Botrocetin
Mostrando 1-8 de 8 artigos, teses e dissertações.
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1. Contribution to the investigation of hemostatic disturbances induced by Bothrops jararaca snake venom in rabbits: study of platelet membrane glycoproteins, function, secretion and survival. / Contribuição à investigação das alterações hemostáticas induzidas pelo veneno da serpente Bothrops jararaca em coelhos: estudo das glicoproteínas da membrana, função, secreção e sobrevivência plaquetárias.
Que o envenenamento pela serpente Bothrops jararaca causa distúrbios hemorrágicos sistêmicos, com alteração da coagulação e fibrinólise sangüíneas, é notório. Contudo, pouco se sabe sobre a ação in vivo desse veneno sobre as plaquetas. Em estudos recentes, demonstrou-se que esse veneno causa trombocitopenia, distúrbios da agregação e diminui
Publicado em: 2002
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2. Purificação e caracterização de uma proteina (SIII-3rp) do veneno de Bothrops alternatus que se liga ao fator de von Willebrand (vwF)
Botrocetin is a platelet coagglutin described in Bothrops jararaca venon suggested as a substitute for ristocetin as a mediator of the interaction between GPIb-IX complex and the von Willebrand factor (vWF) that lead to platelet agglutination (Read et al., 1978). A single chain and a two chain botrocetin were described in B. jararaca venon (Fujimura et al.,
Publicado em: 1995
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3. Botrocetin (venom coagglutinin): reaction with a broad spectrum of multimeric forms of factor VIII macromolecular complex.
Botrocetin, originally called venom coagglutinin, is a Bothrops factor that causes aggregation of blood platelets in the presence of the von Willebrand component of the factor VIII macromolecular complex. The complex consists of a series of multimers with a molecular weight of about 1-20 x 10(6). Ristocetin, another agent that causes platelet aggregation dep
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4. Primary structure of two-chain botrocetin, a von Willebrand factor modulator purified from the venom of Bothrops jararaca.
The complete amino acid sequence and location of the disulfide bonds of two-chain botrocetin, which promotes platelet agglutination in the presence of von Willebrand factor, from venom of the snake Bothrops jararaca are presented. Sequences of the alpha and beta subunits were determined by analysis of peptides generated by digestion of the S-pyridylethylated
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5. von Willebrand disease type B: a missense mutation selectively abolishes ristocetin-induced von Willebrand factor binding to platelet glycoprotein Ib.
von Willebrand factor (vWF) is a multimeric glycoprotein that mediates the adhesion of platelets to the subendothelium by binding to platelet glycoprotein Ib. For human vWF, this interaction can be induced in vitro by the antibiotic ristocetin or the snake venom protein botrocetin. A missense mutation, Gly-561-->Ser, was identified within the proposed glycop
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6. αB-crystallin, a low-molecular-weight heat shock protein, acts as a regulator of platelet function
It has recently been reported that αB-crystallin, a low-molecular-weight heat shock protein, may be released from cells by mechanical stretch. We investigated a physiological role of αB-crystallin in platelet function. αB-crystallin inhibited platelet aggregation induced by thrombin or botrocetin in hamsters and humans. These platelets had specific bindin
Cell Stress Society International.
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7. O-linked carbohydrate of recombinant von Willebrand factor influences ristocetin-induced binding to platelet glycoprotein 1b.
By transfecting the full-length cDNA for human von Willebrand factor (vWf) into a line of Chinese hamster ovary cells with a defect in carbohydrate metabolism, we have prepared recombinant vWf specifically lacking O-linked carbohydrates. We have compared this under-glycosylated protein to fully glycosylated recombinant vWf with respect to several structural
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8. A monomeric von Willebrand factor fragment, Leu-504--Lys-728, inhibits von Willebrand factor interaction with glycoprotein Ib-IX [corrected]
von Willebrand factor interaction with glycoprotein Ib alpha (GPIb alpha) plays a critical role in the initial phase of platelet adhesion at high shear rates, and it may also play a role in platelet thrombus formation in partially occluded arteries. Previous studies have indicated that two peptides, Cys-474--Pro-488 (peptide 153) and Ser-692--Pro-708 (peptid