Association of the low molecular weight GTP-binding protein rap2B with the cytoskeleton during platelet aggregation

Mauro Torti, Giuseppe Ramaschi, Fabiola Sinigaglia, Eduardo G. Lapetina, Cesare Balduini

Risultato della ricerca: Contributo su rivistaArticolo in rivistapeer review

Abstract

The intracellular distribution of the low-molecular-weight GTP-binding protein rap2B was investigated in resting and agonist-activated human platelets. In both cases, platelets were lysed by Triton X-100, and cell fractions were obtained by differential centrifugations. Using a specific polyclonal antiserum, we found that rap2B in resting platelets was completely detergent-soluble. When platelets were aggregated with thrombin, the thromboxane analogue U46619, or the Ca2+-ATPase inhibitor thapsigargin, a significant amount of rap2B became associated with the cytoskeleton. This association was paralleled by a decrease of rap2B in the Triton X-100-soluble fraction. Translocation of rap2B to the cytoskeleton strictly depended on platelet aggregation, and maximal incorporation was found when ≈50% aggregation was measured. Inhibition of fibrinogen binding to the glycoprotein IIb-IIIa complex completely prevented the interaction of rap2B with the cytoskeleton. These results clearly demonstrate that changes in the intracellular localization of rap2B occur during platelet activation and represent evidence that this low molecular weight GTP-binding protein may be involved in platelet function.

Lingua originaleInglese
pagine (da-a)7553-7557
Numero di pagine5
RivistaProceedings of the National Academy of Sciences of the United States of America
Volume90
Numero di pubblicazione16
DOI
Stato di pubblicazionePubblicato - 15 ago 1993
Pubblicato esternamente

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