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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1995-2-21
|
| pubmed:abstractText |
The insulin-like growth factor-1 (IGF-1) receptor is structurally related to the insulin receptor and shares common features in receptor signaling. These features include receptor autophosphorylation, phosphorylation of insulin receptor substrate-1, and activation of Ras and phosphatidylinositol-3-kinase (PI3K). Previously, we reported that after insulin treatment of rat HTC cells expressing human insulin receptors, a unique insulin receptor signaling complex was formed that contained the insulin receptor, the p85 subunit of PI3K, GTPase-activating protein (GAP), and p62 GAP-associated protein. In the present study, using wild type HTC cells, we investigated whether the activated IGF-1 receptor also forms a similar signaling complex. To study the proteins present in IGF-1 receptor signaling complexes, we used immunoprecipitation and Western blotting analysis with appropriate antibodies. In response to IGF-1, insulin receptor substrate-1 was tyrosine phosphorylated and formed a complex with the PI3K heterodimer that consists of a p85 regulatory subunit and a p110 catalytic subunit. In addition, a separate complex was formed, consisting of p85, p62 GAP-associated protein and GAP. The p62 in this complex was tyrosine phosphorylated. These studies suggest, therefore, that the IGF-1 receptor, like the insulin receptor, induces the formation of multiple signaling complexes that most likely mediate the proliferative effects of these receptors.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DOK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/GAP-associated protein p62,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/ras GTPase-Activating Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0013-7227
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
136
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
316-21
|
| pubmed:dateRevised |
2011-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:7828547-Animals,
pubmed-meshheading:7828547-Binding, Competitive,
pubmed-meshheading:7828547-DNA-Binding Proteins,
pubmed-meshheading:7828547-GTPase-Activating Proteins,
pubmed-meshheading:7828547-Insulin,
pubmed-meshheading:7828547-Insulin-Like Growth Factor I,
pubmed-meshheading:7828547-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:7828547-Phosphoproteins,
pubmed-meshheading:7828547-Phosphorylation,
pubmed-meshheading:7828547-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:7828547-Precipitin Tests,
pubmed-meshheading:7828547-Proteins,
pubmed-meshheading:7828547-RNA-Binding Proteins,
pubmed-meshheading:7828547-Rats,
pubmed-meshheading:7828547-Tumor Cells, Cultured,
pubmed-meshheading:7828547-Tyrosine,
pubmed-meshheading:7828547-ras GTPase-Activating Proteins
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Insulin-like growth factor-1 stimulation of cells induces formation of complexes containing phosphatidylinositol-3-kinase, guanosine triphosphatase-activating protein (GAP), and p62 GAP-associated protein.
|
| pubmed:affiliation |
Department of Medicine, Mount Zion Medical Center of the University of California, San Francisco 94115.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|