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A role for protein kinase C in the membrane fusion necessary for platelet
granule secretion
JM Gerrard, LL Beattie, J Park, SJ Israels, A McNicol, D Lint and EJ Cragoe
Department of Pediatrics, Manitoba Institute of Cell Biology, University of
Manitoba, Winnipeg.
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.
Volume 74,
Issue 7,
pp. 2405-2413,
11/15/1989
Copyright © 1989 by The American Society of Hematology
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