CALYCULIN-A INHIBITS THE EXPOSURE OF FIBRINOGEN RECEPTOR IN THROMBIN-STIMULATED PLATELETS

被引：7
作者：
SAKON, M
MURATA, K
FUJITANI, K
YANO, Y
KAMBAYASHI, J
UEMURA, Y
KAWASAKI, T
SHIBA, E
MORI, T
机构：
[1] Department of Surgery II, Osaka University Medical School, Suita, Osaka 565
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 195卷 / 01期
关键词：
D O I：
10.1006/bbrc.1993.2021
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Calyculin A (CLA) and okadaic acid (OA), specific and potent inhibitors of protein phosphatase 1/2A, inhibit platelet aggregation. However, their inhibitory mechanisms remain unknown. We investigated the effects of CLA on the exposure of fibrinogen receptor in thrombin-stimulated platelets, using flow cytometry with a monoclonal antibody against the fibrinogen receptor of activated glycoprotein (Gp)IIb/IIIa complex (PAC−1). CLA inhibited the exposure of fibrinogen receptor in a dose related manner when added either before or 3 min after thrombin stimulation. In contrast, CLA had no significant effect when the expression of GpIIb/IIIa complex was examined in resting platelets, using a monoclonal antibody recognizing non-activated GpIIb/IIIa complex (NNKY1−32). These results suggest that protein phosphatase 1/2A may be directly involved in the exposure of platelet fibrinogen receptor. © 1993 Academic Press, Inc.
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页码：139 / 143
页数：5
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