Extracellular Mutations of Protease-Activated Receptor-1 Result in Differential Activation by Thrombin and Thrombin Receptor Agonist Peptide

2000 ◽  
Vol 58 (6) ◽  
pp. 1178-1187 ◽  
Author(s):  
Brian D. Blackhart ◽  
Lily Ruslim-Litrus ◽  
Chin-Chun Lu ◽  
Veronica L. Alves ◽  
Willy Teng ◽  
...  
1993 ◽  
Vol 190 (3) ◽  
pp. 1001-1008 ◽  
Author(s):  
C.F. Reilly ◽  
T.M. Connolly ◽  
D.M. Feng ◽  
R.F. Nutt ◽  
E.J. Mayer

2006 ◽  
Vol 142 (1) ◽  
pp. 35-38 ◽  
Author(s):  
A. V. Rusanova ◽  
A. M. Makarova ◽  
S. M. Strukova ◽  
E. A. Markvicheva ◽  
L. R. Gorbachyova ◽  
...  

1996 ◽  
Vol 225 (3) ◽  
pp. 1084-1089 ◽  
Author(s):  
Kaneo Satoh ◽  
Yukio Ozaki ◽  
Naoki Asazuma ◽  
Yutaka Yatomi ◽  
Qi Ruomei ◽  
...  

1992 ◽  
Vol 184 (2) ◽  
pp. 790-796 ◽  
Author(s):  
Kwan Y. Hui ◽  
Joseph A. Jakubowski ◽  
Virginia L. Wyss ◽  
Eddie L. Angleton

Blood ◽  
1998 ◽  
Vol 91 (11) ◽  
pp. 4152-4157 ◽  
Author(s):  
Hiroaki Ishihara ◽  
Dewan Zeng ◽  
Andrew J. Connolly ◽  
Carmen Tam ◽  
Shaun R. Coughlin

Recent studies of mice deficient in the thrombin receptor, protease-activated receptor 1 (PAR1), provided definitive evidence for the existence of a second thrombin receptor in mouse platelets. We recently identified a new thrombin receptor designated protease-activated receptor 3 (PAR3). The mRNA encoding a mouse homologue of PAR3 was highly expressed in mouse splenic megakaryocytes, making it a good candidate for the missing mouse platelet thrombin receptor. We now report that PAR3 protein is expressed on the surface of mouse platelets and that PAR3 antibodies partially inhibit activation of mouse platelets by thrombin but not U46619, a thromboxane receptor agonist. These observations suggest that PAR3 contributes to mouse platelet activation by thrombin.


2006 ◽  
Vol 16 (4) ◽  
pp. 321-325 ◽  
Author(s):  
E. Markvicheva ◽  
K. Stashevskaya ◽  
S. Strukova ◽  
I. Prudchenko ◽  
A. Rusanova ◽  
...  

1997 ◽  
Vol 86 (6) ◽  
pp. 1382-1386 ◽  
Author(s):  
Tameshwar Ammar ◽  
Cherie F. Fisher

Background Protamine is currently the most widely used drug for the reversal of heparin anticoagulation. Heparinase 1 (heparinase) is being evaluated as a possible alternative to protamine for the reversal of heparin anticoagulation. The authors evaluated the effects of equivalent doses of heparinase and protamine on platelet reactivity by measuring agonist-induced P-selectin expression. Methods After Institutional Review Board (IRB) approval, informed consent was obtained from 12 healthy volunteers and 8 patients undergoing surgery requiring cardiopulmonary bypass (CPB). Twenty-four ml of blood was obtained from each volunteer; 10 ml of blood was obtained from each patient before the CPB, and another 10 ml was obtained after CPB. Heparin was neutralized using heparinase or protamine. Platelet reactivity was assessed by measuring the expression of P-selectin after stimulation of platelets with increasing concentrations of a thrombin receptor agonist peptide (TRAP). Data were analyzed using analysis of variance. P < 0.05 was considered significant. Results For the healthy volunteers, the activated coagulation times (ACTs) of the heparinized samples returned to baseline values with heparinase (12.5 U/ml) or protamine (32.5 microg/ml). For the 8 patients, the ACTs returned to baseline with heparinase (20 U/ml) or protamine (50 microg/ml). The authors found no difference in the expression of P-selectin in samples neutralized with heparinase, but samples neutralized with protamine showed a significant decrease in the expression of P-selectin when compared with heparinized samples. Conclusions At dosages that reverse the anticoagulant effects of heparin, heparinase has minimal effects on platelets, whereas platelet reactivity was markedly inhibited by protamine.


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