Abstract

Nonsuppressible insulin-like activity extracted and purified from human serum (NSILA-S) mimics all insulin-like effects in vitro and, after injection, in vivo in the presence of excess insulin antibodies. However, there is no evidence that it exerts acute insulin-like effects in its native form in the circulation, where it is almost completely bound to a specific large molecular weight carrier protein. In this paper we show that partially purified NSILA-S-carrier protein, devoid of endogenous insulin-like activity, inhibits the stimulatory effect of NSILA-S, but not of insulin, on 3-0-methylglucose transport and on lipogenesis from [U-14C]glucose in isolated rat fat cells. Concomitantly, it prevents binding of 125I-labeled NSILA-S to the insulin receptor and to the NSILA-S-binding site.

Authors

J. Zapf, E. Schoenle, G. Jagars, I. Sand, J. Grunwald, E. R. Froesch

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