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Engineered peptides corresponding to segments of the H3 domain of syntaxin inhibit insulin release both in intact and permeabilized mouse pancreatic beta cells.

Abstract：

:Syntaxin is one of the proteins involved in the exocytotic event through sequential binding to specific proteins, including SNAP25 and synaptobrevin. In a previous work in digitonin-permeabilized beta cells, we characterized the functional role of two segments: synA and synB of the H3 domain of syntaxin. As a continuation of these experiments in the present study we have initially outlined a zone of 17 residues as the very effective uncoupling element of the synA segment. Further functional studies have been accomplished in intact pancreatic beta cells with a specific myristoylated (myr) 13-mer peptide comprised in this active zone. These experiments showed a concentration-dependent inhibition of glucose-induced insulin release (IC50 = 4 microM) of this engineered peptide that was specific since a myristoylated random peptide with the same composition was ineffective. A second myristoylated 13-mer peptide comprised into the synB segment was shown to be even more potent promoting a selective inhibition of insulin release. These data show for the first time, that nutrient-induced secretory process can be specifically uncoupled in intact beta cells demonstrating at the same time that syntaxin plays a central role in this mechanism.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Martin F,Salinas E,Barahona F,Vázquez J,Soria B,Reig JA

doi

10.1006/bbrc.1998.8923

subject

Has Abstract

pub_date

1998-07-09 00:00:00

pages

83-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(98)98923-9

journal_volume

248

pub_type

杂志文章

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