Source:http://linkedlifedata.com/resource/pubmed/id/21585341
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2011-7-28
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pubmed:abstractText |
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, Ca(2+) and the Ca(2+) carrier ionomycin, lysosomotropic NH(4)Cl, the G-protein activator GTP?S 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.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AKR1B10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1470-8728
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pubmed:author | |
pubmed:copyrightInfo |
© The Authors Journal compilation © 2011 Biochemical Society
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
438
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
71-80
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pubmed:meshHeading |
pubmed-meshheading:21585341-Adenocarcinoma,
pubmed-meshheading:21585341-Adenosine Triphosphate,
pubmed-meshheading:21585341-Aldehyde Reductase,
pubmed-meshheading:21585341-Blotting, Western,
pubmed-meshheading:21585341-Breast Neoplasms,
pubmed-meshheading:21585341-Calcium,
pubmed-meshheading:21585341-Carcinoma, Basal Cell,
pubmed-meshheading:21585341-Colorectal Neoplasms,
pubmed-meshheading:21585341-Culture Media,
pubmed-meshheading:21585341-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:21585341-Exocytosis,
pubmed-meshheading:21585341-Female,
pubmed-meshheading:21585341-Humans,
pubmed-meshheading:21585341-Immunoenzyme Techniques,
pubmed-meshheading:21585341-Intestines,
pubmed-meshheading:21585341-Kidney,
pubmed-meshheading:21585341-Lysosomes
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pubmed:year |
2011
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pubmed:articleTitle |
Aldo-keto reductase family 1, member B10 is secreted through a lysosome-mediated non-classical pathway.
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pubmed:affiliation |
Department of Medical Microbiology, Immunology, & Cell Biology, Simmons Cancer Institute, Southern Illinois University School of Medicine, 913 N. Rutledge Street, Springfield, IL 62794, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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