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  • Title: Human gamma-thrombin: lack of correlation between a platelet functional response and glycoprotein V hydrolysis.
    Author: Jandrot-Perrus M, Guillin MC, Nurden AT.
    Journal: Thromb Haemost; 1987 Oct 28; 58(3):915-20. PubMed ID: 3433254.
    Abstract:
    The ability of purified human gamma-thrombin to stimulate platelet function was related to its capacity to degrade GP V. Compared to alpha-thrombin, much greater amounts of gamma-thrombin were required to induce platelet aggregation; and this also applied to secretion from dense bodies, alpha-granules and lysosomal granules. Platelet stimulation by gamma-thrombin was additionally characterized by the presence of a lag-phase. Platelets with 3H-labelled surface glycoproteins showed the same functional response to both alpha- and gamma-thrombin as unlabelled platelets. But while threshold levels of alpha-thrombin induced little GP V hydrolysis confirming McGowan et al. (1), amounts of gamma-thrombin which induced substantial degradation (e.g. 8.3 nM degraded 36% of platelet GP V in 3 min) were unable to sustain either platelet aggregation or secretion. These results suggest that protein-binding regions remote from the catalytic site of alpha-thrombin are more important for platelet activation than GP V hydrolysis. They also provide further support to the argument that GP V hydrolysis may not be the essential trigger of platelet activation by thrombin.
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