The alpha v beta 3 integrin "vitronectin receptor"
The alpha v beta 3 "vitronectin receptor" is a member of the integrin superfamily of adhesion molecules. As such, this 160/85 kDa heterodimeric protein exhibits many of the typical structural and functional features of integrins. It mediates cell adhesion to extracellular matrix by recogni...
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| Veröffentlicht in: | The international journal of biochemistry & cell biology 1997-05, Vol.29 (5), p.721 |
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| container_title | The international journal of biochemistry & cell biology |
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| creator | Horton, M A |
| description | The alpha v beta 3 "vitronectin receptor" is a member of the integrin superfamily of adhesion molecules. As such, this 160/85 kDa heterodimeric protein exhibits many of the typical structural and functional features of integrins. It mediates cell adhesion to extracellular matrix by recognizing the conserved arg-gly-asp (RGD) sequence of several plasma and matrix proteins. Recently, it has also been shown that alpha v beta 3 is involved in signal transduction and cell to cell interactions. alpha v beta 3 is highly expressed in bone resorbing cells, osteoclasts, and upregulated in response to vascular damage, during angiogenesis and in certain types of malignancy. Antagonists of alpha v beta 3 are being developed for use in a variety of diseases associated with altered receptor function or level. |
| doi_str_mv | 10.1016/S1357-2725(96)00155-0 |
| format | Article |
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As such, this 160/85 kDa heterodimeric protein exhibits many of the typical structural and functional features of integrins. It mediates cell adhesion to extracellular matrix by recognizing the conserved arg-gly-asp (RGD) sequence of several plasma and matrix proteins. Recently, it has also been shown that alpha v beta 3 is involved in signal transduction and cell to cell interactions. alpha v beta 3 is highly expressed in bone resorbing cells, osteoclasts, and upregulated in response to vascular damage, during angiogenesis and in certain types of malignancy. Antagonists of alpha v beta 3 are being developed for use in a variety of diseases associated with altered receptor function or level.</description><subject>Animals</subject><subject>Humans</subject><subject>Models, Molecular</subject><subject>Mutagenesis, Site-Directed</subject><subject>Receptors, Vitronectin - chemistry</subject><subject>Receptors, Vitronectin - genetics</subject><subject>Receptors, Vitronectin - physiology</subject><issn>1357-2725</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9jk1LAzEURbNQaq3-hELoShexee8lM8lSil9Q6MK6Li8zGTvSTodMLPjvVSyuLvdcOFwhpqDvQEMxfwWypcIS7Y0vbrUGa5U-E-N_fCEuh-FD_y5IIzHyaAHJjwWut1Hyrt-yPMoQM0uSbZfje2o7OTu2OR26WOWfkmIV-3xIsytx3vBuiNennIi3x4f14lktV08vi_ul6oFcVsQlB9ZBO3QGa6yISuPAI7Nh19TgLDbONNaAL5gaY6KtwMZgQlWSNzQR0z9v_xn2sd70qd1z-tqcvtM3bH1DKQ</recordid><startdate>199705</startdate><enddate>199705</enddate><creator>Horton, M A</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>199705</creationdate><title>The alpha v beta 3 integrin "vitronectin receptor"</title><author>Horton, M A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p138t-3a7aba0b082842d2c33748192aa4a8fd1852f84f54196a3f44e5c15eb4bc73943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Humans</topic><topic>Models, Molecular</topic><topic>Mutagenesis, Site-Directed</topic><topic>Receptors, Vitronectin - chemistry</topic><topic>Receptors, Vitronectin - genetics</topic><topic>Receptors, Vitronectin - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Horton, M A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>The international journal of biochemistry & cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Horton, M A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The alpha v beta 3 integrin "vitronectin receptor"</atitle><jtitle>The international journal of biochemistry & cell biology</jtitle><addtitle>Int J Biochem Cell Biol</addtitle><date>1997-05</date><risdate>1997</risdate><volume>29</volume><issue>5</issue><spage>721</spage><pages>721-</pages><issn>1357-2725</issn><abstract>The alpha v beta 3 "vitronectin receptor" is a member of the integrin superfamily of adhesion molecules. As such, this 160/85 kDa heterodimeric protein exhibits many of the typical structural and functional features of integrins. It mediates cell adhesion to extracellular matrix by recognizing the conserved arg-gly-asp (RGD) sequence of several plasma and matrix proteins. Recently, it has also been shown that alpha v beta 3 is involved in signal transduction and cell to cell interactions. alpha v beta 3 is highly expressed in bone resorbing cells, osteoclasts, and upregulated in response to vascular damage, during angiogenesis and in certain types of malignancy. Antagonists of alpha v beta 3 are being developed for use in a variety of diseases associated with altered receptor function or level.</abstract><cop>Netherlands</cop><pmid>9251239</pmid><doi>10.1016/S1357-2725(96)00155-0</doi></addata></record> |
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| identifier | ISSN: 1357-2725 |
| ispartof | The international journal of biochemistry & cell biology, 1997-05, Vol.29 (5), p.721 |
| issn | 1357-2725 |
| language | eng |
| recordid | cdi_pubmed_primary_9251239 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals Humans Models, Molecular Mutagenesis, Site-Directed Receptors, Vitronectin - chemistry Receptors, Vitronectin - genetics Receptors, Vitronectin - physiology |
| title | The alpha v beta 3 integrin "vitronectin receptor" |
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