Protein kinase C activation induces platelet apoptosis.
10.7534/j.issn.1009-2137.2013.05.024
- Author:
Li-Li ZHAO
1
,
2
;
Meng-Xing CHEN
;
Ming-Yi ZHANG
;
Ke-Sheng DAI
Author Information
1. Laboratory of Hematology and Cell Biology, School of Biological Science and Medical Engineering, Beijing University of Aeronautics and Astronautics, Beijing 100191, China
2. Jiangsu Institute of Hematology, Key Laboratory of Thrombosis and Hemostasis, Ministry of Health, The First Affiliated Hospital of Soochow University, Suzhou 215006, Jiangsu Province, China.
- Publication Type:Journal Article
- MeSH:
Apoptosis;
Blood Platelets;
cytology;
metabolism;
Caspase 3;
metabolism;
Humans;
Membrane Potential, Mitochondrial;
Phosphatidylserines;
metabolism;
Protein Kinase C;
metabolism
- From:
Journal of Experimental Hematology
2013;21(5):1207-1210
- CountryChina
- Language:Chinese
-
Abstract:
Platelet apoptosis elucidated by either physical or chemical compound or platelet storage occurs wildly, which might play important roles in controlling the numbers and functions of circulated platelets, or in the development of some platelet-related diseases. However, up to now, a little is known about the regulatory mechanisms of platelet apoptosis. Protein kinase C (PKC) is highly expressed in platelets and plays central roles in regulating platelet functions. Although there is evidence indicating that PKC is involved in the regulation of apoptosis of nucleated cells, it is still unclear whether PKC plays a role in platelet apoptosis. The aim of this study was to investigate the role of PKC in platelet apoptosis. The effects of PKC on mitochondrial membrane potential (ΔΨm), phosphatidylserine (PS) exposure, and caspase-3 activation of platelets were analyzed by flow cytometry and Western blot. The results showed that the ΔΨm depolarization in platelets was induced by PKC activator in time-dependent manner, and the caspase-3 activation in platelets was induced by PKC in concentration-dependent manner. However, the platelets incubated with PKC inhibitor did not results in ΔΨm depolarization and PS exposure. It is concluded that the PKC activation induces platelet apoptosis through influencing the mitochondrial functions and activating caspase 3. The finds suggest a novel mechanism for PKC in regulating platelet numbers and functions, which has important pathophysiological implications for thrombosis and hemostasis.
