Premium
Proteomic identification of pleckstrin‐associated proteins in platelets: Possible interactions with actin
Author(s) -
Baig Akeel,
Bao Xiankun,
Haslam Richard J.
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200900060
Subject(s) - moesin , microbiology and biotechnology , immunoprecipitation , actin , filamin , platelet , biology , cytoskeleton , chemistry , biochemistry , immunology , ezrin , cell , gene
Pleckstrin (plek)‐null platelets from a knockout mouse have been shown to be defective in granule secretion, aggregation and actin polymerization. However, the mechanism of plek signaling is currently unknown. Therefore, we sought to identify plek‐binding proteins in platelets by using GST pulldown assays and immunoprecipitation to isolate proteins from extracts of protein kinase C‐activated or inhibited human platelets. Co‐purified plek‐binding proteins were resolved by SDS‐PAGE and identified via nanospray quadruple TOF MS. Identified proteins may be involved in various cellular processes including cytoskeletal reorganization (moesin, radixin and α‐actinin) and signal transduction (serum deprivation response protein, 17 β‐hydroxysteroid dehydrogenase 4 and factor XIIIA). Both platelet aggregation and/or secretion require actin polymerization. However, studies have shown no direct association between plek and actin. Based on our findings we propose indirect associations between plek and actin through 17 β‐hydroxysteroid dehydrogenase 4, α‐actinin, moesin, radixin and factor XIIIA, which in turn suggest new roles for plek in platelet biology.