YD-3, a novel inhibitor of protease-induced platelet activation
نویسندگان
چکیده
منابع مشابه
A trypsin-like platelet protease propagates protease-activated receptor-1 cleavage and platelet activation.
Protease-activated receptor-1 (PAR-1) is a G-protein-linked receptor on platelets and perivascular cells activated by alpha-thrombin and the PAR-1-activating peptide, SFLLRN. alpha-Thrombin activates PAR-1 by cleaving it at R41-S42 to release the 41-residue peptide TR(1-41). Unexpectedly, platelet activation with SFLLRN was also associated with PAR-1 cleavage and the release of TR(1-41). Both P...
متن کاملMRS2179: a novel inhibitor of platelet function
Background Antiplatelet agents, such as aspirin and P2Y12 inhibitors, are essential in the secondary prevention of cardiovascular disease [1]. Despite effective treatment with these drugs, many patients still suffer ischemic events. This suggests the need for additional antiplatelet therapy. The P2Y1 receptor is a seven transmembrane G protein coupled receptor responsible for platelet shape cha...
متن کاملPlatelet-activating factor stimulation of rabbit platelets is blocked by serine protease inhibitor (chymotryptic protease inhibitor).
The serine protease inhibitors diethyl p-nitrophenyl phosphate and phenylmethylsulfonyl fluoride (chemical modifiers of serine residue) and N-acetyl-l-tryptophan ethyl ester (competitive inhibitor of chymotryptic protease) inhibited 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (AGEPC; platelet-activating factor)-induced platelet aggregation and secretion. The inhibition was dependent on the p...
متن کاملSynthesis of novel peptide inhibitors of thrombin-induced platelet activation.
Inhibitors of the activation of platelet aggregation have promise as important therapeutic agents for the management of acute coronary syndrome (ACS). Platelet activation by thrombin, a serine protease, occurs by binding to and cleavage of the extracellular N-terminal domains of protease-activated receptors 1 and 4 (PAR1 and PAR4). The proteolysis of the PARs exposes new tethered ligands that t...
متن کاملActivation of coagulation factor V by a platelet protease.
Factor V must be converted to Factor V(a) in order to bind to a high affinity platelet surface site and participate in prothrombin activation. Osterud et al. (10) presented data that suggested that human platelets contain an activated form of Factor V and a Factor V activator. We find that the Factor V released when platelets are disrupted by freezing and thawing or sonication is activated 3- t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: British Journal of Pharmacology
سال: 2000
ISSN: 0007-1188
DOI: 10.1038/sj.bjp.0703437