within bacterial cells in a time-dependent manner in three engineered clones, including Lactobacillus delbrueckii/HLF, L. delbrueckii/BLF, and L. gasseri/BLF. Lactobacillus delbrueckii and Lactobacillus gasseri originate from yogurt and human milk, respectively, and both strains are functional probiotic strains. Therefore, we further compared the antibacterial activities of disrupted recombinant probiotic clones, conventional strains (host control), and vector control ones by using agar diffusion and broth inhibition analysis, and the expression of rLFs in the above three clones considerately improved their antibacterial efficacies against four important food-borne pathogens, namely, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis, and Salmonellaenterica. In conclusion, this study provides a simple strategy for the production of functional LFs (BLF and HLF) in both functional and LF-resistant hosts for applications in the field.
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Edde, Lynn, Ronaldo B. Hipolito, Freda F. Y. Hwang, Denis R. Headon, Robert A. Shalwitz, and Michael P. Sherman. "Lactoferrin protects neonatal rats from gut-related systemic infection." American Journal of Physiology-Gastrointestinal and Liver Physiology 281, no. 5 (November 1, 2001): G1140—G1150. http://dx.doi.org/10.1152/ajpgi.2001.281.5.g1140.
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Lactoferrin is a milk protein that reportedly protects infants from gut-related, systemic infection. Proof for this concept is limited and was addressed during in vivo and in vitro studies. Neonatal rats pretreated orally with recombinant human lactoferrin (rh-LF) had less bacteremia and lower disease severity scores ( P < 0.001) after intestinal infection with Escherichia coli. Control animals had 1,000-fold more colony-forming units of E. coli per milliliter of blood than treated animals ( P < 0.001). Liver cultures from control animals had a twofold increase in bacterial counts compared with cultures from rh-LF-treated pups ( P < 0.02). Oral therapy with rh-LF + FeSO4did not alter the protective effect. In vitro studies confirmed that rh-LF interacted with the infecting bacterium and rat macrophages. An in vitro assay showed that rh-LF did not kill E. coli, but a combination of rh-LF + lysozyme was microbicidal. In vitro studies showed that rat macrophages released escalating amounts of nitric oxide and tumor necrosis factor-α when stimulated with increasing concentrations of rh-LF. The in vitro studies suggest that rh-LF may act with other “natural peptide antibiotics” or may prime macrophages to kill E. coli in vivo.