|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
41
|
|
pubmed:dateCreated |
1995-12-4
|
|
pubmed:abstractText |
pp120/HA4 is a hepatocyte membrane glycoprotein phosphorylated by the insulin receptor tyrosine kinase. In this study, we have investigated the role of pp120/HA4 in insulin action. Transfection of antisense pp120/HA4 cDNA in H35 hepatoma cells resulted in inhibition of pp120/HA4 expression and was associated with a 2-3-fold decrease in the rate of insulin internalization. Furthermore, insulin internalization in NIH 3T3 fibroblasts co-transfected with insulin receptors and pp120/HA4 was increased 2-fold compared with cells expressing insulin receptors alone. In contrast, no effect on internalization was observed in cells overexpressing a naturally occurring splice variant of pp120/HA4 that lacks the phosphorylation sites in the intracellular domain. Insulin internalization was also unaffected in cells expressing three site-directed mutants of pp120/HA4 in which the sites of phosphorylation by the insulin receptor kinase had been removed (Y488F, Y488F/Y513F, and S503A). Our data suggest that pp120/HA4 is part of a complex of proteins required for receptor-mediated internalization of insulin. It is possible that this function is regulated by insulin-induced phosphorylation of the intracellular domain of pp120/HA4.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AKR1C2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxysteroid Dehydrogenases,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet-Derived Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Platelet-Derived Growth...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thymidine,
http://linkedlifedata.com/resource/pubmed/chemical/bile acid binding proteins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Oct
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
13
|
|
pubmed:volume |
270
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
24073-7
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:7592607-3T3 Cells,
pubmed-meshheading:7592607-Amino Acid Sequence,
pubmed-meshheading:7592607-Animals,
pubmed-meshheading:7592607-Antibodies,
pubmed-meshheading:7592607-Carrier Proteins,
pubmed-meshheading:7592607-Cell Cycle,
pubmed-meshheading:7592607-Cell Division,
pubmed-meshheading:7592607-Hydroxysteroid Dehydrogenases,
pubmed-meshheading:7592607-Insulin,
pubmed-meshheading:7592607-Kinetics,
pubmed-meshheading:7592607-Liver,
pubmed-meshheading:7592607-Membrane Glycoproteins,
pubmed-meshheading:7592607-Mice,
pubmed-meshheading:7592607-Molecular Sequence Data,
pubmed-meshheading:7592607-Mutagenesis, Site-Directed,
pubmed-meshheading:7592607-Peptide Fragments,
pubmed-meshheading:7592607-Phosphorylation,
pubmed-meshheading:7592607-Platelet-Derived Growth Factor,
pubmed-meshheading:7592607-RNA, Antisense,
pubmed-meshheading:7592607-Rats,
pubmed-meshheading:7592607-Receptor, Insulin,
pubmed-meshheading:7592607-Receptors, Platelet-Derived Growth Factor,
pubmed-meshheading:7592607-Recombinant Proteins,
pubmed-meshheading:7592607-Thymidine,
pubmed-meshheading:7592607-Transfection
|
|
pubmed:year |
1995
|
|
pubmed:articleTitle |
Receptor-mediated internalization of insulin. Potential role of pp120/HA4, a substrate of the insulin receptor kinase.
|
|
pubmed:affiliation |
Diabetes Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study
|
