Association of the antagonism of von Willebrand factor but not fibrinogen by platelet αIIbβ3 antagonists with prolongation of bleeding time

Aoki, Toshiaki; Tomiyama, Yoshiaki; Honda, Susumu; Mihara, Kayoko; Yamanaka, Toshio; Okubo, Mitsuru; Moriguchi, Akira; Mutoh, Seitaro

doi:10.1111/j.1538-7836.2005.01534.x

Cited by 5 publications

(3 citation statements)

References 37 publications

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“…A similar uneven distribution of VWF was also reported during thrombus formation in an in vitro study [27]. VWF and fibrinogen may play different roles in thrombus formation after binding to GPIIb/IIIa, as was suggested earlier by experiments showing that several GPIIb/IIIa antagonists having distinct abilities to compete for the binding of fibrinogen and VWF to GPIIb/IIIa [2].…”

Section: Discussionsupporting

confidence: 51%

In vivo imaging analysis of the interaction between unusually large von Willebrand factor multimers and platelets on the surface of vascular wall

Rybałtowski

Mogami

Chlebinska

et al. 2011

Pflugers Arch - Eur J Physiol

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To elucidate how unusually large von Willebrand factor (UL-VWF) multimers facilitate thrombus formation, their behavior was analyzed together with that of platelets in living mice deficient in the gene encoding the protease that cleaves UL-VWF, a disintegrin-like and metalloprotease with thrombospondin type 1 motif 13 (ADAMTS13-/-). By crossing ADAMTS13-/- mice with green fluorescent protein-expressing transgenic mice (GFP mice), GFP-ADAMTS13-/- mice were obtained. The dynamics of GFP-expressing platelets were monitored employing intravital confocal fluorescent microscopy. Administration of a vasopressin derivative, DDAVP, a secretagogue of VWF increased the number of platelets adhered to vascular endothelial cells (VECs) on mesentery at sites recognized by an anti-VWF antibody. Some of these platelets were interconnected and aligned as beads on a string. They reached their maximum length at 5 min and were longer in GFP-ADAMTS13-/- mice than in GFP mice (5.3 ± 4.3, N = 6 vs 2.9 ± 2.1 μm, N = 4) (mean±SE). Focal injury of VECs by topical application of FeCl(3) developed longer (25, 3-50 vs 10, 2-25 μm, P < 0.01) (mean, 10th-90th percentile) and more stable (1.3, 0.3-6.3 vs 0.3, 0.2-1.3 s, P < 0.01) connected platelets in GFP-ADAMTS13-/- mice than in GFP mice. This study revealed that ADAMTS13 cleaves platelet-bound UL-VWF multimers, both during their secretion from VECs and after their adherence to injured vascular walls in veins. UL-VWF multimers either being secreted from VECs or circulating in plasma of ADAMTS13-/- mice appeared to facilitate the accumulation of longer and more stable VWF strings with more associated platelets on injured vascular walls.

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Section: Discussionsupporting

confidence: 51%

In vivo imaging analysis of the interaction between unusually large von Willebrand factor multimers and platelets on the surface of vascular wall

Rybałtowski

Mogami

Chlebinska

et al. 2011

Pflugers Arch - Eur J Physiol

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“…Therefore, a IIb b 3 may contribute to platelet adhesion that is initiated through GPIb binding to VWF [90,91].…”

Section: Binding To Platelet Gpibmentioning

confidence: 99%

Structure and function of von Willebrand factor

Hassan

Saxena

Ahmad

2012

Blood Coagulation &Amp; Fibrinolysis

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von Willebrand factor (VWF) is a long plasma protein that contains many domains and each domain has its own function. VWF exists in a multimeric form and performs varieties of functions in the human body, including thrombus formation and blood coagulation. The crystal structures of three subdomains are known, and, interestingly, all three domains share identical three-dimensional fold with α-β-α sandwiched model. VWF is directly associated with different types of von Willebrand disease. In this review, our aim is to gather recent developments on structure and functions of VWF and its clinical relevance.

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“…Blood from the incision was blotted with Whatman nº2 filter paper every thirty seconds untill all bleeding stopped [9,10]. BT was 600 seconds (reference value 138 seconds).…”

Section: Case Presentationmentioning

confidence: 99%

Disseminated intravascular coagulation in a dog naturally infected by Leishmania (Leishmania) chagasi from Rio de Janeiro – Brazil

et al. 2013

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BackgroundDisseminated intravascular coagulation (DIC) is an acquired disorder characterized by the activation of intravascular coagulation and excessive fibrin formation. It always occurs in association with other clinical conditions, including parasitic diseases. DIC has been described as a unusual complication in human and canine visceral leishmaniasis.Case presentationDIC was found in a seven-year-old male mongrel dog naturally infected by Leishmania (Leishmania) chagasi. Haemostasis parameters demonstrated changes in primary and secondary haemostasis and fibrinolysis.ConclusionDIC is a unusual condition described in canine visceral leishmaniasis and it seems to be associated with several immunological and pathological mechanisms involved in the disease.

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Association of the antagonism of von Willebrand factor but not fibrinogen by platelet αIIbβ3 antagonists with prolongation of bleeding time

Cited by 5 publications

References 37 publications

In vivo imaging analysis of the interaction between unusually large von Willebrand factor multimers and platelets on the surface of vascular wall

In vivo imaging analysis of the interaction between unusually large von Willebrand factor multimers and platelets on the surface of vascular wall

Structure and function of von Willebrand factor

Disseminated intravascular coagulation in a dog naturally infected by Leishmania (Leishmania) chagasi from Rio de Janeiro – Brazil

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