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Destabilization of actin filaments as a requirement for the secretion of catecholamines from permeabilized chromaffin cells
Author(s) -
Lelkes Peter I.,
Friedman Jonathan E.,
Rosenheck Kurt,
Oplatka Avraham
Publication year - 1986
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(86)81049-3
Subject(s) - secretion , microbiology and biotechnology , actin , cytochalasin , cytochalasin b , phalloidin , cytoskeleton , egta , cytochalasin d , biology , biophysics , chemistry , calcium , biochemistry , cell , organic chemistry
In the search for a functional role of cytoskeletal proteins in the mechanism(s) of stimulus‐secretion coupling, we have previously demonstrated that the actomyosin system might be involved in the transport of cations across the plasma membrane of bovine adrenal chromaffin cells [(1986) J. Biol. Chem. 261, 5745‐5750]. To establish whether actin and myosin might also be involved in later stages of the cellular response, we have examined the possible effects of various actin‐specific reagents on the calcium‐mediated secretion of catecholamines from digitonin‐permeabilized cells. F‐Actin‐destabilizing agents, such as cytochalasin D or DNase 1, were found to promote Ca 2+ ‐stimulated (as well as basal) secretion. By contrast, stabilizers, like phalloidin, produced the opposite effect. It is concluded that stimulus‐secretion coupling in chromaffin cells might require the reorganization of actin for modulating both ion transport across the plasma membrane and exocytotic secretion per se.