Phosphorylation control by insulin in adipocytes is interfered with at a post‐receptor step by phosphoinositol and glucosamine

FEBS Letters

Strålfors, Peter²  Alemany, Susana¹ 

[1] Instituto de Ciencias Biomedicas C.S.I.C., Avenida Arzobispo Morzillo 4, E-28029 Madrid, Spain;Department of Physiological Chemistry. University of Lund, Box 94, S-22100 Lund, Sweden

关键词: Protein phosphorylation;    Insulin;    Adipocyte;    Phosphoinositol;    Glucosamine;    Insulin receptor;   

DOI  :  10.1016/0014-5793(90)81000-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Inositol-phosphates, glucosamine and glucose-6-phosphate blocked the effects of insulin on target protein phosphorylation in adipocytes, but the unsubstituted or sulphated derivatives of inositol or of glucose, or N-acetyl-glucosamine were without effect. The insulin stimulated tyrosine phosphorylation of the insulin receptor was not affected. The sugar-phospates inositol-phosphate and glucose-6-phosphate did not enter into the cells. They also blocked the insulin-like effects of a potential second messenger of insulin, a phosphooligosaccharide (POS), which has previously been shown to mimick the effects of insulin on protein phosphorylation in intact cells.

【 授权许可】

Unknown