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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
16
|
| pubmed:dateCreated |
1991-7-1
|
| pubmed:abstractText |
We studied the structure and function of the human insulin receptor (IR) and a mutant which lacked the last 43 amino acids of the beta-subunit (IR delta ct). This deletion removed tyrosine (Tyr1322, Tyr1316) and threonine (Thr1336) phosphorylation sites. In Chinese hamster ovary (CHO) cells, insulin binding to the mutant receptor was normal, and [35S]methionine labeling indicated that both the IR and IR delta ct were processed normally; however, the beta-subunit of IR delta ct was 5 kDa smaller than that of the IR. The time course of insulin-stimulated autophosphorylation of the partially purified IR delta ct was normal, but the maximum autophosphorylation was reduced 20-30%. Tryptic phosphopeptide mapping confirmed the absence of the C-terminal phosphorylation sites and indicated that phosphorylation of the regulatory region (Tyr1146, Tyr1150, Tyr1151) occurred normally; kinase activity of the IR and IR delta ct was activated normally by insulin-stimulated autophosphorylation. In the intact CHO cells, insulin-stimulated serine and threonine phosphorylation of the IR delta ct was reduced 20%, suggesting that most Ser/Thr phosphorylation sites are located outside of the C terminus. During insulin stimulation, the wild-type and mutant insulin receptor activated the phosphatidylinositol 3-kinase. Moreover, insulin itself or human-specific anti-insulin receptor antibodies stimulated glycogen and DNA synthesis equally in both CHO/IR and CHO/IR delta ct cells. These data suggest that the C terminus plays a minimal role in IR function and signal transmission in CHO cells.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-Phosphatidylinositol 4-Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
266
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
10616-23
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:1645354-1-Phosphatidylinositol 4-Kinase,
pubmed-meshheading:1645354-Animals,
pubmed-meshheading:1645354-Autoradiography,
pubmed-meshheading:1645354-Chromatography, High Pressure Liquid,
pubmed-meshheading:1645354-Cricetinae,
pubmed-meshheading:1645354-Cricetulus,
pubmed-meshheading:1645354-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1645354-Female,
pubmed-meshheading:1645354-Glycogen,
pubmed-meshheading:1645354-Humans,
pubmed-meshheading:1645354-Mutation,
pubmed-meshheading:1645354-Ovary,
pubmed-meshheading:1645354-Peptide Mapping,
pubmed-meshheading:1645354-Phosphorylation,
pubmed-meshheading:1645354-Phosphotransferases,
pubmed-meshheading:1645354-Receptor, Insulin,
pubmed-meshheading:1645354-Thymidine,
pubmed-meshheading:1645354-Trypsin,
pubmed-meshheading:1645354-Tyrosine
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
The insulin receptor functions normally in Chinese hamster ovary cells after truncation of the C terminus.
|
| pubmed:affiliation |
Joslin Diabetes Center, Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|