Calpactin‐depleted cytosolic proteins restore Ca2+‐dependent secretion to digitonin‐permeabilized bovine chromaffin cells

FEBS Letters

Wagner, Paul D.¹  Wu, You Neng¹ 

[1] Laboratory of Biochemistry, National Cancer Institute, Bethesda, MD 20892, USA

关键词: Secretion;    Calpactin;    Ca2+;    Chromaffin cell;    Catecholamine;    EGTA;    ethylenebis(oxyethylenenitrilo)-tetraacetic acid;    NE;    norepinephrine;    PIPES;    piperazine-N;    N′-bis(2-ethane-sulfonic acid);    KG-buffer;    potassium/glutamate/MgATP/EGTA/PIPES solution;   

DOI  :  10.1016/0014-5793(91)80476-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Incubation of digitonin-permeabilized bovine chromaffin cells results in a loss of Ca³⁺-dependent catecholamine secretion. The addition of cytosolic proteins prevents this loss of secretory activity. It has been proposed that calpactin might be the protein which is responsible for preventing this loss of activity. The experiments described in this paper show that cytosolic proteins which have been depleted of calpactin are as effective as control cytosolic proteins in preventing the loss of Ca²⁺-dependent secretion. Thus, a cytosolic protein(s) other than calpactin appears to be responsible for preventing this loss of secretory activity.

【 授权许可】

Unknown