A synthetic peptide of the N‐terminus of ADP‐ribosylation factor (ARF) inhibits regulated exocytosis in adrenal chromaffin cells

FEBS Letters

Burgoyne, Robert D.¹  Morgan, Alan¹ 

[1] The Physiological Laboratory, University of Liverpool, PO Box 147, Liverpool, L69 3BX, UK

关键词: Exocytosis;    Calcium;    ADP-ribosylation factor;    GTP-binding protein;    Chromaffin cell;   

DOI  :  10.1016/0014-5793(93)80206-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Ca²⁺-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 CA²⁺ 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.

【 授权许可】

Unknown