Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 2 March 1984:
Vol. 223. no. 4639, pp. 932 - 934
DOI: 10.1126/science.6141638
Prev | Table of Contents | Next

Articles

Science, Vol 223, Issue 4639, 932-934
Copyright © 1984 by American Association for the Advancement of Science

articles

Defect in phosphorylation of insulin receptors in cells from an insulin-resistant patient with normal insulin binding

G Grunberger, Y Zick, and P Gorden

Mononuclear blood cells were obtained from a patient with type A insulin resistance. The cells showed a normal ability to bind iodine 125-labeled insulin. Analysis of solubilized insulin receptors from the patient's cells revealed a defect in insulin-stimulated tyrosine kinase activity, which is closely associated with the receptor itself. The enzyme failed to phosphorylate the insulin receptor and showed a markedly reduced ability to phosphorylate exogenously added substrates. It appears that receptors from this insulin-resistant patient have a defect distal to the insulin-binding site (the alpha subunit of the receptor). The defect could be located in the beta subunit, which has an adenosine triphosphate-binding site, or in another receptor component that transfers a signal of insulin binding into kinase activity. This dissociation between the normal binding and the defective protein kinase component of the insulin receptor represents the first biochemical defect of the receptor distal to ligand binding.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The Macrophage at the Crossroads of Insulin Resistance and Atherosclerosis.
C.-P. Liang, S. Han, T. Senokuchi, and A. R. Tall (2007)
Circ. Res. 100, 1546-1555
   Abstract »    Full Text »    PDF »
Recent Advances in Our Understanding of Insulin Action and Insulin Resistance.
D. Le Roith and Y. Zick (2001)
Diabetes Care 24, 588-597
   Abstract »    Full Text »
Human diabetes associated with a deletion of the tyrosine kinase domain of the insulin receptor.
M Taira, M Taira, N Hashimoto, F Shimada, Y Suzuki, A Kanatsuka, F Nakamura, Y Ebina, M Tatibana, H Makino, et al. (1989)
Science 245, 63-66
   Abstract »    PDF »
Human diabetes associated with a mutation in the tyrosine kinase domain of the insulin receptor.
M Odawara, T Kadowaki, R Yamamoto, Y Shibasaki, K Tobe, D Accili, C Bevins, Y Mikami, N Matsuura, Y Akanuma, et al. (1989)
Science 245, 66-68
   Abstract »    PDF »
After insulin binds.
O. Rosen (1987)
Science 237, 1452-1458
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)