Results 261 to 270 of about 42,405 (307)

Pathophysiology of Platelet Thrombin Receptors

Thrombosis and Haemostasis, 1997
The evidence is reviewed and a model presented for two distinct receptors being involved in platelet activation induced by alpha-thrombin: a high affinity thrombin receptor constituting approximately 50 copies of a supercomplexed form of GPIb coupled to phospholipase A2 and a moderate affinity receptor constituting approximately 2000 copies of the ...
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Thrombin receptor antagonists

Coronary Artery Disease, 1997
The thrombin receptor and protease-activated receptor 2 (PAR-2) are the two currently known members of the large family of G protein-coupled receptors that are activated by proteases. Both receptors are located on cells in and around the vascular space, including platelets, endothelial cells, vascular smooth muscle cells, fibroblasts and some ...
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Platelet activation by thrombin in the absence of the high-affinity thrombin receptor

Biochemistry, 1988
The receptor status of the moderate-affinity platelet binding site for alpha-thrombin has been established by treating platelets with Serratia marcescens protease under conditions causing cleavage of 95-97% glycoprotein Ib (2.5 micrograms for 30 min).
J T, Harmon, G A, Jamieson
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Expression and Purification of the Human Thrombin Receptor

Protein Expression and Purification, 1998
The human thrombin receptor has been overexpressed in Sf9 (Spodoptera frugiperda) insect cells using a baculovirus vector. Cell surface expression of the receptor was confirmed by immunocytochemistry with polyclonal antibodies raised against the extracellular domain of the receptor.
C, Chinni, S P, Bottomley, E J, Duffy, B A, Hemmings, S R, Stone   +4 more
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Molecular mapping of thrombin‐receptor interactions

Proteins: Structure, Function, and Bioinformatics, 2001
AbstractIn addition to its procoagulant and anticoagulant roles in the blood coagulation cascade, thrombin works as a signaling molecule when it interacts with the G‐protein coupled receptors PAR1, PAR3, and PAR4. We have mapped the thrombin epitopes responsible for these interactions using enzymatic assays and Ala scanning mutagenesis.
Y M, Ayala, A M, Cantwell, T, Rose, L A, Bush, D, Arosio, E, Di Cera   +5 more
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The Platelet Thrombin Receptor and Postoperative Bleeding

The Annals of Thoracic Surgery, 1998
We hypothesized that small amounts of thrombin desensitize the platelet thrombin receptor during cardiopulmonary bypass (CPB), resulting in postoperative platelet dysfunction and bleeding.Seventy-nine patients were entered into a study designed to measure changes in platelet thrombin receptor function during CPB and to correlate them to postoperative ...
V A, Ferraris, S P, Ferraris, A, Singh, W, Fuhr, D, Koppel, D, McKenna, E, Rodriguez, H, Reich   +7 more
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Role of the thrombin receptor in restenosis and atherosclerosis

The American Journal of Cardiology, 1995
Thrombus generation is central to thrombosis at vascular lesion sites, including post-PCTA acute reocclusion and chronic restenosis. Thrombin stimulates platelet activation, monocyte and neutrophil chemotaxis, and endothelial production of prothrombotic factors.
D, Baykal, J F, Schmedtje, M S, Runge
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Platelet Receptors: The Thrombin Receptor

1997
The serine protease thrombin evokes biological responses from a variety of cells such as platelets, megakaryoblasts, endothelial cells (Vu et al. 1991a), monocytes (Hoffman and Church 1993; Joseph and MacDermot 1993), fibroblasts (Vouret-Craviari et al. 1992), mesangial cells (Grandaliano et al. 1994), smooth muscle cells (Herbert et al.
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[Cellular receptor of thrombin].

Annales de biologie clinique, 1995
Thrombin is a serine protease able to evoke biological responses from a variety of cells, including platelets, endothelial cells, fibroblasts and smooth muscle cells. The structure of the thrombin receptor present in the human megakaryoblastic cell line and in hamster fibroblasts has recently been deduced by expression in the Xenopus laevis oocyte. The
D, Lasne, F, Rendu, M, Aiach
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Thrombin inhibitors and thrombin receptor agonists/antagonists

1996
Summary The information presented in this article illustrates the feasibility of designing low molecular weight protein mimetics by exploiting the three dimensional array of functional binding elements of the parent protein. In the case of thrombin, the unique mechanism of enzyme inhibition exerted by hirudin is preserved in low molecular weight ...
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