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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1997-1-31
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pubmed:abstractText |
We tested the hypothesis that the constitutive glucose transporter (GLUT1) in 3T3-L1 adipocytes belongs to the family of glucose-regulated proteins which are transcriptionally regulated by glucose deprivation. Using cDNA probes for both GRP78 (BiP) and GLUT1, we show that the level of GRP78 mRNA increased by 15-fold within 24 h of glucose deprivation with little change in GLUT1 mRNA. The elevated GRP78 mRNA in turn led to a time-dependent increase in GRP78 protein. While glucose deprivation did not alter the expression of the normal glycoform of GLUT1, a lower molecular weight glycoform accumulated with extended deprivation. Mannose and fructose, but not galactose, prevented the induction of GRP78 and accumulation of the abnormal GLUT1. Because GRP78 acts as a chaperone in other cell systems, we also sought evidence to support this activity in 3T3-L1 adipocytes. Using the technique of co-immunoprecipitation, we demonstrate that GRP78 bound several proteins unique to the glucose-deprived state. No deprivation-specific proteins could be detected in association with GLUT1. These data lead us to conclude that GLUT1 does not display characteristics of the glucose-regulated proteins, at least in 3T3-L1 adipocytes, a widely used model for differentiation, hormone action, and nutrient control. However, the mechanisms for activating traditional members of this family appear intact.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 1,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Slc2a1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin,
http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0300-8177
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
162
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
51-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8905625-3T3 Cells,
pubmed-meshheading:8905625-Adipocytes,
pubmed-meshheading:8905625-Animals,
pubmed-meshheading:8905625-Carrier Proteins,
pubmed-meshheading:8905625-DNA, Complementary,
pubmed-meshheading:8905625-Gene Expression Regulation,
pubmed-meshheading:8905625-Glucose,
pubmed-meshheading:8905625-Glucose Transporter Type 1,
pubmed-meshheading:8905625-Glycosylation,
pubmed-meshheading:8905625-Heat-Shock Proteins,
pubmed-meshheading:8905625-Mice,
pubmed-meshheading:8905625-Molecular Chaperones,
pubmed-meshheading:8905625-Monosaccharide Transport Proteins,
pubmed-meshheading:8905625-RNA, Messenger,
pubmed-meshheading:8905625-Tunicamycin
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pubmed:year |
1996
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pubmed:articleTitle |
Differential regulation of GRP78 and GLUT1 expression in 3T3-L1 adipocytes.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Florida, Gainesville 32610, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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