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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| Veröffentlicht in: | Journal of thrombosis and haemostasis 2005-11, Vol.3 (11), p.2514-2525 |
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| creator | LIER, M. LEE, F. FARNDALE, R. W. GORTER, G. VERHOEF, S. OHNO‐IWASHITA, Y. AKKERMAN, J‐W. N. HEIJNEN, H. F. G. |
| description | 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. |
| doi_str_mv | 10.1111/j.1538-7836.2005.01597.x |
| format | Article |
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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.</description><identifier>ISSN: 1538-7933</identifier><identifier>ISSN: 1538-7836</identifier><identifier>EISSN: 1538-7836</identifier><identifier>DOI: 10.1111/j.1538-7836.2005.01597.x</identifier><identifier>PMID: 16241950</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Inc</publisher><subject>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</subject><ispartof>Journal of thrombosis and haemostasis, 2005-11, Vol.3 (11), p.2514-2525</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3677-d3aabfa8e5c437f0a8ca3dff7ab8d4b49e47e92d81348886b60cf2e14ad189273</citedby><cites>FETCH-LOGICAL-c3677-d3aabfa8e5c437f0a8ca3dff7ab8d4b49e47e92d81348886b60cf2e14ad189273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16241950$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LIER, M.</creatorcontrib><creatorcontrib>LEE, F.</creatorcontrib><creatorcontrib>FARNDALE, R. W.</creatorcontrib><creatorcontrib>GORTER, G.</creatorcontrib><creatorcontrib>VERHOEF, S.</creatorcontrib><creatorcontrib>OHNO‐IWASHITA, Y.</creatorcontrib><creatorcontrib>AKKERMAN, J‐W. N.</creatorcontrib><creatorcontrib>HEIJNEN, H. F. G.</creatorcontrib><title>Adhesive surface determines raft composition in platelets adhered under flow</title><title>Journal of thrombosis and haemostasis</title><addtitle>J Thromb Haemost</addtitle><description>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.</description><subject>Blood Platelets - chemistry</subject><subject>Blood Platelets - metabolism</subject><subject>Blood Platelets - ultrastructure</subject><subject>Cells, Cultured</subject><subject>Cholesterol - deficiency</subject><subject>Cholesterol - metabolism</subject><subject>collagen</subject><subject>Collagen - metabolism</subject><subject>glycoprotein Ib</subject><subject>glycoprotein VI</subject><subject>Humans</subject><subject>Membrane Glycoproteins</subject><subject>Membrane Microdomains - chemistry</subject><subject>Membrane Microdomains - metabolism</subject><subject>Membrane Proteins - metabolism</subject><subject>Perfusion</subject><subject>Platelet Adhesiveness - physiology</subject><subject>Platelet Aggregation - physiology</subject><subject>Platelet Glycoprotein GPIb-IX Complex</subject><subject>Platelet Membrane Glycoproteins - metabolism</subject><subject>Pseudopodia - chemistry</subject><subject>Pseudopodia - metabolism</subject><subject>rafts</subject><subject>Rheology</subject><subject>Signal Transduction - physiology</subject><subject>Surface Properties</subject><subject>von Willebrand factor</subject><subject>von Willebrand Factor - metabolism</subject><issn>1538-7933</issn><issn>1538-7836</issn><issn>1538-7836</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM1OwzAQhC0EoqXwCsgnbgl2nMTOgUNVAQVV4lLOlmOvhav8FDuh9O1JaIEre9mRdmZW-hDClMR0mNtNTDMmIi5YHieEZDGhWcHjzxM0_T2c_uiCsQm6CGFDCC2yhJyjCc2TdNBkilZz8wbBfQAOvbdKAzbQga9dAwF7ZTus23rbBte5tsGuwdtKdVBBF7Aakh4M7hsDHtuq3V2iM6uqAFfHPUOvD_frxTJavTw-LearSLOc88gwpUqrBGQ6ZdwSJbRixlquSmHSMi0g5VAkRlCWCiHyMifaJkBTZagoEs5m6ObQu_Xtew-hk7ULGqpKNdD2QeaCU8GzZDCKg1H7NgQPVm69q5XfS0rkSFJu5AhJjsDkSFJ-k5SfQ_T6-KMvazB_wSO6wXB3MOxcBft_F8vn9XJU7Au9loNa</recordid><startdate>200511</startdate><enddate>200511</enddate><creator>LIER, M.</creator><creator>LEE, F.</creator><creator>FARNDALE, R. W.</creator><creator>GORTER, G.</creator><creator>VERHOEF, S.</creator><creator>OHNO‐IWASHITA, Y.</creator><creator>AKKERMAN, J‐W. N.</creator><creator>HEIJNEN, H. F. G.</creator><general>Blackwell Science Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200511</creationdate><title>Adhesive surface determines raft composition in platelets adhered under flow</title><author>LIER, M. ; LEE, F. ; FARNDALE, R. W. ; GORTER, G. ; VERHOEF, S. ; OHNO‐IWASHITA, Y. ; AKKERMAN, J‐W. N. ; HEIJNEN, H. F. 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W.</creatorcontrib><creatorcontrib>GORTER, G.</creatorcontrib><creatorcontrib>VERHOEF, S.</creatorcontrib><creatorcontrib>OHNO‐IWASHITA, Y.</creatorcontrib><creatorcontrib>AKKERMAN, J‐W. N.</creatorcontrib><creatorcontrib>HEIJNEN, H. F. G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of thrombosis and haemostasis</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LIER, M.</au><au>LEE, F.</au><au>FARNDALE, R. W.</au><au>GORTER, G.</au><au>VERHOEF, S.</au><au>OHNO‐IWASHITA, Y.</au><au>AKKERMAN, J‐W. N.</au><au>HEIJNEN, H. F. G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Adhesive surface determines raft composition in platelets adhered under flow</atitle><jtitle>Journal of thrombosis and haemostasis</jtitle><addtitle>J Thromb Haemost</addtitle><date>2005-11</date><risdate>2005</risdate><volume>3</volume><issue>11</issue><spage>2514</spage><epage>2525</epage><pages>2514-2525</pages><issn>1538-7933</issn><issn>1538-7836</issn><eissn>1538-7836</eissn><abstract>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.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Inc</pub><pmid>16241950</pmid><doi>10.1111/j.1538-7836.2005.01597.x</doi><tpages>12</tpages></addata></record> |
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| 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 |
| title | Adhesive surface determines raft composition in platelets adhered under flow |
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