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A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells

Nature volume 340, pages 313–315 (1989)Cite this article

Abstract

STIMULATION of bovine adrenal chromaffin cells results in a rise in the concentration of cytosolic calcium1-3 which triggers the release of catecholamines by exocytosis. Several cytosolic proteins that bind to secretory granule membranes in a calcium-dependent manner have been implicated in exocytosis4-12 and some belong to a family of calcium-binding proteins, the annexins6. One of these, calpactin, is a tetramer consisting of two heavy and two light chains (relative molecular masses 36,000 and 10,000 respectively)7,8 and can aggregate10,11 and fuse membranes in vitro in the presence of arachidonic acid10. Calpactin is found at the cell periphery13,14 and is phosphorylated when chromaffin cells are stimulated15. We show here that both calpactin and calpactin heavy chain (p36) reconstitute secretion in permeabilized chromaffin cells in which secretion has been reduced as a result of leakage of cellular components. This effect is inhibited by an affinity-purified antibody against p36. Secretion from permeabilized cells is inhibited by a synthetic annexin-consensus peptide, but not by a nonspecific hydrophobic peptide; this inhibition is reversed by p36. Our results indicate that either calpactin or p36 is essential for exocytosis.

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Authors and Affiliations

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

    Shahid M. Ali & Robert D. Burgoyne

  2. Delta Biotechnology, Castle Boulevard, Nottingham, NG7 1FD, UK

    Michael J. Geisow

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  1. Shahid M. Ali
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  2. Michael J. Geisow
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  3. Robert D. Burgoyne
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Ali, S., Geisow, M. & Burgoyne, R. A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells. Nature 340, 313–315 (1989). https://doi.org/10.1038/340313a0

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