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Journal articles on the topic 'Protein secretion'

Author: Grafiati

Published: 4 June 2021

Last updated: 31 January 2023

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1

Blocker, Ariel, Pierre Gounon, Eric Larquet, Kirsten Niebuhr, Véronique Cabiaux, Claude Parsot, and Philippe Sansonetti. "The Tripartite Type III Secreton of Shigella flexneri Inserts Ipab and Ipac into Host Membranes." Journal of Cell Biology 147, no. 3 (November 1, 1999): 683–93. http://dx.doi.org/10.1083/jcb.147.3.683.

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Bacterial type III secretion systems serve to translocate proteins into eukaryotic cells, requiring a secreton and a translocator for proteins to pass the bacterial and host membranes. We used the contact hemolytic activity of Shigella flexneri to investigate its putative translocator. Hemolysis was caused by formation of a 25-Å pore within the red blood cell (RBC) membrane. Of the five proteins secreted by Shigella upon activation of its type III secretion system, only the hydrophobic IpaB and IpaC were tightly associated with RBC membranes isolated after hemolysis. Ipa protein secretion and hemolysis were kinetically coupled processes. However, Ipa protein secretion in the immediate vicinity of RBCs was not sufficient to cause hemolysis in the absence of centrifugation. Centrifugation reduced the distance between bacterial and RBC membranes beyond a critical threshold. Electron microscopy analysis indicated that secretons were constitutively assembled at 37°C before any host contact. They were composed of three parts: (a) an external needle, (b) a neck domain, and (c) a large proximal bulb. Secreton morphology did not change upon activation of secretion. In mutants of some genes encoding the secretion machinery the organelle was absent, whereas ipaB and ipaC mutants displayed normal secretons.

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Possot, Odile M., Guillaume Vignon, Natalia Bomchil, Frank Ebel, and Anthony P. Pugsley. "Multiple Interactions between Pullulanase Secreton Components Involved in Stabilization and Cytoplasmic Membrane Association of PulE." Journal of Bacteriology 182, no. 8 (April 15, 2000): 2142–52. http://dx.doi.org/10.1128/jb.182.8.2142-2152.2000.

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ABSTRACT We report attempts to analyze interactions between components of the pullulanase (Pul) secreton (type II secretion machinery) fromKlebsiella oxytoca encoded by a multiple-copy-number plasmid in Escherichia coli. Three of the 15 Pul proteins (B, H, and N) were found to be dispensable for pullulanase secretion. The following evidence leads us to propose that PulE, PulL, and PulM form a subcomplex with which PulC and PulG interact. The integral cytoplasmic membrane protein PulL prevented proteolysis and/or aggregation of PulE and mediated its association with the cytoplasmic membrane. The cytoplasmic, N-terminal domain of PulL interacted directly with PulE, and both PulC and PulM were required to prevent proteolysis of PulL. PulM and PulL could be cross-linked as a heterodimer whose formation in a strain producing the secreton required PulG. However, PulL and PulM produced alone could also be cross-linked in a 52-kDa complex, indicating that the secreton exerts subtle effects on the interaction between PulE and PulL. Antibodies against PulM coimmunoprecipitated PulL, PulC, and PulE from detergent-solubilized cell extracts, confirming the existence of a complex containing these four proteins. Overproduction of PulG, which blocks secretion, drastically reduced the cellular levels of PulC, PulE, PulL, and PulM as well as PulD (secretin), which probably interacts with PulC. The Pul secreton components E, F, G, I, J, K, L, and M could all be replaced by the corresponding components of the Out secretons of Erwinia chrysanthemi and Erwinia carotovora, showing that they do not play a role in secretory protein recognition and secretion specificity.

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3

Seo, Jin, Anja Brencic, and Andrew J. Darwin. "Analysis of Secretin-Induced Stress in Pseudomonas aeruginosa Suggests Prevention Rather than Response and Identifies a Novel Protein Involved in Secretin Function." Journal of Bacteriology 191, no. 3 (November 21, 2008): 898–908. http://dx.doi.org/10.1128/jb.01443-08.

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ABSTRACT Secretins are bacterial outer membrane proteins that are important for protein export. However, they can also mislocalize and cause stress to the bacterial cell, which is dealt with by the well-conserved phage shock protein (Psp) system in a highly specific manner. Nevertheless, some bacteria have secretins but no Psp system. A notable example is Pseudomonas aeruginosa, a prolific protein secretor with the potential to produce seven different secretins. We were interested in investigating how P. aeruginosa might deal with the potential for secretin-induced stress without a Psp system. Microarray analysis revealed the absence of any transcriptional response to XcpQ secretin overproduction. However, transposon insertions in either rpoN, truB, PA4068, PA4069, or PA0943 rendered P. aeruginosa hypersensitive to XcpQ production. The PA0943 gene was studied further and found to encode a soluble periplasmic protein important for XcpQ localization to the outer membrane. Consistent with this, a PA0943 null mutation reduced the levels of type 2 secretion-dependent proteins in the culture supernatant. Therefore, this work has identified a novel protein required for normal secretin function in P. aeruginosa. Taken together, all of our data suggest that P. aeruginosa lacks a functional equivalent of the Psp stress response system. Rather, null mutations in genes such as PA0943 may cause increased secretin-induced stress to which P. aeruginosa cannot respond. Providing the PA0943 mutant with the ability to respond, in the form of critical Psp proteins from another species, alleviated its secretin sensitivity.

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4

Atmakuri, Krishnamohan, and Sarah M. Fortune. "Regulation of Protein Secretion by … Protein Secretion?" Cell Host & Microbe 4, no. 3 (September 2008): 190–91. http://dx.doi.org/10.1016/j.chom.2008.08.009.

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5

Honzawa, Norikiyo, Kei Fujimoto, Masaki Kobayashi, Daisuke Kohno, Osamu Kikuchi, Hiromi Yokota-Hashimoto, Eri Wada, et al. "Protein Kinase C (Pkc)-δ Mediates Arginine-Induced Glucagon Secretion in Pancreatic α-Cells." International Journal of Molecular Sciences 23, no. 7 (April 4, 2022): 4003. http://dx.doi.org/10.3390/ijms23074003.

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The pathophysiology of type 2 diabetes involves insulin and glucagon. Protein kinase C (Pkc)-δ, a serine–threonine kinase, is ubiquitously expressed and involved in regulating cell death and proliferation. However, the role of Pkcδ in regulating glucagon secretion in pancreatic α-cells remains unclear. Therefore, this study aimed to elucidate the physiological role of Pkcδ in glucagon secretion from pancreatic α-cells. Glucagon secretions were investigated in Pkcδ-knockdown InR1G9 cells and pancreatic α-cell-specific Pkcδ-knockout (αPkcδKO) mice. Knockdown of Pkcδ in the glucagon-secreting cell line InR1G9 cells reduced glucagon secretion. The basic amino acid arginine enhances glucagon secretion via voltage-dependent calcium channels (VDCC). Furthermore, we showed that arginine increased Pkcδ phosphorylation at Thr505, which is critical for Pkcδ activation. Interestingly, the knockdown of Pkcδ in InR1G9 cells reduced arginine-induced glucagon secretion. Moreover, arginine-induced glucagon secretions were decreased in αPkcδKO mice and islets from αPkcδKO mice. Pkcδ is essential for arginine-induced glucagon secretion in pancreatic α-cells. Therefore, this study may contribute to the elucidation of the molecular mechanism of amino acid-induced glucagon secretion and the development of novel antidiabetic drugs targeting Pkcδ and glucagon.

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6

Chen, Zhuo, Jonathan J. Chen, and Rong Fan. "Single-Cell Protein Secretion Detection and Profiling." Annual Review of Analytical Chemistry 12, no. 1 (June 12, 2019): 431–49. http://dx.doi.org/10.1146/annurev-anchem-061318-115055.

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Secreted proteins play important roles in mediating various biological processes such as cell–cell communication, differentiation, migration, and homeostasis at the population or tissue level. Here, we review bioanalytical technologies and devices for detecting protein secretions from single cells. We begin by discussing conventional approaches followed by detailing the latest advances in microengineered systems for detecting single-cell protein secretions with an emphasis on multiplex measurement. These platforms include droplet microfluidics, micro-/nanowell-based assays, and microchamber-based assays, among which the advantages and limitations are compared. Microscale systems also enable the tracking of protein secretion dynamics in single cells, further empowering the study of the cell–cell communication network. Looking forward, we discuss the remaining challenges and future opportunities that will transform basic research of cellular secretion functions at the systems level and the clinical applications for immune monitoring and cancer treatment.

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7

Byun, Hyunjong, Jiyeon Park, Benedict U. Fabia, Joshua Bingwa, Mihn Hieu Nguyen, Haeshin Lee, and Jung Hoon Ahn. "Generalized Approach towards Secretion-Based Protein Production via Neutralization of Secretion-Preventing Cationic Substrate Residues." International Journal of Molecular Sciences 23, no. 12 (June 15, 2022): 6700. http://dx.doi.org/10.3390/ijms23126700.

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Many heterologous proteins can be secreted by bacterial ATP-binding cassette (ABC) transporters, provided that they are fused with the C-terminal signal sequence, but some proteins are not secretable even though they carry the right signal sequence. The invention of a method to secrete these non-secretable proteins would be valuable both for understanding the secretory physiology of ABC transporters and for industrial applications. Herein, we postulate that cationic “supercharged” regions within the target substrate protein block the secretion by ABC transporters. We also suggest that the secretion of such substrate proteins can be rescued by neutralizing those cationic supercharged regions via structure-preserving point mutageneses. Surface-protruding, non-structural cationic amino acids within the cationic supercharged regions were replaced by anionic or neutral hydrophilic amino acids, reducing the cationic charge density. The examples of rescued secretions we provide include the spike protein of SARS-CoV-2, glutathione-S-transferase, streptavidin, lipase, tyrosinase, cutinase, growth factors, etc. In summary, our study provides a method to predict the secretability and a tool to rescue the secretion by correcting the secretion-blocking regions, making a significant step in understanding the physiological properties of ABC transporter-dependent protein secretion and laying the foundation for the development of a secretion-based protein-producing platform.

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8

NAKANO, Akihiko. "Protein Secretion and GTP-binding Proteins." Seibutsu Butsuri 31, no. 2 (1991): 53–57. http://dx.doi.org/10.2142/biophys.31.53.

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9

Deng, Xiaoying, Dulce R. Guarita, Martha R. A. Pedroso, Christianna Kreiss, Paul G. Wood, Alan F. Sved, and David C. Whitcomb. "PYY inhibits CCK-stimulated pancreatic secretion through the area postrema in unanesthetized rats." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 281, no. 2 (August 1, 2001): R645—R653. http://dx.doi.org/10.1152/ajpregu.2001.281.2.r645.

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Peptide YY (PYY) inhibits CCK-8-secretin-stimulated pancreatic secretion in vivo. To investigate whether CCK-8-secretin-stimulated pancreatic secretion is mediated through a vago-vagal pathway and whether PYY inhibits this pathway through the area postrema (AP), chronic pancreatic, biliary, and duodenal catheters were implanted in AP-lesioned (APX) or sham-operated rats. The effects of APX on pancreatic secretion stimulated by bethanechol, pancreatic juice diversion (PJD), or CCK-8-secretin, were tested, with and without background PYY infusion, in unanesthetized rats. APX reduced basal pancreatic secretion by 15–20% ( P < 0.01). APX had no effect on bethanechol-stimulated secretion and potentiated protein secretion stimulated by PJD (396 vs. 284%) and exogenous CCK-8-secretin. In sham-operated rats, background PYY potently inhibited CCK-8-secretin-stimulated pancreatic fluid (1.8 vs. 48.2%) and protein secretion (3.7 vs. 45.8%) but potentiated fluid (52.9 vs. 43.1%) and protein (132.9 vs. 68.9%) secretion in APX rats. Our findings demonstrate that PYY inhibits CCK-8-secretin-stimulated pancreatic secretion through an AP-dependent mechanism in sham-operated rats. The AP also contributes to basal pancreatic secretion.

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10

Dumont, Mark E., Fred Sherman, and David Y. Thomas. "Protein targeting and protein secretion." Genome 31, no. 2 (January 15, 1989): 1109–10. http://dx.doi.org/10.1139/g89-199.

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11

Chard, Tim, and Jurgis Grudzinskas. "Pregnancy Protein Secretion." Seminars in Reproductive Medicine 10, no. 02 (May 1992): 61–71. http://dx.doi.org/10.1055/s-2007-1018862.

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12

Tame, Jeremy R. H. "Autotransporter protein secretion." BioMolecular Concepts 2, no. 6 (December 1, 2011): 525–36. http://dx.doi.org/10.1515/bmc.2011.045.

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AbstractAutotransporter proteins are a large family of virulence factors secreted from Gram-negative bacteria by a unique mechanism. First described in the 1980s, these proteins have a C-terminal region that folds into a β-barrel in the bacterial outer membrane. The so-called passenger domain attached to this barrel projects away from the cell surface and may be liberated from the cell by self-cleavage or surface proteases. Although the majority of passenger domains have a similar β-helical structure, they carry a variety of subdomains, allowing them to carry out widely differing functions related to pathogenesis. Considerable biochemical and structural characterisation of the barrel domain has shown that ‘autotransporters’ in fact require a conserved and essential protein complex in the outer membrane for correct folding. Although the globular domains of this complex projecting into the periplasmic space have also been structurally characterised, the overall secretion pathway of the autotransporters remains highly puzzling. It was presumed for many years that the passenger domain passed through the centre of the barrel domain to reach the cell surface, driven at least in part by folding. This picture is complicated by conflicting data, and there is currently little hard information on the true nature of the secretion intermediates. As well as their medical importance therefore, autotransporters are proving to be an excellent system to study the folding and membrane insertion of outer membrane proteins in general. This review focuses on structural aspects of autotransporters; their many functions in pathogenesis are beyond its scope.

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Sakaguchi, Masao. "Eukaryotic protein secretion." Current Opinion in Biotechnology 8, no. 5 (October 1997): 595–601. http://dx.doi.org/10.1016/s0958-1669(97)80035-3.

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14

Ding, Yu, Juan Wang, Junqi Wang, York-Dieter Stierhof, David G. Robinson, and Liwen Jiang. "Unconventional protein secretion." Trends in Plant Science 17, no. 10 (October 2012): 606–15. http://dx.doi.org/10.1016/j.tplants.2012.06.004.

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15

Alvaro, D., A. Mennone, and J. L. Boyer. "Role of kinases and phosphatases in the regulation of fluid secretion and Cl-/HCO3- exchange in cholangiocytes." American Journal of Physiology-Gastrointestinal and Liver Physiology 273, no. 2 (August 1, 1997): G303—G313. http://dx.doi.org/10.1152/ajpgi.1997.273.2.g303.

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The role of protein kinase A (PKA), protein kinase C (PKC), and protein phosphatases in the process of secretin stimulation of fluid and bicarbonate secretion from biliary epithelium was examined using a novel isolated bile duct unit (IBDU) model from rat liver. Sp-adenosine 3',5'-cyclic monophosphothiolate (Sp-cAMPS), 100 microM, a PKA-specific agonist, significantly increased secretion during a 30-min perfusion (+61%, P < 0.01). In contrast, preincubation and perfusion of Rp-cAMPS, 100 microM, a specific PKA inhibitor, reduced the ability of secretin to stimulate both fluid secretion (111 vs. 25%; P < 0.01) and Cl-/HCO3- exchanger activity (80 vs. 28%). Neither the PKC agonist phorbol 12-myristate 13-acetate, 10 microM, nor the PKC antagonist staurosporine showed any effect on either basal or secretin-stimulated fluid secretion or Cl-/HCO3- exchange activity in IBDU. Okadaic acid, a specific inhibitor of protein phosphatases 1 and 2A, also had no effect on basal fluid secretion or on the basal activity of the Cl-/HCO3- exchanger. However, okadaic acid resulted in persistence of secretion after removal of secretin, in contrast to the reduction in secretion observed in controls. These findings indicate that PKA but not PKC is involved in the signal transduction of secretin-stimulated fluid secretion and Cl-/HCO3- exchange activity in rat bile duct epithelium, a process inactivated by dephosphorylation by protein phosphatases 1 and/or 2A.

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16

Hueck, Christoph J. "Type III Protein Secretion Systems in Bacterial Pathogens of Animals and Plants." Microbiology and Molecular Biology Reviews 62, no. 2 (June 1, 1998): 379–433. http://dx.doi.org/10.1128/mmbr.62.2.379-433.1998.

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SUMMARY Various gram-negative animal and plant pathogens use a novel, sec-independent protein secretion system as a basic virulence mechanism. It is becoming increasingly clear that these so-called type III secretion systems inject (translocate) proteins into the cytosol of eukaryotic cells, where the translocated proteins facilitate bacterial pathogenesis by specifically interfering with host cell signal transduction and other cellular processes. Accordingly, some type III secretion systems are activated by bacterial contact with host cell surfaces. Individual type III secretion systems direct the secretion and translocation of a variety of unrelated proteins, which account for species-specific pathogenesis phenotypes. In contrast to the secreted virulence factors, most of the 15 to 20 membrane-associated proteins which constitute the type III secretion apparatus are conserved among different pathogens. Most of the inner membrane components of the type III secretion apparatus show additional homologies to flagellar biosynthetic proteins, while a conserved outer membrane factor is similar to secretins from type II and other secretion pathways. Structurally conserved chaperones which specifically bind to individual secreted proteins play an important role in type III protein secretion, apparently by preventing premature interactions of the secreted factors with other proteins. The genes encoding type III secretion systems are clustered, and various pieces of evidence suggest that these systems have been acquired by horizontal genetic transfer during evolution. Expression of type III secretion systems is coordinately regulated in response to host environmental stimuli by networks of transcription factors. This review comprises a comparison of the structure, function, regulation, and impact on host cells of the type III secretion systems in the animal pathogens Yersinia spp., Pseudomonas aeruginosa, Shigella flexneri, Salmonella typhimurium, enteropathogenic Escherichia coli, and Chlamydia spp. and the plant pathogens Pseudomonas syringae, Erwinia spp., Ralstonia solanacearum, Xanthomonas campestris, and Rhizobium spp.

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Gawin, A. Z., B. E. Emery, J. N. Baraniuk, and M. A. Kaliner. "Nasal glandular secretory response to cholinergic stimulation in humans and guinea pigs." Journal of Applied Physiology 71, no. 6 (December 1, 1991): 2460–68. http://dx.doi.org/10.1152/jappl.1991.71.6.2460.

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A guinea pig model of nasal secretory responses was developed to assess the contributions of vascular permeability and glandular secretion responsible for the production of cholinergically stimulated nasal secretions. The nasal secretory responses to provocation with saline, methacholine, and atropine on the ipsilateral (challenged) side and contralateral (reflex) side were analyzed by measurement of total protein (Lowry method), guinea pig albumin (enzyme-linked immunosorbent assay), 125I-labeled bovine serum albumin after intravenous injection, and alkaline phosphatase enzyme activity in nasal fluid. Alkaline phosphatase was found to be localized to submucosal glands by zymography. Topical methacholine challenge increased the secretion of total protein, alkaline phosphatase activity, and albumin on the ipsilateral challenged side, whereas the percentage of total protein represented by albumin was not increased. This response was totally prevented by atropine pretreatment. Serial provocation with methacholine resulted in progressively reduced amounts of both the total protein and alkaline phosphatase in secretions. The observation that repeated challenges produced progressively smaller responses was also examined employing human nasal provocation. Repeating methacholine (25 mg) challenges four times at 10-min intervals in six human volunteers revealed that the initial challenge produced the largest response as reflected in total protein, albumin, lysozyme, lactoferrin, immunoglobulin (Ig) G, IgA, and secretory IgA secretion. When the constituents in secretions were analyzed in relationship to the total protein, the two vascular proteins, IgG and albumin, demonstrated the greatest decrements with repeated methacholine challenges. The glandular proteins, lactoferrin, lysozyme, and secretory IgA, either remained constant or increased in their relative proportion to total protein. Thus, cholinergic stimulation causes glandular secretion from both the guinea pig and human nasal mucosa.(ABSTRACT TRUNCATED AT 250 WORDS)

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18

Busler, Valerie J., Victor J. Torres, Mark S. McClain, Oscar Tirado, David B. Friedman, and Timothy L. Cover. "Protein-Protein Interactions among Helicobacter pylori Cag Proteins." Journal of Bacteriology 188, no. 13 (July 1, 2006): 4787–800. http://dx.doi.org/10.1128/jb.00066-06.

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ABSTRACT Many Helicobacter pylori isolates contain a 40-kb region of chromosomal DNA known as the cag pathogenicity island (PAI). The risk for development of gastric cancer or peptic ulcer disease is higher among humans infected with cag PAI-positive H. pylori strains than among those infected with cag PAI-negative strains. The cag PAI encodes a type IV secretion system that translocates CagA into gastric epithelial cells. To identify Cag proteins that are expressed by H. pylori during growth in vitro, we compared the proteomes of a wild-type H. pylori strain and an isogenic cag PAI deletion mutant using two-dimensional difference gel electrophoresis (2D-DIGE) in multiple pH ranges. Seven Cag proteins were identified by this approach. We then used a yeast two-hybrid system to detect potential protein-protein interactions among 14 Cag proteins. One heterotypic interaction (CagY/7 with CagX/8) and two homotypic interactions (involving H. pylori VirB11/ATPase and Cag5) were similar to interactions previously reported to occur among homologous components of the Agrobacterium tumefaciens type IV secretion system. Other interactions involved Cag proteins that do not have known homologues in other bacterial species. Biochemical analysis confirmed selected interactions involving five of the proteins that were identified by 2D-DIGE. Protein-protein interactions among Cag proteins are likely to have an important role in the assembly of the H. pylori type IV secretion apparatus.

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Pugsley, Anthony P., Nicolas Bayan, and Nathalie Sauvonnet. "Disulfide Bond Formation in Secreton Component PulK Provides a Possible Explanation for the Role of DsbA in Pullulanase Secretion." Journal of Bacteriology 183, no. 4 (February 15, 2001): 1312–19. http://dx.doi.org/10.1128/jb.183.4.1312-1319.2001.

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ABSTRACT When expressed in Escherichia coli, the 15Klebsiella oxytoca pul genes that encode the so-called Pul secreton or type II secretion machinery promote pullulanase secretion and the assembly of one of the secreton components, PulG, into pili. Besides these pul genes, efficient pullulanase secretion also requires the host dsbA gene, encoding a periplasmic disulfide oxidoreductase, independently of disulfide bond formation in pullulanase itself. Two secreton components, the secretin pilot protein PulS and the minor pseudopilin PulK, were each shown to posses an intramolecular disulfide bond whose formation was catalyzed by DsbA. PulS was apparently destabilized by the absence of its disulfide bond, whereas PulK stability was not dramatically affected either by adsbA mutation or by the removal of one of its cysteines. The pullulanase secretion defect in a dsbA mutant was rectified by overproduction of PulK, indicating reduced disulfide bond formation in PulK as the major cause of the secretion defect under the conditions tested (in which PulS is probably present in considerable excess of requirements). PulG pilus formation was independent of DsbA, probably because PulK is not needed for piliation.

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Van Deventer, James A., Ryan L. Kelly, Saravanan Rajan, K. Dane Wittrup, and Sachdev S. Sidhu. "A switchable yeast display/secretion system." Protein Engineering Design and Selection 28, no. 10 (September 1, 2015): 317–25. http://dx.doi.org/10.1093/protein/gzv043.

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21

Stephens, Craig. "Protein secretion: Getting folded proteins across membranes." Current Biology 8, no. 16 (July 1998): R578—R581. http://dx.doi.org/10.1016/s0960-9822(07)00366-1.

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Henderson, Ian R., Renato Cappello, and James P. Nataro. "Autotransporter proteins, evolution and redefining protein secretion." Trends in Microbiology 8, no. 12 (December 2000): 529–32. http://dx.doi.org/10.1016/s0966-842x(00)01853-9.

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Van Ulsen, Peter, and Jan Tommassen. "Protein secretion and secreted proteins in pathogenicNeisseriaceae." FEMS Microbiology Reviews 30, no. 2 (March 2006): 292–319. http://dx.doi.org/10.1111/j.1574-6976.2006.00013.x.

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Jo, Y. H., Y. L. Lee, K. Y. Lee, T. M. Chang, and W. Y. Chey. "Neurohormonal mechanism of pancreatic exocrine secretion stimulated by sodium oleate and L-tryptophan in dogs." American Journal of Physiology-Gastrointestinal and Liver Physiology 263, no. 1 (July 1, 1992): G12—G16. http://dx.doi.org/10.1152/ajpgi.1992.263.1.g12.

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In the present investigation, we have studied the effect of atropine on the pancreatic secretion stimulated by intraduodenal administration of either sodium oleate or exogenous cholecystokinin (CCK). In four dogs prepared with gastric and Thomas duodenal cannulas, pancreatic juice was collected for measurement of volume, bicarbonate, and protein output, and peripheral venous blood samples were obtained for radioimmunoassay of both secretin and CCK. Volume, bicarbonate, and protein output of the pancreatic juice increased significantly in response to sodium oleate (1-4 mmol/h) in a dose-dependent manner. The increase in pancreatic secretion paralleled the increments in both plasma CCK and secretin. Atropine given intravenously suppressed completely both pancreatic secretion and release of CCK stimulated by sodium oleate, whereas the release of secretin was not affected. Pancreatic secretion was significantly increased in a dose-dependent manner by exogenous CCK octapeptide (CCK-8) at 16, 32, and 64 micrograms (14, 28, and 56 pmol).kg-1.h-1. Atropine inhibited protein output only partially, but it did not influence bicarbonate output. In five additional dogs, the effect of atropine on L-tryptophan-stimulated pancreatic secretion was studied. Interestingly, atropine failed to influence the CCK release and pancreatic secretion of volume and bicarbonate, except for protein secretion, which was significantly inhibited. It was shown previously that atropine inhibited significantly the pancreatic secretion of bicarbonate stimulated by secretin in physiological doses. Thus we conclude that the inhibition by atropine of the pancreatic exocrine secretion stimulated by sodium oleate is mediated by both suppression of CCK release and inhibition of action of secretin on the exocrine pancreas.(ABSTRACT TRUNCATED AT 250 WORDS)

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Uchida, Kaoru, Kohei Dono, and Shin-Ichi Aizawa. "Identification of the Key Sequence in the FliK C-Terminal Domain for Substrate Specificity Switching in the Flagellar Protein Secretion." Journal of Bacteriology 198, no. 3 (November 2, 2015): 410–15. http://dx.doi.org/10.1128/jb.00712-15.

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ABSTRACTThe flagellar hook is a short tubular structure located between the external filament and the membrane-bound basal body. The average hook length is 55 nm and is determined by the soluble protein FliK and the integral membrane protein FlhB. Hook elongation is terminated by FliK-mediated cessation of hook protein secretion, followed by the secretion of filamentous proteins. This process is referred to as the substrate specificity switch. Switching of the secretion modes results from a direct interaction between the FliK C-terminal domain (FliKC) and the secretion gate in FlhB. FliKCconsists of two α-helices and four β-strands. Loop 2 connects the first two β-sheets and contains a conserved sequence of 9 residues. Genetic and physiological analyses of variousfliKpartial deletion mutants pointed to loop 2 as essential for induction of a conformational change in the FlhB gate. We constructed single-amino-acid substitutions in the conserved region of loop 2 of FliK and discovered that the loop sequence LRL is essential for the timely switching of secretion modes.IMPORTANCEFlagellar protein secretion is controlled by the soluble protein FliK. We discovered that the loop 2 sequence LRL in the FliK C terminus was essential for timely switching of secretion modes. This mechanism is applicable to type three secretions systems that secrete virulence factors in bacterial pathogens.

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Zhang, Jing, Yongxiang Wang, Shuwen Fu, Quan Yuan, Qianru Wang, Ningshao Xia, Yumei Wen, Jisu Li, and Shuping Tong. "Role of Small Envelope Protein in Sustaining the Intracellular and Extracellular Levels of Hepatitis B Virus Large and Middle Envelope Proteins." Viruses 13, no. 4 (April 2, 2021): 613. http://dx.doi.org/10.3390/v13040613.

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Hepatitis B virus (HBV) expresses co-terminal large (L), middle (M), and small (S) envelope proteins. S protein drives virion and subviral particle secretion, whereas L protein inhibits subviral particle secretion but coordinates virion morphogenesis. We previously found that preventing S protein expression from a subgenomic construct eliminated M protein. The present study further examined impact of S protein on L and M proteins. Mutations were introduced to subgenomic construct of genotype A or 1.1 mer replication construct of genotype A or D, and viral proteins were analyzed from transfected Huh7 cells. Mutating S gene ATG to prevent expression of full-length S protein eliminated M protein, reduced intracellular level of L protein despite its blocked secretion, and generated a truncated S protein through translation initiation from a downstream ATG. Truncated S protein was secretion deficient and could inhibit secretion of L, M, S proteins from wild-type constructs. Providing full-length S protein in trans rescued L protein secretion and increased its intracellular level from mutants of lost S gene ATG. Lost core protein expression reduced all the three envelope proteins. In conclusion, full-length S protein could sustain intracellular and extracellular L and M proteins, while truncated S protein could block subviral particle secretion.

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Hamilton, Jaeger J., Victoria L. Marlow, Richard A. Owen, Marília de Assis Alcoforado Costa, Manman Guo, Grant Buchanan, Govind Chandra, et al. "A holin and an endopeptidase are essential for chitinolytic protein secretion in Serratia marcescens." Journal of Cell Biology 207, no. 5 (December 8, 2014): 615–26. http://dx.doi.org/10.1083/jcb.201404127.

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Pathogenic bacteria adapt to their environment and manipulate the biochemistry of hosts by secretion of effector molecules. Serratia marcescens is an opportunistic pathogen associated with healthcare-acquired infections and is a prolific secretor of proteins, including three chitinases (ChiA, ChiB, and ChiC) and a chitin binding protein (Cbp21). In this work, genetic, biochemical, and proteomic approaches identified genes that were required for secretion of all three chitinases and Cbp21. A genetic screen identified a holin-like protein (ChiW) and a putative l-alanyl-d-glutamate endopeptidase (ChiX), and subsequent biochemical analyses established that both were required for nonlytic secretion of the entire chitinolytic machinery, with chitinase secretion being blocked at a late stage in the mutants. In addition, live-cell imaging experiments demonstrated bimodal and coordinated expression of chiX and chiA and revealed that cells expressing chiA remained viable. It is proposed that ChiW and ChiX operate in tandem as components of a protein secretion system used by gram-negative bacteria.

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Hashimoto, Y., N. Koyabu, and T. Imoto. "Effects of signal sequences on the secretion of hen lysozyme by yeast: construction of four secretion cassette vectors." Protein Engineering Design and Selection 11, no. 2 (February 1, 1998): 75–77. http://dx.doi.org/10.1093/protein/11.2.75.

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29

Tommassen, Jan, Alain Filloux, Marc Bally, Maryse Murgier, and AndrÃ©e Lazdunski. "Protein secretion inPseudomonas aeruginosa." FEMS Microbiology Letters 103, no. 1 (September 1992): 73–90. http://dx.doi.org/10.1111/j.1574-6968.1992.tb05824.x.

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30

Morosoli, R., F. Shareck, and D. Kluepfel. "Protein secretion in streptomycetes." FEMS Microbiology Letters 146, no. 2 (January 17, 2006): 167–74. http://dx.doi.org/10.1111/j.1574-6968.1997.tb10188.x.

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31

Marshall, J. "Inner Workings: Protein secretion." Proceedings of the National Academy of Sciences 111, no. 25 (June 24, 2014): 9021. http://dx.doi.org/10.1073/pnas.1410308111.

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32

Liu, Xiuxia, Wei Zhang, Zihao Zhao, Xiaofeng Dai, Yankun Yang, and Zhonghu Bai. "Protein secretion inCorynebacterium glutamicum." Critical Reviews in Biotechnology 37, no. 4 (October 13, 2016): 541–51. http://dx.doi.org/10.1080/07388551.2016.1206059.

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33

Thiele, Christoph, Hans-Hermann Gerdes, and Wieland B. Huttner. "Protein secretion: Puzzling receptors." Current Biology 7, no. 8 (August 1997): R496—R500. http://dx.doi.org/10.1016/s0960-9822(06)00247-8.

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Thiele, C., H. H. Gerdes, and W. B. Huttner. "Protein secretion: Puzzling receptors." Current Biology 8, no. 2 (January 1998): R41. http://dx.doi.org/10.1016/s0960-9822(98)70028-4.

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Loh, Y. Peng. "Protein secretion: Puzzling receptors." Current Biology 8, no. 2 (January 1998): R41. http://dx.doi.org/10.1016/s0960-9822(98)70029-6.

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36

Vella, F. "Protein Targeting and Secretion." Biochemical Education 20, no. 2 (April 1992): 121–22. http://dx.doi.org/10.1016/0307-4412(92)90131-5.

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37

Cavalli, Giulio, and Simone Cenci. "Autophagy and Protein Secretion." Journal of Molecular Biology 432, no. 8 (April 2020): 2525–45. http://dx.doi.org/10.1016/j.jmb.2020.01.015.

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38

Udaka, Shigezo, and Hideo Yamagata. "Protein secretion inBacillus brevis." Antonie van Leeuwenhoek 64, no. 2 (1994): 137–43. http://dx.doi.org/10.1007/bf00873023.

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JONES, RUSSELL L., and DAVID G. ROBINSON. "Protein secretion in plants." New Phytologist 111, no. 4 (April 1989): 567–97. http://dx.doi.org/10.1111/j.1469-8137.1989.tb02352.x.

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40

Gennity, Joseph M., and Masayori Inouye. "Protein secretion in bacteria." Current Opinion in Biotechnology 2, no. 5 (October 1991): 661–67. http://dx.doi.org/10.1016/0958-1669(91)90031-y.

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41

Hegyi, Péter, Zoltán Rakonczay, László Tiszlavicz, András Varró, András Tóth, Gábor Rácz, Gábor Varga, Michael A. Gray, and Barry E. Argent. "Protein kinase C mediates the inhibitory effect of substance P on HCO3− secretion from guinea pig pancreatic ducts." American Journal of Physiology-Cell Physiology 288, no. 5 (May 2005): C1030—C1041. http://dx.doi.org/10.1152/ajpcell.00430.2003.

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The inhibitory control of pancreatic ductal HCO3− secretion may be physiologically important in terms of limiting the hydrostatic pressure developed within the ducts and in terms of switching off pancreatic secretion after a meal. Substance P (SP) inhibits secretin-stimulated HCO3− secretion by modulating a Cl−-dependent HCO3− efflux step at the apical membrane of the duct cell (Hegyi P, Gray MA, and Argent BE. Am J Physiol Cell Physiol 285: C268–C276, 2003). In the present study, we have shown that SP is present in periductal nerves within the guinea pig pancreas, that PKC mediates the effect of SP, and that SP inhibits an anion exchanger on the luminal membrane of the duct cell. Secretin (10 nM) stimulated HCO3− secretion by sealed, nonperfused, ducts about threefold, and this effect was totally inhibited by SP (20 nM). Phorbol 12,13-dibutyrate (PDBu; 100 nM), an activator of PKC, reduced basal HCO3− secretion by ∼40% and totally blocked secretin-stimulated secretion. In addition, bisindolylmaleimide I (1 nM to 1 μM), an inhibitor of PKC, relieved the inhibitory effect of SP on secretin-stimulated HCO3− secretion and also reversed the inhibitory effect of PDBu. Western blot analysis revealed that guinea pig pancreatic ducts express the α-, βI-, δ-, ε-, η-, θ-, ζ-, and μ-isoforms of PKC. In microperfused ducts, luminal H2DIDS (0.5 mM) caused intracellular pH to alkalinize and, like SP, inhibited basal and secretin-stimulated HCO3− secretion. SP did not inhibit secretion further when H2DIDS was present in the lumen, suggesting that SP and H2DIDS both inhibit the activity of an anion exchanger on the luminal membrane of the duct cell.

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Miura, Natsuko, and Mitsuyoshi Ueda. "Evaluation of Unconventional Protein Secretion by Saccharomyces cerevisiae and other Fungi." Cells 7, no. 9 (August 31, 2018): 128. http://dx.doi.org/10.3390/cells7090128.

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Development of proteome analysis of extracellular proteins has revealed that a wide variety of proteins, including fungal allergens are present outside the cell. These secreted allergens often do not contain known secretion signal sequences. Recent research progress shows that some fungal allergens are secreted by unconventional secretion pathways, including autophagy- and extracellular-vesicle-dependent pathways. However, secretion pathways remain unknown for the majority of extracellular proteins. This review summarizes recent data on unconventional protein secretion in Saccharomyces cerevisiae and other fungi. Particularly, methods for evaluating unconventional protein secretion are proposed for fungal species, including S. cerevisiae, a popular model organism for investigating protein secretion pathways.

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Souza, S. A. de, and A. M. Leal-Zanchet. "Histological and histochemical characterization of the secretory cells of Choeradoplana iheringi Graff, 1899 (Platyhelminthes: Tricladida: Terricola)." Brazilian Journal of Biology 64, no. 3a (August 2004): 511–22. http://dx.doi.org/10.1590/s1519-69842004000300014.

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The present study aims at providing a detailed description of the histology, as well as the first histochemical characterization, of the secretory cells of the epidermis, pharynx, and copulatory organs of Choeradoplana iheringi, in order to give further support to studies on the physiology of these organs. The secretory cells are distinguished on the basis of secretion morphology and its staining properties, using trichrome methods and histochemical reactions. Four cell types open through the epidermis of Ch. iheringi, three of them secreting basic protein and a fourth containing glycosaminoglycan mucins. The epidermal lining cells store glycogen. In the pharynx, four secretory cell types were distinguished. Two types produce glycoprotein, a third type secretes basic protein, and another one produces glycosaminoglycan mucins. In the male copulatory organs, the prostatic vesicle receives four secretory cell types containing basic protein, except for one type which produces glycoprotein. The two secretory cell types opening into the male atrium secrete, respectively, glycoprotein, and glycosaminoglycan mucins. In the female copulatory organs, the female atrium and its proximal diverticulum, the vagina, receive two types of secretory cells producing, respectively, basic protein and glycosaminoglycan mucins. Another secretory cell type constitutes the so-called shell glands which open into the common glandular duct, secreting basic protein. The lining cells of the male and female atria produce a mucous secretion containing glycosaminoglycans. In addition, the lining epithelium of the female atrium presents an apical secretion of a proteic nature. The occurrence of a kind of spermatophore is reported for the first time for a species of Choeradoplana. This structure is located in the male or female atria in different specimens, and characterized by erythrophil, xanthophil, and/or mixed secretions associated with sperm.

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Park, Yoonsuk, and Richard J. Lamont. "Contact-Dependent Protein Secretion inPorphyromonas gingivalis." Infection and Immunity 66, no. 10 (October 1, 1998): 4777–82. http://dx.doi.org/10.1128/iai.66.10.4777-4782.1998.

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ABSTRACT Porphyromonas gingivalis can induce its uptake by host epithelial cells; however, the nature and role of the P. gingivalis molecules involved in this invasion process have yet to be determined. In this study, modulation of secreted P. gingivalis proteins following association with gingival epithelial cells was investigated. Western immunoblot analysis showed that contact with epithelial cells or epithelial cell growth media induces P. gingivalis 33277 to secrete several proteins with molecular masses between 35 and 95 kDa. Secretion of the Arg-gingipain and Lys-gingipain proteases was repressed under these conditions. The contact-induced secreted protein profile was altered in Arg-gingipain-deficient and Lys-gingipain-deficient mutants, indicating a possible role for these proteases in the secretion pathway. TheP. gingivalis contact-dependent protein secretion pathway differs to some extent from type III protein secretion pathways in enteric pathogens, as a gene homologous to the invA family genes was not detected in P. gingivalis. The secreted proteins of P. gingivalis may play a role in the interactions of the organism with host cells.

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Moughan, Paul J., Malcolm F. Fuller, Kyoung-Sik Han, Arie K. Kies, and Warren Miner-Williams. "Food-Derived Bioactive Peptides Influence Gut Function." International Journal of Sport Nutrition and Exercise Metabolism 17, s1 (February 2007): S5—S22. http://dx.doi.org/10.1123/ijsnem.17.s1.s5.

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Bioactive peptides either present in foods or released from food proteins during digestion have a wide range of physiological effects, including on gut function. Many of the bioactive peptides characterized to date that influence gut motility, secretion, and absorption are opioid agonists or antagonists. The authors review a body of experimental evidence that demonstrates an effect of peptides from food proteins on endogenous (nondietary) protein flow at the terminal ileum of simple-stomached mammals, including adult humans. At least some dietary peptides (1000-5000 Da) significantly enhance the loss of protein from the small intestine, causing an increased amount of protein to enter the colon. Food-derived peptides appear to either stimulate protein secretion into the gut lumen or inhibit amino acid reabsorption or influence both processes simultaneously. The effect of dietary peptides on small-intestine secretory-protein dynamics is discussed in the context of the major components of gut endogenous protein, sloughed cells, enzymatic secretions, mucin, and bacterial protein.

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Takacs, Michelle, Olga V. Makhlynets, Patricia L. Tolbert, and Ivan V. Korendovych. "Secretion of functional formate dehydrogenase in Pichia pastoris." Protein Engineering, Design and Selection 30, no. 3 (February 15, 2017): 279–84. http://dx.doi.org/10.1093/protein/gzx010.

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47

Konturek, S. J., W. Pawlik, K. Czarnobilski, P. Gustaw, J. Jaworek, G. Beck, and H. Jendralla. "Effects of leukotriene C4 on pancreatic secretion and circulation in dogs." American Journal of Physiology-Gastrointestinal and Liver Physiology 254, no. 6 (June 1, 1988): G849—G855. http://dx.doi.org/10.1152/ajpgi.1988.254.6.g849.

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In the present study the effects of leukotriene C4 (LTC4) on exocrine pancreatic secretion and pancreatic blood flow were determined. LTC4 given intravenously in various doses ranging from 0.35 to 2.8 nmol.kg-1.h-1 in conscious dogs caused a dose-dependent inhibition of pancreatic HCO-3 and protein responses to exogenous hormones such as secretin, cholecystokinin octapeptide (CCK-8), and bombesin and to endogenous stimulants including meat feeding and duodenal perfusion with oleate. In tests with pancreatic secretion induced by secretin plus CCK, maximal inhibition by LTC4 occurred at a dose of 1.4 nmol.kg-1.h-1 and reached approximately 70% of the control value for HCO-3 output and 45% for protein output. In tests with separate secretin- or CCK-induced secretion, maximal inhibition occurred at a dose of 1.4 nmol.kg-1.h-1 and reached 38 and 66% of the control HCO-3 and protein secretion, respectively. The same dose of LTC4 reduced the postprandial HCO-3 secretion by approximately 80% and protein output by approximately 70%. After administration of indomethacin, the pancreatic secretion declined, but the inhibitory effects of LTC4 remained unchanged. Pancreatic tissue generated two to three times more LTC4 than the gastrointestinal mucosa, and indomethacin caused further increase in this generation, suggesting that LTC4 may contribute to indomethacin-induced pancreatic inhibition. (ABSTRACT TRUNCATED AT 250 WORDS)

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48

Henderson, Ian R., Renato Cappello, and James P. Nataro. "Autotransporter proteins, evolution and redefining protein secretion: Response." Trends in Microbiology 8, no. 12 (December 2000): 534–35. http://dx.doi.org/10.1016/s0966-842x(00)01884-9.

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Jacob-Dubuisson, Françoise, Rudy Antoine, and Camille Locht. "Autotransporter proteins, evolution and redefining protein secretion: Response." Trends in Microbiology 8, no. 12 (December 2000): 533–34. http://dx.doi.org/10.1016/s0966-842x(00)01885-0.

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50

Turner, MD, ME Rennison, SE Handel, CJ Wilde, and RD Burgoyne. "Proteins are secreted by both constitutive and regulated secretory pathways in lactating mouse mammary epithelial cells." Journal of Cell Biology 117, no. 2 (April 15, 1992): 269–78. http://dx.doi.org/10.1083/jcb.117.2.269.

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Lactating mammary epithelial cells secrete high levels of caseins and other milk proteins. The extent to which protein secretion from these cells occurs in a regulated fashion was examined in experiments on secretory acini isolated from the mammary glands of lactating mice at 10 d postpartum. Protein synthesis and secretion were assayed by following the incorporation or release, respectively, of [35S]methionine-labeled TCA-precipitable protein. The isolated cells incorporated [35S]methionine into protein linearly for at least 5 h with no discernible lag period. In contrast, protein secretion was only detectable after a lag of approximately 1 h, consistent with exocytotic secretion of proteins immediately after passage through the secretory pathway and package into secretory vesicles. The extent of protein secretion was unaffected by the phorbol ester PMA, 8-bromo-cAMP, or 8-bromo-cGMP but was doubled by the Ca2+ ionophore ionomycin. In a pulse-label protocol in which proteins were prelabeled for 1 h before a chase period, constitutive secretion was unaffected by depletion of cytosolic Ca2+ but ionomycin was found to give a twofold stimulation of the secretion of presynthesized protein in a Ca(2+)-dependent manner. Ionomycin was still able to stimulate protein secretion after constitutive secretion had terminated. These results suggest that lactating mammary cells possess both a Ca(2+)-independent constitutive pathway and a Ca(2+)-activated regulatory pathway for protein secretion. The same proteins were secreted by both pathways. No ultrastructural evidence for apocrine secretion was seen in response to ionomycin and so it appears that regulated casein release involves exocytosis. Ionomycin was unlikely to be acting by disassembling the cortical actin network since cytochalasin D did not mimic its effects on secretion. The regulated pathway may be controlled by Ca2+ acting at a late step such as exocytotic membrane fusion.

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