The Effects of Brinolase (Fibrinolytic Enzyme from Aspergillus Oryzae) on Platelet Aggregation of Dog and Man

1972 ◽  
Vol 28 (01) ◽  
pp. 031-048 ◽  
Author(s):  
W. H. E Roschlau ◽  
R Gage

SummaryInhibition of blood platelet aggregation by brinolase (fibrinolytic enzyme from Aspergillus oryzae) has been demonstrated with human platelets in vitro and with dog platelets in vivo and in vitro, using both ADP and collagen as aggregating stimuli. It is suggested that the optimal inhibitory effects of brinolase occur indirectly through the generation of plasma fibrinogen degradation products, without compromising platelet viability, rather than by direct proteolysis of platelet structures.

1995 ◽  
Vol 15 (6) ◽  
pp. 748-753 ◽  
Author(s):  
Jonathan D. Emery ◽  
David W. Leifer ◽  
Glaci L. Moura ◽  
Patricia Southern ◽  
James H. Morrissey ◽  
...  

Author(s):  
Thanuja D. Herath ◽  
Gunaranjan Paturi ◽  
Christine A. Butts ◽  
Catherine E. Sansom ◽  
Marco P. Morgenstern

Molecules ◽  
2021 ◽  
Vol 26 (17) ◽  
pp. 5340
Author(s):  
Li Ming Lien ◽  
Wan Jung Lu ◽  
Kuan Hung Lin ◽  
Ling Hsuan Kang ◽  
Ting Yu Chen ◽  
...  

Vincristine is a clinically used antimicrotubule drug for treating patients with lymphoma. Due to its property of increasing platelet counts, vincristine is also used to treat patients with immune thrombocytopenia. Moreover, antiplatelet agents were reported to be beneficial in thrombotic thrombocytopenic purpura (TTP). Therefore, we investigated the detailed mechanisms underlying the antiplatelet effect of vincristine. Our results revealed that vincristine inhibited platelet aggregation induced by collagen, but not by thrombin, arachidonic acid, and the thromboxane A2 analog U46619, suggesting that vincristine exerts higher inhibitory effects on collagen-mediated platelet aggregation. Vincristine also reduced collagen-mediated platelet granule release and calcium mobilization. In addition, vincristine inhibited glycoprotein VI (GPVI) signaling, including Syk, phospholipase Cγ2, protein kinase C, Akt, and mitogen-activated protein kinases. In addition, the in vitro PFA-100 assay revealed that vincristine did not prolong the closure time, and the in vivo study tail bleeding assay showed that vincristine did not prolong the tail bleeding time; both findings suggested that vincristine may not affect normal hemostasis. In conclusion, we demonstrated that vincristine exerts antiplatelet effects at least in part through the suppression of GPVI signaling. Moreover, this property of antiplatelet activity of vincristine may provide additional benefits in the treatment of TTP.


2020 ◽  
Author(s):  
Thanuja D Herath ◽  
Gunaranjan Paturi ◽  
Christine A Butts ◽  
Catherine E Sansom ◽  
Marco P Morgenstern

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