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Platelet Receptors for Thrombin

1985
Platelets are activated by many different agonists, lach agonist presumably acts on a different receptor, but in no case has a receptor been defined1. Thrombin is perhaps the most potent physiological platelet agonist. In this paper, we review the current state of knowledge of the mechanism of thrombin-induced platelet activation. Results of studies of
T C, Detwiler, E B, McGowan
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Domains specifying thrombin–receptor interaction

Nature, 1991
Platelet activation by the coagulation protease thrombin is central to arterial thrombosis, a major cause of morbidity and mortality. We recently isolated a complementary DNA encoding the platelet thrombin receptor. The extracellular amino-terminal extension of this seven transmembrane domain receptor contains the putative thrombin cleavage site LDPR/S
T K, Vu   +4 more
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Binding of a Thrombin Receptor Tethered Ligand Analogue to Human Platelet Thrombin Receptor

Molecular Pharmacology, 1997
A thrombin receptor-radioligand binding assay was developed using [3H]A(pF-F)R(ChA)(hR)Y-NH2 ([3H]haTRAP), a high affinity thrombin receptor-activating peptide (TRAP), and human platelet membranes. Scatchard analysis of saturation binding data indicated that [3H]haTRAP bound to platelet membranes with a Kd of 15 nM and a Bmax of 5.2 pmol/mg of protein.
H S, Ahn   +6 more
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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 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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[Cell receptors of thrombin].

Ukrainskii biokhimicheskii zhurnal (1978), 1987
Modern notions on the structure, function and localization of thrombin receptors in different human and animal cells are considered. Molecular models of thrombin interaction with receptors are presented. The role these receptors play in the DNA synthesis regulation, proliferation and migration of cells is described.
V A, MonastyrskiÄ­, I I, Birka
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Thrombin induces ACSL4-dependent ferroptosis during cerebral ischemia/reperfusion

Signal Transduction and Targeted Therapy, 2022
Yang Shu, Yu-Jie Guo, Scott Ayton
exaly  

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