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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1989-8-18
|
| pubmed:abstractText |
We have characterized the induction of glucose-regulated proteins (GRPs) in Xenopus laevis A6 cells, a kidney epithelial cell line. Exposure of A6 cells to medium in which 2-deoxyglucose replaced galactose resulted in enhanced synthesis of two proteins at 78 and 98 kd. The 78 kd protein was determined by two-dimensional PAGE to consist of two isoelectric variants with pls of 5.3 and 5.2 whereas the 98 kd protein resolved into a single spot with a pl of 5.1. The 78 kd protein cross-reacted with antiserum against chicken GRP78 (glucose-regulated protein), suggesting that the Xenopus protein shares homology with a previously characterized GRP. This was supported by the finding that a rat GRP78 probe hybridized with a 2-deoxyglucose-inducible mRNA. Synthesis of the two proteins was also induced by tunicamycin, 2-deoxygalactose, and dithiothreitol. However, the GRPs were not induced by glucosamine or calcium ionophore A23187 at concentrations and exposure periods that have previously been shown to elicit a GRP response in mammalian and avian cells. Enhanced synthesis of the two GRPs by 2-deoxyglucose was transient, reaching maximal levels by 12-24 h and decreasing to near control levels by 48 h. Removal of the stress at the point of peak synthesis resulted in decreased synthesis of both proteins within 6 h and a return to control levels within 24 h of recovery. These data suggest that Xenopus cells have a GRP response that is similar, but not identical, to that found in mammalian cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Deoxyglucose,
http://linkedlifedata.com/resource/pubmed/chemical/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Fucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin,
http://linkedlifedata.com/resource/pubmed/chemical/glucose-regulated proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0021-9541
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
140
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
239-45
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2501316-Animals,
pubmed-meshheading:2501316-Calcimycin,
pubmed-meshheading:2501316-Cell Line,
pubmed-meshheading:2501316-Deoxyglucose,
pubmed-meshheading:2501316-Dithiothreitol,
pubmed-meshheading:2501316-Dose-Response Relationship, Drug,
pubmed-meshheading:2501316-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:2501316-Epithelial Cells,
pubmed-meshheading:2501316-Epithelium,
pubmed-meshheading:2501316-Fucose,
pubmed-meshheading:2501316-Gene Expression Regulation,
pubmed-meshheading:2501316-Glucosamine,
pubmed-meshheading:2501316-HSP70 Heat-Shock Proteins,
pubmed-meshheading:2501316-Immunoblotting,
pubmed-meshheading:2501316-Kidney,
pubmed-meshheading:2501316-Membrane Proteins,
pubmed-meshheading:2501316-Nucleic Acid Hybridization,
pubmed-meshheading:2501316-Tunicamycin,
pubmed-meshheading:2501316-Xenopus laevis
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Induction of glucose-regulated proteins in Xenopus laevis A6 cells.
|
| pubmed:affiliation |
Department of Biology, University of Waterloo, Ontario, Canada.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|