Insulin causes insulin-receptor internalization in human erythrocyte ghosts
نویسندگان
چکیده
منابع مشابه
Insulin degradation by human erythrocyte lysates.
In vitro hemolysates of isolated human erythrocytes degrade 125I-labeled insulin. Ten- to 100-fold dilutions of the hemolysate give a proportionately decreased degradation of 125I-labeled insulin at 37 degrees C, while dilutions of up to eightfold do not. Like the control, diluted "Buffer G" containing 5 mmol/L Tris and 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid buffer alone, more than ...
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The internalization and degradation of insulin was assessed in Chinese hamster ovary cell lines expressing either the wild-type receptor or mutated receptors lacking kinase activity. The mutated receptors included receptors which differed from the wild-type receptor by a single amino acid (substitution of an arginine for lysine at position 1030, a site critical for ATP binding) as well as recep...
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Phorbol 12-myristate 13-acetate (PMA) was used to examine the role of insulin receptor phosphorylation in the regulation of insulin receptor internalization in vascular endothelial cells. Association of 125I-insulin in rat capillary and bovine aortic endothelial cells preincubated with PMA was increased by 80 and 64% over control, respectively. The increase was due to enhanced 125I-insulin inte...
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We have studied the phosphorylation state of the insulin receptor during receptor-mediated endocytosis in the well-differentiated rat hepatoma cell line Fao. Insulin induced the rapid internalization of surface-iodinated insulin receptors into a trypsin-resistant compartment, with a 3-fold increase in the internalization rate over that seen in the absence of insulin. Within 20 min of insulin st...
متن کاملInsulin-induced surface redistribution regulates internalization of the insulin receptor and requires its autophosphorylation.
The role of insulin-induced receptor autophosphorylation in its internalization was analyzed by comparing 125I-labeled insulin (125I-insulin) internalization in Chinese hamster ovary (CHO) cell lines transfected with normal (CHO.T) or mutated insulin receptors. In four cell lines with a defect of insulin-induced autophosphorylation, 125I-insulin internalization was impaired. By contrast, in CHO...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1987
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2410093