Insulin receptor binding and receptor-mediated insulin degradation in human adipocytes
نویسندگان
چکیده
منابع مشابه
Binding and receptor-mediated degradation of insulin in adipocytes.
Previous studies have shown that most of the degradation of insulin in a suspension of rat adipocytes (37°C pH 7.4, 10 mg/ml of albumin) is accounted for by protease(s) unrelated to receptors (Gammeltoft, S., and Gliemann, J. (1973) Biochim. Biophys. Acta 320, 16-32). The aim of the present study was to investigate whether receptor-mediated insulin degradation also occurred. Total insulin degra...
متن کاملReceptor-mediated insulin degradation and insulin-stimulated glycogenesis in cultured foetal hepatocytes.
Insulin-stimulated glycogenesis and insulin degradation were studied simultaneously at 37 degrees C in cultured foetal hepatocytes grown for 2-3 days in the presence of cortisol. Degradation of cell-associated insulin, as measured by trichloroacetic acid precipitation, was significant after 4 min in the presence of 1-3 nM-125I-labelled insulin. This process became maximal (30% of insulin degrad...
متن کاملEffects of autoantibodies to the insulin receptor on isolated adipocytes. Studies of insulin binding and insulin action.
Autoantibodies to the insulin receptor have been detected in the sera of several patients with the Type B syndrome of insulin resistance and acanthosis nigricans. In this study we have used three of these sera (B-1, B-2, and B-3) as probes of the insulin receptor in isolated rat adipocytes. Preincubation of adipocytes with each of the three sera resulted in an inhibition of subsequent [(125)I]i...
متن کاملEffects of insulin incubation on insulin binding, glucose transport, and insulin degradation by isolated rat adipocytes. Evidence for hormone-induced desensitization at the receptor and postreceptor level.
We have examined the effect of in vitro hyperinsulinemia on insulin binding, glucose transport, and insulin degradation in isolated rat adipocytes. When cells were incubated with insulin for 2 or 4 h at 37 degrees C, followed by washing in insulin-free buffer to remove extracellular and receptor-bound insulin, a time and dose-dependent decrease in insulin receptors was observed, which was accom...
متن کاملInsulin binding and insulin-dependent phosphorylation of the insulin receptor solubilized from human erythrocytes.
Insulin receptors were extracted from human erythrocytes contained in 100 ml of blood with the nonionic detergent Triton X-100 with almost 100% yield. The solubilized receptor had binding characteristics similar to those of the intact cell. Using 125I-monoiodoinsulin as tracer and a computer-assisted statistical curve-fitting program, a cooperative model gave values of 1.7 X 10(9) M-1 for the K...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Diabetologia
سال: 1981
ISSN: 0012-186X,1432-0428
DOI: 10.1007/bf00257433