A rho gene product in human blood platelets. II. Effects of the ADP- ribosylation by botulinum C3 ADP-ribosyltransferase on platelet aggregation
作者： N Morii , T Teru-uchi , T Tominaga , N Kumagai , S Kozaki
DOI: 10.1016/S0021-9258(19)36776-6
关键词: Exoenzyme 、 Molecular biology 、 ADP-ribosylation 、 G protein 、 Chemistry 、 Integrin 、 GTP-binding protein regulators 、 Thrombin 、 Platelet aggregation inhibitor 、 Platelet
摘要: In the accompanying paper (Nemoto, Y., Namba, T., Teru-uchi, Ushikubi, F., Morii, N., and Narumiya, S. (1992) J. Biol. Chem. 267, 20916-20920), we have identified rhoA protein as sole substrate for botulinum C3 ADP-ribosyltransferase (C3 exoenzyme) in human blood platelets. Here examined role of platelet functions. exoenzyme added to washed platelets dose- time-dependently ADP-ribosylated situ cells. Concomitant with this modification, inhibition thrombin-induced aggregation was observed. This not reversed by washing treated platelets, but found when pretreated mouse monoclonal anti-C3 antibody. treatment did affect inositol 1,4,5-trisphosphate production. Secretion preloaded [14C]serotonin delayed enzyme treatment, extent secretion influenced. addition, change expression glycoprotein IIb-IIIa complex on surface. The also suppressed induced phorbol myristate acetate. These results suggest that plays a mainly process downstream from receptor-phospholipase C coupling. This, together previous finding modulates stress fiber formation cultured fibroblasts (Paterson, H. Self, A. J., Garrett, M. D., Just, I., Aktories, K., Hall, (1990) Cell 111, 1001-1007), suggests regulates assembly actin filaments avidity integrin (glycoprotein IIb-IIIa) process.
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