scholarly journals Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells

1988 ◽  
Vol 250 (1) ◽  
pp. 95-101 ◽  
Author(s):  
O Koshio ◽  
Y Akanuma ◽  
M Kasuga
Keyword(s):  
Insulin Receptor ◽  
Kinase Activity ◽  
Intact Cell ◽  
Insulin Receptors ◽  
Beta Subunit ◽  
Receptor Kinase ◽  
Intact Cells ◽  
Tyrosine Residues ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity

H-35 rat hepatoma cells were labelled with [32P]orthophosphate and their insulin receptors isolated on wheat germ agglutinin (WGA)-agarose and anti-(insulin receptor) serum. The incubation of these cells with 10 mM-H2O2 for 10 min increased the phosphorylation of both the serine and tyrosine residues of the beta subunit of the insulin receptor. Next, insulin receptors were purified on WGA-agarose from control and H2O2-treated H-35 cells and the purified fractions incubated with [gamma-32P]ATP and Mn2+. Phosphorylation of the beta subunit of insulin receptors obtained from H2O2-treated cells was 150% of that of control cells. The kinase activity of the WGA-purified receptor preparation obtained from H2O2-treated cells, as measured by phosphorylation of src-related synthetic peptide, was increased about 4-fold over control cells. These data suggest that in intact cell systems, H2O2 may increase the insulin receptor kinase activity by inducing phosphorylation of the beta subunit of insulin receptor.

Insulin resistance in uremia: insulin receptor kinase activity in liver and muscle from chronic uremic rats

1988 ◽  
Vol 254 (4) ◽  
pp. E394-E401 ◽  
Author(s):  
F. Cecchin ◽  
O. Ittoop ◽  
M. K. Sinha ◽  
J. F. Caro
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Insulin Receptor ◽  
Kinase Activity ◽  
Insulin Binding ◽  
Beta Subunit ◽  
Receptor Kinase ◽  
Ad Libitum ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity

We have studied the structure and function of the partially purified insulin receptors from liver and skeletal muscle in a rat model of severe chronic uremia. 125I-insulin binding was higher in the liver from uremic rats when compared with ad libitum- and pair-fed controls. Furthermore, the ability of insulin to stimulate the autophosphorylation of the beta-subunit and insulin receptor kinase activity using Glu80, Tyr20 as exogenous phosphoacceptor was increased in the liver of the uremic animals. The structural characteristic of the receptors, as determined by electrophoretic mobilities of affinity labeled alpha-subunit and the phosphorylated beta-subunit, were normal in uremia. 125I-insulin binding and insulin receptor kinase activity were similar in the skeletal muscle from uremic and pair- and ad libitum-fed animals. Thus our data are supportive of the hypothesis that in liver and muscle of chronic uremic rats, insulin resistance is due to a defect(s) distal to the insulin receptor kinase.

Insulin receptor kinase activity in muscles and white adipose tissue during course of VMH obesity

1992 ◽  
Vol 262 (2) ◽  
pp. E161-E166 ◽  
Author(s):  
A. Pujol ◽  
B. Cousin ◽  
A. F. Burnol ◽  
M. Loizeau ◽  
L. Picon ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Insulin Receptor ◽  
White Adipose Tissue ◽  
Kinase Activity ◽  
Insulin Receptors ◽  
Ventromedial Hypothalamus ◽  
Receptor Kinase ◽  
Insulin Receptor Tyrosine Kinase ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity

Early after lesion of the ventromedial hypothalamus nuclei (VMH), insulin-induced glucose utilization is increased in white adipose tissue (WAT), whereas oxidative and glycolytic muscles are, respectively, normoresponsive or resistant to insulin. Five weeks later, all of the muscles are resistant, whereas WAT returns to normal responsiveness. The aim of this study was to characterize the insulin receptor kinase activity in WAT and muscles 1 and 6 wk after lesion. The number and affinity of insulin receptors were not modified in any of the tissues studied. Autophosphorylation and phosphorylation of an exogenous substrate were similar in oxidative and glycolytic muscles of VMH and control rats both 1 and 6 wk after the lesion. Insulin receptors from WAT of 1-wk VMH rats exhibited a 2.5-fold increase in insulin-stimulated autophosphorylation and phosphorylation. Six weeks after the lesion, both autophosphorylation and phosphorylation returned to normal values. This suggests that insulin receptor tyrosine kinase activity does not play a significant role in the insulin resistance of skeletal muscles but has a crucial role in mediating the variations of insulin action on WAT observed during the development of VMH obesity.

Insulin-receptor kinase activity of adipose tissue from morbidly obese humans with and without NIDDM

Diabetes ◽  
1987 ◽  
Vol 36 (5) ◽  
pp. 620-625 ◽  
Author(s):  
M. K. Sinha ◽  
W. J. Pories ◽  
E. G. Flickinger ◽  
D. Meelheim ◽  
J. F. Caro
Keyword(s):  
Adipose Tissue ◽  
Insulin Receptor ◽  
Kinase Activity ◽  
Morbidly Obese ◽  
Receptor Kinase ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity

Alteration of insulin-receptor kinase activity by high-fat feeding

Diabetes ◽  
1988 ◽  
Vol 37 (10) ◽  
pp. 1397-1404 ◽  
Author(s):  
T. Watarai ◽  
M. Kobayashi ◽  
Y. Takata ◽  
T. Sasaoka ◽  
M. Iwasaki ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Kinase Activity ◽  
Receptor Kinase ◽  
High Fat ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity ◽  
Fat Feeding

Insulin receptor kinase activity in rat adipocytes is decreased during aging

1989 ◽  
Vol 160 (1) ◽  
pp. 303-309 ◽  
Author(s):  
JoséM. Carrascosa ◽  
Pilar Ruíz ◽  
Carmen Martínez ◽  
Juan A. Pulido ◽  
Jorgina Satrústegui ◽  
...  
Keyword(s):  
Insulin Receptor ◽  
Kinase Activity ◽  
Receptor Kinase ◽  
Rat Adipocytes ◽  
Insulin Receptor Kinase ◽  
Insulin Receptor Kinase Activity
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