Interactions of thermally denatured fibrinogen on polyethylene with plasma proteins and platelets
During the investigation of fibrin deposition onto hydrophobic polymers in contact with human blood, a model was developed in which fibrinogen was denatured and irreversibly coated onto a polyethylene surface by heating to 70°C for 10 min. The denatured fibrinogen‐polyethylene surface is resistant t...
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| Veröffentlicht in: | Journal of biomedical materials research 1992-12, Vol.26 (12), p.1651-1663 |
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| creator | Rubens, Fraser Brash, John Weitz, Jeff Kinlough-Rathbone, Raelene |
| description | During the investigation of fibrin deposition onto hydrophobic polymers in contact with human blood, a model was developed in which fibrinogen was denatured and irreversibly coated onto a polyethylene surface by heating to 70°C for 10 min. The denatured fibrinogen‐polyethylene surface is resistant to fluid wall shear rates of up to 550 s−1 and the fibrinogen does not desorb in the presence of plasma proteins. Compared to uncoated polyethylene, little albumin or fibrinogen adsorbs to heat‐denatured fibrinogen. Thrombin binds to the denatured fibrinogen‐coated polyethylene with low affinity and also acts on the surface‐bound denatured fibrinogen and cleaves fibrinopeptide A (FPA) quantitatively. Washed, 51Cr‐labeled platelets do not adhere to the thermally denatured fibrinogen at either low or high shear rates compared to surfaces coated with undenatured fibrinogen (p < 0.01). These observations support the role of the D domain of fibrinogen in platelet adhesion because this is the region that is denatured by heating. In contrast, the E domain of fibrinogen is not altered by heating to 70°C and hence remains susceptible to thrombin and/or plasmin cleavage. The characteristics of this surface are such that it can be used to develop fibrin‐coated surfaces for use in studies of thrombus formation on artificial surfaces. © 1992 John Wiley & Sons, Inc. |
| doi_str_mv | 10.1002/jbm.820261209 |
| format | Article |
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The denatured fibrinogen‐polyethylene surface is resistant to fluid wall shear rates of up to 550 s−1 and the fibrinogen does not desorb in the presence of plasma proteins. Compared to uncoated polyethylene, little albumin or fibrinogen adsorbs to heat‐denatured fibrinogen. Thrombin binds to the denatured fibrinogen‐coated polyethylene with low affinity and also acts on the surface‐bound denatured fibrinogen and cleaves fibrinopeptide A (FPA) quantitatively. Washed, 51Cr‐labeled platelets do not adhere to the thermally denatured fibrinogen at either low or high shear rates compared to surfaces coated with undenatured fibrinogen (p < 0.01). These observations support the role of the D domain of fibrinogen in platelet adhesion because this is the region that is denatured by heating. In contrast, the E domain of fibrinogen is not altered by heating to 70°C and hence remains susceptible to thrombin and/or plasmin cleavage. The characteristics of this surface are such that it can be used to develop fibrin‐coated surfaces for use in studies of thrombus formation on artificial surfaces. © 1992 John Wiley & Sons, Inc.</description><identifier>ISSN: 0021-9304</identifier><identifier>EISSN: 1097-4636</identifier><identifier>DOI: 10.1002/jbm.820261209</identifier><identifier>PMID: 1484068</identifier><identifier>CODEN: JBMRBG</identifier><language>eng</language><publisher>New York: John Wiley & Sons, Inc</publisher><subject>Absorption ; Biological and medical sciences ; Blood Proteins - chemistry ; Chromium Radioisotopes ; Fibrinogen - chemistry ; Fibrinolysin - chemistry ; Fibrinopeptide A - chemistry ; Hot Temperature ; Humans ; Iodine Radioisotopes ; Medical sciences ; Platelet Adhesiveness ; Polyethylenes - chemistry ; Protein Denaturation ; Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects) ; Technology. Biomaterials. Equipments. Material. Instrumentation ; Thrombin - chemistry</subject><ispartof>Journal of biomedical materials research, 1992-12, Vol.26 (12), p.1651-1663</ispartof><rights>Copyright © 1992 John Wiley & Sons, Inc.</rights><rights>1993 INIST-CNRS</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4659-cb7412754783b38fd949df58a9433ad8ff76fc9b582c2bc304c99a25b9298b8a3</citedby><cites>FETCH-LOGICAL-c4659-cb7412754783b38fd949df58a9433ad8ff76fc9b582c2bc304c99a25b9298b8a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjbm.820261209$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjbm.820261209$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4412385$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1484068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rubens, Fraser</creatorcontrib><creatorcontrib>Brash, John</creatorcontrib><creatorcontrib>Weitz, Jeff</creatorcontrib><creatorcontrib>Kinlough-Rathbone, Raelene</creatorcontrib><title>Interactions of thermally denatured fibrinogen on polyethylene with plasma proteins and platelets</title><title>Journal of biomedical materials research</title><addtitle>J. Biomed. Mater. Res</addtitle><description>During the investigation of fibrin deposition onto hydrophobic polymers in contact with human blood, a model was developed in which fibrinogen was denatured and irreversibly coated onto a polyethylene surface by heating to 70°C for 10 min. The denatured fibrinogen‐polyethylene surface is resistant to fluid wall shear rates of up to 550 s−1 and the fibrinogen does not desorb in the presence of plasma proteins. Compared to uncoated polyethylene, little albumin or fibrinogen adsorbs to heat‐denatured fibrinogen. Thrombin binds to the denatured fibrinogen‐coated polyethylene with low affinity and also acts on the surface‐bound denatured fibrinogen and cleaves fibrinopeptide A (FPA) quantitatively. Washed, 51Cr‐labeled platelets do not adhere to the thermally denatured fibrinogen at either low or high shear rates compared to surfaces coated with undenatured fibrinogen (p < 0.01). These observations support the role of the D domain of fibrinogen in platelet adhesion because this is the region that is denatured by heating. In contrast, the E domain of fibrinogen is not altered by heating to 70°C and hence remains susceptible to thrombin and/or plasmin cleavage. The characteristics of this surface are such that it can be used to develop fibrin‐coated surfaces for use in studies of thrombus formation on artificial surfaces. © 1992 John Wiley & Sons, Inc.</description><subject>Absorption</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - chemistry</subject><subject>Chromium Radioisotopes</subject><subject>Fibrinogen - chemistry</subject><subject>Fibrinolysin - chemistry</subject><subject>Fibrinopeptide A - chemistry</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Iodine Radioisotopes</subject><subject>Medical sciences</subject><subject>Platelet Adhesiveness</subject><subject>Polyethylenes - chemistry</subject><subject>Protein Denaturation</subject><subject>Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects)</subject><subject>Technology. Biomaterials. Equipments. Material. Instrumentation</subject><subject>Thrombin - chemistry</subject><issn>0021-9304</issn><issn>1097-4636</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvEzEUhS0EKqGwZIk0C8Ruit-PJVSkLbRlA-rS8nhs4uLxBNtRyb_HUaLAiq4s-Xw-9_geAF4jeIYgxO_vh-lMYog5wlA9AQsElegpJ_wpWDQd9YpA-hy8KOUeQqgUQSfgBFFJIZcLYK5SddnYGuZUutl3deXyZGLcdqNLpm6yGzsfhhzS_MOlbk7deo5bV1fb6JLrHkJddetoymS6dZ6rC83GpHF3V110tbwEz7yJxb06nKfg-_LTt_PL_vrrxdX5h-veUs5UbwdBERaMCkkGIv2oqBo9k0ZRQswovRfcWzUwiS0ebPuTVcpgNiis5CANOQXv9r4txq-NK1VPoVgXo0lu3hQtCIOMK_4oiJkQSCrxKIjakhGnrIH9HrR5LiU7r9c5TCZvNYJ6V5JuJeljSY1_czDeDJMb_9L7Vpr-9qCbYk302SQbyhGjbVFE7saKPfYQotv-f6b-_PHm3wCHwKFU9_v40uSfmgsimL67vdDk8ssdvF3e6CX5A1nmuhI</recordid><startdate>199212</startdate><enddate>199212</enddate><creator>Rubens, Fraser</creator><creator>Brash, John</creator><creator>Weitz, Jeff</creator><creator>Kinlough-Rathbone, Raelene</creator><general>John Wiley & Sons, Inc</general><general>John Wiley & Sons</general><scope>BSCLL</scope><scope>IQODW</scope><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7SR</scope><scope>JG9</scope><scope>7X8</scope></search><sort><creationdate>199212</creationdate><title>Interactions of thermally denatured fibrinogen on polyethylene with plasma proteins and platelets</title><author>Rubens, Fraser ; Brash, John ; Weitz, Jeff ; Kinlough-Rathbone, Raelene</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4659-cb7412754783b38fd949df58a9433ad8ff76fc9b582c2bc304c99a25b9298b8a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Absorption</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - chemistry</topic><topic>Chromium Radioisotopes</topic><topic>Fibrinogen - chemistry</topic><topic>Fibrinolysin - chemistry</topic><topic>Fibrinopeptide A - chemistry</topic><topic>Hot Temperature</topic><topic>Humans</topic><topic>Iodine Radioisotopes</topic><topic>Medical sciences</topic><topic>Platelet Adhesiveness</topic><topic>Polyethylenes - chemistry</topic><topic>Protein Denaturation</topic><topic>Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects)</topic><topic>Technology. Biomaterials. Equipments. Material. Instrumentation</topic><topic>Thrombin - chemistry</topic><toplevel>online_resources</toplevel><creatorcontrib>Rubens, Fraser</creatorcontrib><creatorcontrib>Brash, John</creatorcontrib><creatorcontrib>Weitz, Jeff</creatorcontrib><creatorcontrib>Kinlough-Rathbone, Raelene</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Research Database</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biomedical materials research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rubens, Fraser</au><au>Brash, John</au><au>Weitz, Jeff</au><au>Kinlough-Rathbone, Raelene</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interactions of thermally denatured fibrinogen on polyethylene with plasma proteins and platelets</atitle><jtitle>Journal of biomedical materials research</jtitle><addtitle>J. Biomed. Mater. Res</addtitle><date>1992-12</date><risdate>1992</risdate><volume>26</volume><issue>12</issue><spage>1651</spage><epage>1663</epage><pages>1651-1663</pages><issn>0021-9304</issn><eissn>1097-4636</eissn><coden>JBMRBG</coden><abstract>During the investigation of fibrin deposition onto hydrophobic polymers in contact with human blood, a model was developed in which fibrinogen was denatured and irreversibly coated onto a polyethylene surface by heating to 70°C for 10 min. The denatured fibrinogen‐polyethylene surface is resistant to fluid wall shear rates of up to 550 s−1 and the fibrinogen does not desorb in the presence of plasma proteins. Compared to uncoated polyethylene, little albumin or fibrinogen adsorbs to heat‐denatured fibrinogen. Thrombin binds to the denatured fibrinogen‐coated polyethylene with low affinity and also acts on the surface‐bound denatured fibrinogen and cleaves fibrinopeptide A (FPA) quantitatively. Washed, 51Cr‐labeled platelets do not adhere to the thermally denatured fibrinogen at either low or high shear rates compared to surfaces coated with undenatured fibrinogen (p < 0.01). These observations support the role of the D domain of fibrinogen in platelet adhesion because this is the region that is denatured by heating. In contrast, the E domain of fibrinogen is not altered by heating to 70°C and hence remains susceptible to thrombin and/or plasmin cleavage. The characteristics of this surface are such that it can be used to develop fibrin‐coated surfaces for use in studies of thrombus formation on artificial surfaces. © 1992 John Wiley & Sons, Inc.</abstract><cop>New York</cop><pub>John Wiley & Sons, Inc</pub><pmid>1484068</pmid><doi>10.1002/jbm.820261209</doi><tpages>13</tpages></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Absorption Biological and medical sciences Blood Proteins - chemistry Chromium Radioisotopes Fibrinogen - chemistry Fibrinolysin - chemistry Fibrinopeptide A - chemistry Hot Temperature Humans Iodine Radioisotopes Medical sciences Platelet Adhesiveness Polyethylenes - chemistry Protein Denaturation Radiotherapy. Instrumental treatment. Physiotherapy. Reeducation. Rehabilitation, orthophony, crenotherapy. Diet therapy and various other treatments (general aspects) Technology. Biomaterials. Equipments. Material. Instrumentation Thrombin - chemistry |
| title | Interactions of thermally denatured fibrinogen on polyethylene with plasma proteins and platelets |
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