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Effects of low-concentration polymyxin B on insulin secretion induced by 12-O-tetradecanoyl-phorbol-13-acetate (TPA), glucose, or tolbutamide from the isolated perfused rat pancreas.

Authors
Type
Published Article
Journal
Metabolism
0026-0495
Publisher
Elsevier
Publication Date
Volume
38
Issue
4
Pages
334–337
Identifiers
PMID: 2542720
Source
Medline

Abstract

To evaluate the role of protein kinase C on insulin secretion, we investigated the effects of low-concentration polymyxin B (100 mumol/L) on insulin secretion from the isolated perfused rat pancreas induced by 12-O-tetradecanoyl-phorbol-13-acetate (TPA, 10 nmol/L), a protein kinase C activator, glucose (10 mmol/L), or tolbutamide (738 mumol/L). Polymyxin B, a potent and relatively selective protein kinase C inhibitor at this low concentration, did significantly inhibit the gradual rise of insulin secretion induced by TPA (P less than .05). As for glucose or tolbutamide stimulation, polymyxin B significantly inhibited not only the second phase but also the first phase of insulin secretion (P less than .05) without changing the secretion patterns. Although the possibility of nonspecific effects of polymyxin B other than protein kinase C inhibition could not be excluded, the data suggest that protein kinase C might be involved in insulin secretion as a potentiating modulator.

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