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A more recent version of this article appeared on July 11, 2003
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M212407200v1
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Papers In Press, published online ahead of print April 30, 2003
J. Biol. Chem, 10.1074/jbc.M212407200
Submitted on December 5, 2002
Revised on March 31, 2003
Accepted on April 30, 2003

Direct demonstration of involvement of protein kinase Calpha in the Ca2+-induced platelet aggregation

Arata Tabuchi, Akira Yoshioka, Tomohito Higashi, Ryutaro Shirakawa, Hiroaki Nishioka, Toru Kita, and Hisanori Horiuchi

Geriatric Medicine, Kyoto University Graduate School of Medicine, Kyoto 606-8507

Corresponding Author: horiuchi{at}kuhp.kyoto-u.ac.jp

Platelets play critical roles in hemostasis and thrombosis through their aggregation following activation of integrin alpha IIbbeta 3. However, the molecular mechanism of the integrin activation inside platelets remains largely unknown. Pharmacological experiments have demonstrated that Protein kinase C (PKC) plays an important role in platelet aggregation. Since PKC inhibitors can have multiple substrates, and given that non-PKC-phorbol ester-binding signaling molecules have been demonstrated to play important roles, the precise involvement of PKC in cellular functions requires re-evaluation. Here, we have established an assay for analyzing the Ca2+-induced aggregation of permeabilized platelets. The aggregation of platelets was inhibited by addition of the arginine-glycine-aspartate-serine peptide, an integrin binding peptide inhibitor of alpha IIbbeta 3, suggesting that the aggregation was mediated by the integrin. The aggregation was also dependent on exogenous ATP and platelet cytosol, indicating the existence of essential cytosolic factors required for the aggregation. To examine the role of PKC in the aggregation assay, we immuno-depleted PKC alpha and beta from the cytosol. The PKC-depleted cytosol lost the aggregation-supporting activity, which was recovered by addition of purified PKCalpha . Furthermore, addition of purified PKCalpha in the absence of cytosol did not support the aggregation, whereas the cytosol containing less PKC supported it efficiently, suggesting that additional factors besides PKC would also be required. Thus, we directly demonstrated that PKCalpha is involved in the regulation of Ca2+-induced platelet aggregation.


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