Aldo-keto reductase family 1, member B10 is secreted through a lysosome-mediated non-classical pathway

2011 ◽  
Vol 438 (1) ◽  
pp. 71-80 ◽  
Author(s):  
Di-xian Luo ◽  
Mei C. Huang ◽  
Jun Ma ◽  
Zachary Gao ◽  
Duan-fang Liao ◽  
...  
Keyword(s):  
G Protein ◽  
Protein Secretion ◽  
Cultured Cells ◽  
Sandwich Elisa ◽  
Acid Methyl Ester ◽  
Protein Synthesis Inhibitor ◽  
Classical Pathway ◽  
Synthesis Inhibitor ◽  
Secretion Pathway ◽  
Protein Secretion Pathway

AKR1B10 (aldo-keto reductase family 1, member B10) protein is primarily expressed in normal human small intestine and colon, but overexpressed in several types of human cancers and considered as a tumour marker. In the present study, we found that AKR1B10 protein is secreted from normal intestinal epithelium and cultured cancer cells, as detected by a newly developed sandwich ELISA and Western blotting. The secretion of AKR1B10 was not affected by the protein-synthesis inhibitor cycloheximide and the classical protein-secretion pathway inhibitor brefeldin A, but was stimulated by temperature, ATP, Ca2+ and the Ca2+ carrier ionomycin, lysosomotropic NH4Cl, the G-protein activator GTPγS and the G-protein coupling receptor N-formylmethionyl-leucyl-phenylalanine. The ADP-ribosylation factor inhibitor 2-(4-fluorobenzoylamino)-benzoic acid methyl ester and the phospholipase C inhibitor U73122 inhibited the secretion of AKR1B10. In cultured cells, AKR1B10 was present in lysosomes and was secreted with cathepsin D, a lysosomal marker. In the intestine, AKR1B10 was specifically expressed in mature epithelial cells and secreted into the lumen at 188.6–535.7 ng/ml of ileal fluids (mean=298.1 ng/ml, n=11). Taken together, our results demonstrate that AKR1B10 is a new secretory protein belonging to a lysosome-mediated non-classical protein-secretion pathway and is a potential serum marker.

A signal peptide-independent protein secretion pathway

1992 ◽  
Vol 61 (2) ◽  
pp. 111-113 ◽  
Author(s):  
C�cile Wandersman ◽  
Philippe Delepelaire ◽  
Sylvie Letoffe ◽  
Jean-Marc Ghigo
Keyword(s):  
Protein Secretion ◽  
Signal Peptide ◽  
Secretion Pathway ◽  
Protein Secretion Pathway ◽  
Independent Protein

scholarly journals Mutations in the Extracellular Protein Secretion Pathway Genes (eps) Interfere with Rugose Polysaccharide Production in and Motility of Vibrio cholerae

2000 ◽  
Vol 68 (4) ◽  
pp. 1967-1974 ◽  
Author(s):  
Afsar Ali ◽  
Judith A. Johnson ◽  
Augusto A. Franco ◽  
Daniel J. Metzger ◽  
Terry D. Connell ◽  
...  
Keyword(s):  
Vibrio Cholerae ◽  
Protein Secretion ◽  
Diarrheal Disease ◽  
Extracellular Protein ◽  
Aquatic Environments ◽  
Wild Type ◽  
Causal Organism ◽  
Secretion Pathway ◽  
Protein Secretion System ◽  
Protein Secretion Pathway

ABSTRACT Vibrio cholerae is the causal organism of the diarrheal disease cholera. The rugose variant of V. cholerae is associated with the secretion of an exopolysaccharide. The rugose polysaccharide has been shown to confer increased resistance to a variety of agents, such as chlorine, bioacids, and oxidative and osmotic stresses. It also promotes biofilm formation, thereby increasing the survival of the bacteria in the aquatic environments. Here we show that the extracellular protein secretion system (gene designated eps) is involved directly or indirectly in the production of rugose polysaccharide. A TnphoA insertion inepsD gene of the eps operon abolished the production of rugose polysaccharide, reduced the secretion of cholera toxin and hemolysin, and resulted in a nonmotile phenotype. We have constructed defined mutations of the epsD andepsE genes that affected these phenotypes and complemented these defects by plasmid clones of the respective wild-type genes. These results suggest a major role for the eps system in pathogenesis and environmental survival of V. cholerae.

scholarly journals Specific Chaperones for the Type VII Protein Secretion Pathway

2012 ◽  
Vol 287 (38) ◽  
pp. 31939-31947 ◽  
Author(s):  
Maria H. Daleke ◽  
Aniek D. van der Woude ◽  
Annabel H. A. Parret ◽  
Roy Ummels ◽  
A. Marit de Groot ◽  
...  
Keyword(s):  
Protein Secretion ◽  
Secretion Pathway ◽  
Protein Secretion Pathway

scholarly journals Surrogate Antigen Processing Mediated by TAP-dependent Antigenic Peptide Secretion

1998 ◽  
Vol 140 (1) ◽  
pp. 17-27 ◽  
Author(s):  
Reinhard Gabathuler ◽  
Judie Alimonti ◽  
Qian-Jin Zhang ◽  
Gerassimos Kolaitis ◽  
Gregor Reid ◽  
...  
Keyword(s):  
Mhc Class I ◽  
Antigen Processing ◽  
Brefeldin A ◽  
Class I ◽  
Protein Synthesis Inhibitor ◽  
Functional Assay ◽  
Synthesis Inhibitor ◽  
Secretion Pathway ◽  
Peptide Secretion ◽  
Mhc Class I Molecules

MHC class I proteins assemble with peptides in the ER. The peptides are predominantly generated from cytoplasmic proteins, probably by the action of the proteasome, a multicatalytic proteinase complex. Peptides are translocated into the ER by the transporters associated with antigen processing (TAP), and bind to the MHC class I molecules before transport to the cell surface. Here, we use a new functional assay to demonstrate that peptides derived from vesicular stomatitis virus nucleoprotein (VSV-N) antigen are actively secreted from cells. This secretion pathway is dependent on the expression of TAP transporters, but is independent of the MHC genotype of the donor cells. Furthermore, the expression and transport of MHC class I molecules is not required. This novel pathway is sensitive to the protein secretion inhibitors brefeldin A (BFA) and a temperature block at 21°C, and is also inhibited by the metabolic poison, azide, and the protein synthesis inhibitor, emetine. These data support the existence of a novel form of peptide secretion that uses the TAP transporters, as opposed to the ER translocon, to gain access to the secretion pathway. Finally, we suggest that this release of peptides in the vicinity of uninfected cells, which we term surrogate antigen processing, could contribute to various immune and secretory phenomena.

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