Fibulin, a novel protein that interacts with the fibronectin receptor β subunit cytoplasmic domain
A 100 kd protein was isolated from tissue and cell extracts by affinity chromatography on a synthetic peptide representing the cytoplasmic domain of the fibronectin receptor β subunit. The 100 kd protein also bound to native fibronectin receptor, and this binding could be reversed with EDTA. Calcium...
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| Veröffentlicht in: | Cell 1989-08, Vol.58 (4), p.623-629 |
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| container_title | Cell |
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| creator | Argraves, W.Scott Dickerson, Kenneth Burgess, Wilson H. Ruoslahti, Erkki |
| description | A 100 kd protein was isolated from tissue and cell extracts by affinity chromatography on a synthetic peptide representing the cytoplasmic domain of the fibronectin receptor β subunit. The 100 kd protein also bound to native fibronectin receptor, and this binding could be reversed with EDTA. Calcium may be the divalent cation required for the binding since the 100 kd protein was found to bind
45Ca
2+. The N-terminal amino acid sequence of the 100 kd protein was not similar to any sequence in a protein data base. Immunofluorescent staining of cells cultured on fibronectin showed the 100 kd protein coinciding with the fibronectin receptor β subunit in sites of substrate contact. Therefore this protein, which we term fibulin, interacts with the fibronectin receptor in vitro and associates with the receptor in vivo. Fibulin is a potential mediator of interactions between adhesion receptors and the cytoskeleton. |
| doi_str_mv | 10.1016/0092-8674(89)90097-4 |
| format | Article |
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45Ca
2+. The N-terminal amino acid sequence of the 100 kd protein was not similar to any sequence in a protein data base. Immunofluorescent staining of cells cultured on fibronectin showed the 100 kd protein coinciding with the fibronectin receptor β subunit in sites of substrate contact. Therefore this protein, which we term fibulin, interacts with the fibronectin receptor in vitro and associates with the receptor in vivo. Fibulin is a potential mediator of interactions between adhesion receptors and the cytoskeleton.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/0092-8674(89)90097-4</identifier><identifier>PMID: 2527614</identifier><identifier>CODEN: CELLB5</identifier><language>eng</language><publisher>Cambridge, MA: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Calcium-Binding Proteins - physiology ; Cell Compartmentation ; Chromatography, Affinity ; Cytoplasm - physiology ; Cytoskeleton - physiology ; fibronectin ; Fibronectins - physiology ; Fluorescent Antibody Technique ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Humans ; Molecular Sequence Data ; Precipitin Tests ; Proteins ; Receptors, Fibronectin ; Receptors, Immunologic - physiology ; Receptors, Immunologic - ultrastructure</subject><ispartof>Cell, 1989-08, Vol.58 (4), p.623-629</ispartof><rights>1989</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-874dd42a97af266b215e9474bb31f9b1846410783123da16593a9eb42dc4fb8b3</citedby><cites>FETCH-LOGICAL-c417t-874dd42a97af266b215e9474bb31f9b1846410783123da16593a9eb42dc4fb8b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0092-8674(89)90097-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6881159$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2527614$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Argraves, W.Scott</creatorcontrib><creatorcontrib>Dickerson, Kenneth</creatorcontrib><creatorcontrib>Burgess, Wilson H.</creatorcontrib><creatorcontrib>Ruoslahti, Erkki</creatorcontrib><title>Fibulin, a novel protein that interacts with the fibronectin receptor β subunit cytoplasmic domain</title><title>Cell</title><addtitle>Cell</addtitle><description>A 100 kd protein was isolated from tissue and cell extracts by affinity chromatography on a synthetic peptide representing the cytoplasmic domain of the fibronectin receptor β subunit. The 100 kd protein also bound to native fibronectin receptor, and this binding could be reversed with EDTA. Calcium may be the divalent cation required for the binding since the 100 kd protein was found to bind
45Ca
2+. The N-terminal amino acid sequence of the 100 kd protein was not similar to any sequence in a protein data base. Immunofluorescent staining of cells cultured on fibronectin showed the 100 kd protein coinciding with the fibronectin receptor β subunit in sites of substrate contact. Therefore this protein, which we term fibulin, interacts with the fibronectin receptor in vitro and associates with the receptor in vivo. Fibulin is a potential mediator of interactions between adhesion receptors and the cytoskeleton.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Calcium-Binding Proteins - physiology</subject><subject>Cell Compartmentation</subject><subject>Chromatography, Affinity</subject><subject>Cytoplasm - physiology</subject><subject>Cytoskeleton - physiology</subject><subject>fibronectin</subject><subject>Fibronectins - physiology</subject><subject>Fluorescent Antibody Technique</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Precipitin Tests</subject><subject>Proteins</subject><subject>Receptors, Fibronectin</subject><subject>Receptors, Immunologic - physiology</subject><subject>Receptors, Immunologic - ultrastructure</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1q3DAQgEVpSTebvkEKOpSSQJ1KsmxJl0AJSVsI9NKehSSPiYItbSU5Ia_VB-kzRZtd9tie9DPfDDPfIHRKyQUltP9MiGKN7AU_k-pc1Zdo-Cu0oi8XKthrtDogb9FxzveEENl13RE6Yh0TPeUr5G68XSYfPmGDQ3yACW9SLOADLnemYB8KJONKxo--3NU_wKO3KQZwpTIJHGxKTPjvH5wXuwRfsHsqcTOZPHuHhzgbH07Qm9FMGd7tzzX6dXP98-pbc_vj6_erL7eNq-2WRgo-DJwZJczI-t4y2oHiglvb0lFZKnnPKRGypawdDO071RoFlrPB8dFK267Rx13dOsLvBXLRs88OpskEiEvWQlFBBBf_BWnXilYSVkG-A12KOScY9Sb52aQnTYneLkFvDeutYS2VflmC5jXt_b7-YmcYDkl76zX-YR832ZlpTCY4nw9YLyWldbo1utxhUKU9eEg6Ow_BweCr-KKH6P_dxzMYd6Pn</recordid><startdate>19890825</startdate><enddate>19890825</enddate><creator>Argraves, W.Scott</creator><creator>Dickerson, Kenneth</creator><creator>Burgess, Wilson H.</creator><creator>Ruoslahti, Erkki</creator><general>Elsevier Inc</general><general>Cell Press</general><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890825</creationdate><title>Fibulin, a novel protein that interacts with the fibronectin receptor β subunit cytoplasmic domain</title><author>Argraves, W.Scott ; Dickerson, Kenneth ; Burgess, Wilson H. ; Ruoslahti, Erkki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-874dd42a97af266b215e9474bb31f9b1846410783123da16593a9eb42dc4fb8b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Calcium-Binding Proteins - physiology</topic><topic>Cell Compartmentation</topic><topic>Chromatography, Affinity</topic><topic>Cytoplasm - physiology</topic><topic>Cytoskeleton - physiology</topic><topic>fibronectin</topic><topic>Fibronectins - physiology</topic><topic>Fluorescent Antibody Technique</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Precipitin Tests</topic><topic>Proteins</topic><topic>Receptors, Fibronectin</topic><topic>Receptors, Immunologic - physiology</topic><topic>Receptors, Immunologic - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Argraves, W.Scott</creatorcontrib><creatorcontrib>Dickerson, Kenneth</creatorcontrib><creatorcontrib>Burgess, Wilson H.</creatorcontrib><creatorcontrib>Ruoslahti, Erkki</creatorcontrib><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Argraves, W.Scott</au><au>Dickerson, Kenneth</au><au>Burgess, Wilson H.</au><au>Ruoslahti, Erkki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Fibulin, a novel protein that interacts with the fibronectin receptor β subunit cytoplasmic domain</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1989-08-25</date><risdate>1989</risdate><volume>58</volume><issue>4</issue><spage>623</spage><epage>629</epage><pages>623-629</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><abstract>A 100 kd protein was isolated from tissue and cell extracts by affinity chromatography on a synthetic peptide representing the cytoplasmic domain of the fibronectin receptor β subunit. The 100 kd protein also bound to native fibronectin receptor, and this binding could be reversed with EDTA. Calcium may be the divalent cation required for the binding since the 100 kd protein was found to bind
45Ca
2+. The N-terminal amino acid sequence of the 100 kd protein was not similar to any sequence in a protein data base. Immunofluorescent staining of cells cultured on fibronectin showed the 100 kd protein coinciding with the fibronectin receptor β subunit in sites of substrate contact. Therefore this protein, which we term fibulin, interacts with the fibronectin receptor in vitro and associates with the receptor in vivo. Fibulin is a potential mediator of interactions between adhesion receptors and the cytoskeleton.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>2527614</pmid><doi>10.1016/0092-8674(89)90097-4</doi><tpages>7</tpages></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Calcium-Binding Proteins - physiology Cell Compartmentation Chromatography, Affinity Cytoplasm - physiology Cytoskeleton - physiology fibronectin Fibronectins - physiology Fluorescent Antibody Technique Fundamental and applied biological sciences. Psychology Glycoproteins Humans Molecular Sequence Data Precipitin Tests Proteins Receptors, Fibronectin Receptors, Immunologic - physiology Receptors, Immunologic - ultrastructure |
| title | Fibulin, a novel protein that interacts with the fibronectin receptor β subunit cytoplasmic domain |
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