Insulin resistance and growth retardation in mice lacking insulin receptor substrate-1 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-11

AUTHORS

Hiroyuki Tamemoto, Takashi Kadowaki, Kazuyuki Tobe, Takeshi Yagi, Hiroshi Sakura, Takaki Hayakawa, Yasuo Terauchi, Kohjiro Ueki, Yasushi Kaburagi, Shinobu Satoh, Hisahiko Sekihara, Shinji Yoshioka, Hiroyoshi Horikoshi, Yasuhide Furuta, Yoji Ikawa, Masato Kasuga, Yoshio Yazaki, Shinichi Aizawa

ABSTRACT

Insulin receptor substrate-1 (IRS-1) is the major substrate of insulin receptor and IGF-1 receptor tyrosine kinases; it has an apparent relative molecular mass of 160-190,000 (M(r), 160-190K) on SDS polyacrylamide gel. Tyrosine-phosphorylated IRS-1 binds the 85K subunit of phosphatidylinositol 3-kinase which may be involved in the translocation of glucose transporters and the abundant src homology protein (ASH)/Grb2 which may be involved in activation of p21ras and MAP kinase cascade. IRS-1 also has binding sites for Syp and Nck and other src homology 2 (SH2) signalling molecules. To clarify the physiological roles of IRS-1 in vivo, we made mice with a targeted disruption of the IRS-1 gene locus. Mice homozygous for targeted disruption of the IRS-1 gene were born alive but were retarded in embryonal and postnatal growth. They also had resistance to the glucose-lowering effects of insulin, IGF-1 and IGF-2. These data suggest the existence of both IRS-1-dependent and IRS-1-independent pathways for signal transduction of insulin and IGFs. More... »

PAGES

182-186

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/372182a0

DOI

http://dx.doi.org/10.1038/372182a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046415369

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7969452


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