期刊
CURRENT OPINION IN HEMATOLOGY
卷 14, 期 3, 页码 249-254出版社
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1097/MOH.0b013e3280ef68f8
关键词
aggregation; calpain-1; protein tyrosine kinases; protein tyrosine phosphatases
类别
资金
- NHLBI NIH HHS [R01 HL051445, R56 HL051445, HL51445] Funding Source: Medline
Purpose of review There is considerable interest in understanding the function and mechanism of calpains in platelet aggregation, spreading, and granular secretion pathways. Recent insights from the calpain-1 knockout platelets suggest a pivotal role of these cysteine proteases in the regulation of outside-in signaling, aggregation, and clot retraction. Recent findings The calpain-1 knockout mouse provided direct evidence for the role of calpain-1 in platelet aggregation and clot retraction. Reduced tyrosine phosphorylation of platelet proteins correlated with reduced platelet aggregation and clot retraction. Future investigations of the mechanism of platelet defects in calpain-1 null mice may unveil the physiological functions of this important and elusive protease in mammalian cells. Summary This review focuses on the role of calpains in platelets with a particular emphasis on recent findings in calpain-1 null platelets. Previous studies used synthetic inhibitors to study the role of calpains in platelet function yielding useful information about the identification of calpain substrates. The development of calpain-1 null mice demonstrated that calpain-1 plays an important function in the regulation of platelet aggregation and clot retraction. Since the combined deletion of calpain-1 and calpain-2 genes results in embryonic lethality, the calpain-1 null mouse remains the only experimental model available to study the physiological role of calpains in mammalian cells.
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