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A synthetic peptide of the N‐terminus of ADP‐ribosylation factor (ARF) inhibits regulated exocytosis in adrenal chromaffin cells
Author(s) -
Morgan Alan,
Burgoyne Robert D.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80206-a
Subject(s) - exocytosis , adp ribosylation factor , chromaffin cell , chemistry , adp ribosylation , peptide , microbiology and biotechnology , endocrinology , biochemistry , biology , secretion , adrenal medulla , catecholamine , cell , enzyme , nad+ kinase , golgi apparatus
We have investigated the role of ADP‐ribosylation factor (ARF) in regulated exocytosis in digitonin‐permeabilized adrenal ehromaffin cells by the use of a synthetic peptide, hARFl(2–17), based on the N‐terminus of the protein. hARFl(2–17) inhibited Ca 2+ ‐dependent but not basal exocytosis, whereas equimolar levels of other synthetic peptides were ineffective. The inhibitory effect of hARFl(2–17) was dose‐dependent and half‐maximal at 12 μM. GTPγS‐induced secretion in the presence of non‐stimulatory CA 2+ concentrations was also inhibited by hARFl(2–17). These results point to a hitherto unsuspected role for ARF in regulated exocytosis, and the potency of the hARFl(2–17) peptide suggests that ARF is essential for exocytosis in bovine adrenal chromaffin cells.