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Human Islet Amyloid Polypeptide at Pharmacological Levels Inhibits Insulin and Phorbol Ester-stimulated Glucose Transport in in Vitro Incubated Human Muscle Strips by J. R. Zierath; D. Galuska; . Engstrm; K. H. Johnson; C. Betsholtz; P. Westermark; H. Wallberg-Henriksson is a Medicine article available to read on EtoBox.

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Human islet amyloid polypeptide, at concentrations of 1-100 nmol/1, has been demonstrated to inhibit the insulin-stimulated increase in rat muscle glycogen content. However, at physiological concentrations (1-10 pmol/1) of islet amyloid polypeptide, no effects have been reported. We tested the effect of a wide range of concentrations of human islet amyloid polypeptide on insulin-and phorbol esterstimulated 3-0-methylglucose transport in in vitro incubated human skeletal muscle. Muscle specimens from the quadriceps femoris muscle were obtained from 23 healthy subjects with the use of a newly-developed open muscle biopsy technique. Human islet amyloid polypeptide at a concentration of 100 nmol/1 had no effect on basal glucose transport, but inhibited the stimulatory effect of a maximal insulin concentration (1000 gU/ml) by 69 % (p < 0.001). The presence of human islet amyloid polypeptide at 1, 10 and 100 nmol/1 decreased the effect of 100 btU/ml of insulin on glucose transport by 61% (p < 0.05), 78 % (p < 0.05) and 76 % (p < 0.05), respectively. Similarly, human islet amyloid polypeptide at a concentration of 10 nmol/1 inhibited phorbol ester-stimulated glucose transport by 100 % (p

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Author

J. R. Zierath; D. Galuska; . Engstrm; K. H. Johnson; C. Betsholtz; P. Westermark; H. Wallberg-Henriksson

Publisher

Springer; Springer-Verlag; Springer Verlag; Springer Science and Business Media LLC (ISSN 0012-186X)

Published

1992

Language

EN

Field

Medicine (Health Sciences)