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No evidence for calpain I involvement in fodrin rearrangements linked to regulated secretion
Author(s) -
Perrin Dominique,
Söling Hans-Dieter
Publication year - 1992
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(92)81125-6
Subject(s) - calpain , secretion , cleavage (geology) , microbiology and biotechnology , stimulation , cytoskeleton , protease , chemistry , biology , biochemistry , cell , endocrinology , enzyme , paleontology , fracture (geology)
Stimulation of secretion in chromaffin and parotid acinar cells is associated with dramatic rearrangements of the subplasmalemmal cytoskeleton, notably of fodrin and F‐actin. It has been proposed that a proteolytic cleavage of fodrin resulting from an activation of the neutral calcium activated protease (calpain) could be responsible for these changes. Using an affinity‐purified anti‐α‐fodrin antibody, several cleavage products of fodrin could clearly be detected following incubation of total cell homogenates from chromaffin and parotid acinar cells with purified calpain I. On the other hand, maximum stimulation of secretion of chromaffin cells by nicotine, and of parotid acinar cells by carbachol plus isoproterenol, was not associated with an increased appearance of cleavage products of fodrin. This result is not compatible with the ‘proteolytic cleavage’ hypothesis.