PMID: 640301Apr 1, 1978

NSILA-carrier protein abolishes the action of nonsuppressible insulin-like activity (NSILA-S) on perfused rat heart

Diabetologia
C MeuliE R Froesch

Abstract

Human serum in a concentration of 10% in the perfusion medium failed to increase glucose uptake by the isolated perfused rat heart, indicating that nonsuppressible insulin-like activity (NSILA) in whole serum was inactive in this system. When NSILA-carrier protein was added to partially purified NSILA-S, its biological activity on the rat heart disappeared. In contrast, the action of insulin was not affected by the presence of NSILA-carrier protein. Binding of 125I-labelled NSILA-S to rat heart was inhibited by NSILA-carrier protein. 125I-labelled insulin binding was not inhibited. These results support the hypothesis that NSILA-S bound to serum carrier protein is a large molecular compound which does not readily diffuse out of the capillary bed and therefore does not exert insulin-like effects in vivo.

References

Sep 1, 1975·The Journal of Clinical Endocrinology and Metabolism·K MegyesiP Gorden
Jun 1, 1975·Archives of Biochemistry and Biophysics·J ZapfE R Froesch
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Citations

Jun 1, 1982·Pflügers Archiv : European journal of physiology·J C HenquinW Schmeer
Jan 1, 1983·The International Journal of Biochemistry·H J Cornell, A C Herington
Jan 1, 1983·The International Journal of Biochemistry·A C HeringtonA D Kuffer
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Feb 14, 1980·The New England Journal of Medicine·L S Phillips, R Vassilopoulou-Sellin
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Aug 1, 1979·The Australian & New Zealand Journal of Obstetrics & Gynaecology·M W Brinsmead, G C Liggins

Related Concepts

Metazoa
Biological Availability
Carrier Proteins
Insulin B Chain
Myocardium
Perfusion
Plasma Protein Binding Capacity
Right Whale, North Atlantic
Rats, Laboratory

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