A role for protein kinase C in the membrane fusion necessary for platelet granule secretion release_sf3j4zcrzzdbxk5gecktquznzi

by J M Gerrard, L L Beattie, J Park, S J Israels, A McNicol, D Lint, E J Cragoe

Abstract

The addition of 1-oleoyl-2-acetylglycerol (OAG), or phorbol-12-myristate-13-acetate (PMA) to platelets induced the phosphorylation of a 47,000 dalton protein (47 Kd), fusion of granule membranes with membranes of the surface connected canalicular system, the formation of large vesicles and the secretion of serotonin. 1-(5-isoquinolinesulfonyl)-2-methyl-piperazine (H7), and sphingosine, inhibitors of protein kinase C, significantly inhibited the ultrastructural changes and the phosphorylation of 47 Kd. N-(2-guanidinoethyl)-5-isoquinolinesulfonamide (HA1004), structurally similar to H7, but a weaker inhibitor of protein kinase C, did not attenuate these responses to OAG or to PMA. H7, but not HA1004, also markedly inhibited secretion induced by the synergistic combination of OAG and the calcium ionophore A23187. Amiloride and 5-(N,N dimethyl)-amiloride, inhibitors of the Na+/H+ transporter, did not inhibit the ultrastructural response and the protein phosphorylation induced by OAG, or the secretion induced by the combination of A23187 and OAG. The results link the activation of protein kinase C by diglycerides to the labilization and fusion of granule membranes important for secretion.
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Published in Blood
ISSN-L 0006-4971
Volume 74
Issue 7
Page(s) 2405-13
Release Date 1989-11-15
Primary Language en (lookup)

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Type  article-journal
Stage   published
Date   1989-11-15
PubMed  2553164
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ISSN-L:  0006-4971
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