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

Ali, Shahid; Geisow, Michael J.; Burgoyne, Robert D.

doi:10.1038/340313a0

Cited by 322 publications

(160 citation statements)

References 22 publications

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“…It is possible that the activation of PKC causes the retention of a cytosolic protein, required for exocytosis, within the permeabilized cell. A possible candidate is annexin II (calpactin I), which has been shown to be necessary for exocytosis in the permeabilized bovine adrenal chromaffin cell (Ali et al, 1989). Pretreatment of chromaffin cells with PMA leads to an increase in membrane bound annexin II, retarding its loss on permeabilization with digitonin (Sarafian et al, 1991).…”

Section: Discussionmentioning

confidence: 99%

Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini

O’Sullivan

Jamieson

1992

Biochemical Journal

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The effect of protein kinase C (PKC) on amylase discharge from streptolysin-O-permeabilized rat pancreatic acini was investigated. Addition of phorbol 12-myristate 13-acetate (PMA) to permeabilized cells potentiated Ca2+-stimulated release, but had no effect on discharge at non-stimulatory Ca2+ concentrations. PMA markedly shifted the Ca2+-concentration-dependence of amylase discharge to the left, by enhancing the time over which the permeabilized cells release. This effect was inhibited by both staurosporine and PKC-19-31-amide peptide inhibitor, indicating that the effect of PMA was due to its action on PKC. Staurosporine also partially inhibited amylase release at the optimal concentration of Ca2+; this effect was not replicated by the more specific PKC-19-3 1-amide peptide inhibitor and may be due to an effect on another second-messenger system. PKC appears to be an important modulator of release in pancreatic acini, but its activation is not an absolute requirement for Ca2+-dependent amylase discharge.

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Section: Discussionmentioning

confidence: 99%

Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini

O’Sullivan

Jamieson

1992

Biochemical Journal

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“…Given the results obtained by Creutz et al (1987), Ali et al (1989), Burgoyne (1990), and Saraflan et al (1991) investigated the role of annexin 2 in digitonin-or streptolysin 0-permeabilized cells. Soluble heterotetrameric annexin 2 was shown Received September 18.…”

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Phosphorylation by Protein Kinase C of Annexin 2 in Chromaffin Cells Stimulated by Nicotine

Delouche

Pradel

Henry

1997

Journal of Neurochemistry

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Annexin 2 phosphorylated in vitro by protein kinase C has been shown to restore partially catecholamine secretion in streptolysin 0-permeabilized chromaffin cells depleted of their protein kinase C activity. This result suggested a phosphorylation of annexin 2 in stimulated cells. Nicotine stimulation induced an increase of 32p incorporation in annexin 2 heavy chain concomitant with catecholamine release. This incorporation results from phosphorylation by protein kinase C because (a) serin.e was the only phosphorylated residue, (b) 32P incorporation was inhibited by the protein kinase inhibitors H7, GF 1 09203X, and staurosporine, and (c) activators of this enzyme, 1 2-O-tetradecanoylphorbol 13-acetate and 1,2-dioctanoylglycerate, increased the incorporation of radioactivity. The phosphorylated heavy chain had an electrophoretic mobility lower than that of the unmodified one, thus allowing determination of the fraction of phosphorylated protein. In the resting state, a significant fraction of annexin 2 heavy chain was phosphorylated, and nicotine stimulation resulted in an activation of both phosphorylation and dephosphorylation. Phosphorylation was largely increased in the presence of okadaic acid, indicating the involvement of type 1 and 2A phosphatases. Key Words: Annexin-Protein kinase C-Phosphorylation-Chromaffin cells-Secretion. J. Neurochem. 68, 1720-1727 (1997).Adrenal chromaffin cells, which secrete catecholamines on stimulation by acetylcholine, have served as a good model for the study of the molecular mechanisms involved in regulated exocytosis. Primary cultures of chromaffln cells have allowed the study of stimulation by acetylcholine of catecholamine secretion and the characterization of factors essential for secretion (Fenwick et al., 1978;Kilpatrick et al., 1980). Along this line, Michener et al. (1986) and Creutz et a!. (1987) demonstrated the phosphorylation of two phospholipid and calcium binding proteins, chromobindins 8 and 9, when chromaffin cells were preincubated with 32P0 4 3 and stimulated by nicotine. These chromobindins were identified as annexins 1 and 2. Annexin 2 differs from the other annexins in being a heterotetramer composed of two 36-kDa heavy chains and two I l-kDa light chains or a monomer with one 36-kDa heavy chain. Only the heterotetramer is able to bind chromaffin granules, to promote their aggregation at a physiological calcium concentration of 5 ,uM, and, at pH 6, to induce the fusion of granules after addition of arachidonic acid (Drust and Creutz, 1988). The heavy chain of annexin 2 is phosphorylated by various protein kinases, and it is the major substrate for protein kinase C and for the Rous sarcoma virus enzyme pp60~"°. In human cells treated with epiderma! growth factor and platelet-derived growth factor, annexin 2 is phosphorylated on a tyrosine as well as on a serine (Isacke et a!., 1986). The serine residue was identified as Ser25 within the amino-terminal region (Glenney and Tack, 1985). Alternatively, in vitro phosphorylations of annexin 2 with ca...

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“…Although annexins are not directly fusogenic, the concept that they may mediate exocytotic events is based in part on evidence that, in the presence of Ca2", annexin II can bind to, aggregate, and (in conjunction with arachidonic acid and low pH) fuse secretory vesicle membranes (2,30).…”

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Properties and Partial Protein Sequence of Plant Annexins

Blackbourn¹,

Barker²,

Huskisson³

et al. 1992

Plant Physiol.

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We have examined the characteristics of Ca2"-dependent phospholipid-binding proteins (annexins) Iongiflorum. Immunolocalization at the light microscope level suggests that these proteins are predominantly confined to the nongranular zone at the tube tip, a region rich in secretory vesicles. Our hypothesis that plant annexins mediate exocytotic events is supported by the finding that p23, p33, and p35 bind to these secretory vesicles in a Ca2"-dependent manner.

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

Cited by 322 publications

References 22 publications

Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini

Activation of protein kinase C is not an absolute requirement for amylase release from permeabilized rat pancreatic acini

Phosphorylation by Protein Kinase C of Annexin 2 in Chromaffin Cells Stimulated by Nicotine

Properties and Partial Protein Sequence of Plant Annexins

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