von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively.

von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively. Research Abstract Details 

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von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively. Abstract Text:

O J T McCarty,S D J Calaminus,M C Berndt,L M Machesky,S P Watson,

BACKGROUND: von Willebrand factor (VWF) plays a critical role in the process of hemostasis by mediating flow-dependent adhesion and spreading of platelets on exposed extracellular matrix proteins following vascular injury. To accomplish this, VWF binds to two distinct platelet receptors: glycoprotein (GP)Ib-IX-V and integrin alpha(IIb)beta3. OBJECTIVE: To evaluate the ability of GPIb and alpha(IIb)beta3 to mediate platelet adhesion and lamellipodia formation on immobilized VWF in the presence of the biochemical modulators, ristocetin and botrocetin. RESULTS: In the presence of botrocetin and inhibitors of adenosine diphosphate (ADP) and thromboxane A2 (TxA2), VWF is able to support formation of lamellipodia through a GPIb-dependent mechanism that is independent of alpha(IIb)beta3 and PI3-kinase. Lamellipodia formation under these conditions is incomplete. In marked contrast, in the presence of ristocetin, VWF stimulates formation of fully spread lamellipodia through a pathway that is dependent upon alpha(IIb)beta3 and PI3-kinase. Furthermore, alpha(IIb)beta3 also supports platelet spreading on VWF alone, but only in the absence of inhibitors of ADP and TxA2. The localization of filamentous actin and the Arp2/3 complex in platelets on VWF in the presence of botrocetin and ristocetin are distinct, yielding disparate lamellipodium kinetic signatures. Interestingly, botrocetin significantly enhances platelet adhesion to VWF under flow in whole blood in an alpha(IIb)beta3-independent manner, while ristocetin augments washed platelet adhesion and spreading to VWF under flow in an alpha(IIb)beta3-dependent manner. CONCLUSIONS: These observations demonstrate that VWF is able to induce lamellipodia formation through distinct receptors, and has important consequences for investigation of the role of VWF-GPIb interactions in the context of platelet regulation.

von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively. Publishing Authors By Initials

OJ McCarty,SD Calaminus,MC Berndt,LM Machesky,SP Watson,

For similar proteins: blood proteins: blood coagulation factors: von willebrand factor research abstracts see: proteins: blood proteins: blood coagulation factors: von willebrand factor research

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von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of thrombosis and haemostasis : JTH

VOLUME: 4

Page Numbers: 1367-78

Journal Abbreviation: J. Thromb. Haemost.

ISSN: 1538-7933

DAY: 30

MONTH: Jun

YEAR: 2006

von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively. Information

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LANGUAGE: eng

NlmUniqueID: 101170508

von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively. Keywords Mesh Terms:

KEYWORDS: von Willebrand Factor

MESH TERMS: metabolism

Chemical & Substance for Abstract: von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively. Information

Substance Name: rac GTP-Binding Proteins

Registry Number: EC 3.6.5.2

Grant and Affiliation Information for von Willebrand factor mediates platelet spreading through glycoprotein Ib and alpha(IIb)beta3 in the presence of botrocetin and ristocetin, respectively.

AFFILIATION: Centre for Cardiovascular Sciences, University of Birmingham, Birmingham, UK. mccartyo@ohsu.edu

Country: England

AGENCY: United Kingdom Wellcome T

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MEDLINETA: J Thromb Haemost

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