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Tyrosine kinases and phosphoinositide metabolism in thrombin-stimulated human platelets

C Guinebault, B Payrastre, C Sultan, G Mauco, M Breton, S Levy-Toledano, M Plantavid, H Chap
Biochemical Journal Jun 15, 1993, 292 (3) 851-856; DOI: 10.1042/bj2920851
C Guinebault
*Institut National de la Santé et de la Recherche Médicale, Unité 326, Hôpital Purpan, 31059 Toulouse, France.
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B Payrastre
*Institut National de la Santé et de la Recherche Médicale, Unité 326, Hôpital Purpan, 31059 Toulouse, France.
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C Sultan
*Institut National de la Santé et de la Recherche Médicale, Unité 326, Hôpital Purpan, 31059 Toulouse, France.
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G Mauco
*Institut National de la Santé et de la Recherche Médicale, Unité 326, Hôpital Purpan, 31059 Toulouse, France.
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M Breton
*Institut National de la Santé et de la Recherche Médicale, Unité 326, Hôpital Purpan, 31059 Toulouse, France.
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S Levy-Toledano
†Unité 348, Hôpital Lariboisière, 75475 Paris Cedex, France.
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M Plantavid
*Institut National de la Santé et de la Recherche Médicale, Unité 326, Hôpital Purpan, 31059 Toulouse, France.
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H Chap
*Institut National de la Santé et de la Recherche Médicale, Unité 326, Hôpital Purpan, 31059 Toulouse, France.
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Abstract

In this study we have examined the implication of tyrosine kinase activities in aggregation, 5-hydroxytryptamine secretion and mainly phosphoinositide metabolism in response to human platelet stimulation by thrombin. Using the potent tyrosine kinase inhibitor tyrphostin AG-213, we have observed a significant inhibition of aggregation and 5-hydroxytryptamine release; however, this percentage inhibition was lower at high thrombin concentrations. On the other hand, tyrphostin treatment of metabolically 32P-labelled platelets significantly inhibited the thrombin-dependent accumulation of PtdIns(3,4)P2, which involves at least a PtdIns 3-kinase and/or a PtdIns3P 4-kinase, whereas the synthesis of phosphatidic acid (PtdOH), a good reflection of the phospholipase C (PLC) activation in platelets, was partially blocked. Inositol phosphate production was also inhibited by about 40% when tyrphostin-treated platelets were stimulated with thrombin. In addition, we show by Western-blot analysis that PLC gamma 1, as well as the regulatory subunit (p85) of the PtdIns 3-kinase, were present in the anti-phosphotyrosine immunoprecipitate isolated from thrombin-stimulated platelets. Furthermore, tyrphostin treatment clearly decreased the PLC gamma 1 and p85 contents in such an anti-phosphotyrosine immunoprecipitate. Our results provide the first evidence for a direct or indirect regulation of PtdIns(3,4)P2 accumulation and PLC gamma 1 activity by tyrosine phosphorylation during thrombin stimulation of human platelets.

  • © 1993 The Biochemical Society, London
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June 1993

Volume: 292 Issue: 3

Biochemical Journal: 292 (3)
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Tyrosine kinases and phosphoinositide metabolism in thrombin-stimulated human platelets
C Guinebault, B Payrastre, C Sultan, G Mauco, M Breton, S Levy-Toledano, M Plantavid, H Chap
Biochemical Journal Jun 1993, 292 (3) 851-856; DOI: 10.1042/bj2920851
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Tyrosine kinases and phosphoinositide metabolism in thrombin-stimulated human platelets
C Guinebault, B Payrastre, C Sultan, G Mauco, M Breton, S Levy-Toledano, M Plantavid, H Chap
Biochemical Journal Jun 1993, 292 (3) 851-856; DOI: 10.1042/bj2920851

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