Abstract
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.

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