Adhesive surface determines raft composition in platelets adhered under flow

Adhesion to von Willebrand factor (VWF) induces platelet spreading, whereas adhesion to collagen induces aggregation. Here we report that cholesterol‐rich domains (CRDs) or rafts play a critical role in clustering of receptors that control these responses. Platelets adhered to VWF and collagen show...

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Bibliographic Details
Published in:Journal of thrombosis and haemostasis 2005-11, Vol.3 (11), p.2514-2525
Main Authors: LIER, M., LEE, F., FARNDALE, R. W., GORTER, G., VERHOEF, S., OHNO‐IWASHITA, Y., AKKERMAN, J‐W. N., HEIJNEN, H. F. G.
Format: Article
Language:English
Subjects:
Blood Platelets - chemistry
Blood Platelets - metabolism
Blood Platelets - ultrastructure
Cells, Cultured
Cholesterol - deficiency
Cholesterol - metabolism
collagen
Collagen - metabolism
glycoprotein Ib
glycoprotein VI
Humans
Membrane Glycoproteins
Membrane Microdomains - chemistry
Membrane Microdomains - metabolism
Membrane Proteins - metabolism
Perfusion
Platelet Adhesiveness - physiology
Platelet Aggregation - physiology
Platelet Glycoprotein GPIb-IX Complex
Platelet Membrane Glycoproteins - metabolism
Pseudopodia - chemistry
Pseudopodia - metabolism
rafts
Rheology
Signal Transduction - physiology
Surface Properties
von Willebrand factor
von Willebrand Factor - metabolism
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Summary:Adhesion to von Willebrand factor (VWF) induces platelet spreading, whereas adhesion to collagen induces aggregation. Here we report that cholesterol‐rich domains (CRDs) or rafts play a critical role in clustering of receptors that control these responses. Platelets adhered to VWF and collagen show CRDs concentrated in filopodia which contain both the VWF receptor glycoprotein (GP) Ibα and the collagen receptor GPVI. Biochemical analysis of CRDs shows a threefold enrichment of GPIbα (but not GPVI) in VWF‐adhered platelets and a fourfold enrichment of GPVI (but not GPIbα) in collagen‐adhered platelets. Depletion of cholesterol (i) leaves the initial adhesion unchanged, (ii) inhibits spreading on VWF and aggregate formation on collagen, (iii) leaves filopodia formation intact, and (iv) reduces the localization in filopodia of GPIbα but not of GPVI. These data show that the adhesive substrate determines the composition of CRDs, and that cholesterol is crucial for redistribution of GPIbα but not of GPVI.
ISSN:1538-7933
1538-7836
1538-7836
DOI:10.1111/j.1538-7836.2005.01597.x