The collagen receptor alpha 2 beta 1, from MG-63 and HT1080 cells, interacts with a cyclic RGD peptide
Several receptors for the extracellular matrix protein collagen have been described which belong to the superfamily of receptors collectively known as integrins. Although several integrins have been shown to interact with extracellular matrix molecules via a common recognition site, arginine-glycine...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-11, Vol.267 (32), p.23159-23164 |
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| creator | Cardarelli, P M Yamagata, S Taguchi, I Gorcsan, F Chiang, S L Lobl, T |
| description | Several receptors for the extracellular matrix protein collagen have been described which belong to the superfamily of receptors
collectively known as integrins. Although several integrins have been shown to interact with extracellular matrix molecules
via a common recognition site, arginine-glycine-aspartic Acid (RGD), within the beta 1 integrin subfamily, only the fibronectin
receptor (alpha 5 beta 1) has been convincingly shown to interact with RGD. In the present study, we tested whether a collagen
receptor could interact with RGD. Adhesion of an osteosarcoma cell line, MG-63, to immobilized collagen I was inhibited by
the cyclic RGD-containing peptide, C*GRGDSPC* (where C* indicates that Cys participates in disulfide), and not by the linear
GRGDSP or the non-RGD-containing cyclic peptide, C*GKGESPC*. Similarly, using collagen-Sepharose affinity chromatography,
a heterodimeric protein could be specifically eluted from the column by the cyclic RGD peptide. Immunoprecipitations of the
eluted material with monoclonal antibodies showed reactivity with the collagen receptor alpha 2 beta 1 and not alpha 3 beta
1. Our data demonstrate that RGD peptides can interact with the collagen receptor, and the differences seen with the linear
and cyclic peptide suggest that the cyclic C*GRGDSPC* has a higher avidity for the receptor than the more flexible linear
GRGDSP. In this paper, we provide supportive evidence that one possible mode of collagen interaction with alpha 2 beta 1 is
via the RGD recognition sequence. |
| doi_str_mv | 10.1016/S0021-9258(18)50070-3 |
| format | Article |
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collectively known as integrins. Although several integrins have been shown to interact with extracellular matrix molecules
via a common recognition site, arginine-glycine-aspartic Acid (RGD), within the beta 1 integrin subfamily, only the fibronectin
receptor (alpha 5 beta 1) has been convincingly shown to interact with RGD. In the present study, we tested whether a collagen
receptor could interact with RGD. Adhesion of an osteosarcoma cell line, MG-63, to immobilized collagen I was inhibited by
the cyclic RGD-containing peptide, C*GRGDSPC* (where C* indicates that Cys participates in disulfide), and not by the linear
GRGDSP or the non-RGD-containing cyclic peptide, C*GKGESPC*. Similarly, using collagen-Sepharose affinity chromatography,
a heterodimeric protein could be specifically eluted from the column by the cyclic RGD peptide. Immunoprecipitations of the
eluted material with monoclonal antibodies showed reactivity with the collagen receptor alpha 2 beta 1 and not alpha 3 beta
1. Our data demonstrate that RGD peptides can interact with the collagen receptor, and the differences seen with the linear
and cyclic peptide suggest that the cyclic C*GRGDSPC* has a higher avidity for the receptor than the more flexible linear
GRGDSP. In this paper, we provide supportive evidence that one possible mode of collagen interaction with alpha 2 beta 1 is
via the RGD recognition sequence.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)50070-3</identifier><identifier>PMID: 1331077</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Cell Adhesion - drug effects ; Chromatography, Affinity ; collagen ; Collagen - metabolism ; Fibrosarcoma ; HT1080 cells ; Humans ; integrin ; interaction ; Kinetics ; man ; membrane proteins ; MG-63 cells ; Molecular Sequence Data ; Oligopeptides - chemical synthesis ; Oligopeptides - metabolism ; Oligopeptides - pharmacology ; Osteosarcoma ; peptides ; Peptides, Cyclic - chemical synthesis ; Peptides, Cyclic - metabolism ; Peptides, Cyclic - pharmacology ; receptors ; Receptors, Cell Surface - drug effects ; Receptors, Cell Surface - isolation & purification ; Receptors, Cell Surface - metabolism ; Receptors, Collagen ; Tumor Cells, Cultured</subject><ispartof>The Journal of biological chemistry, 1992-11, Vol.267 (32), p.23159-23164</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c343t-60b83f0d8dd64041d3495a1cfa3d3f3fc8fc66bbeef83bc78e9c074a8d55ea0e3</citedby><cites>FETCH-LOGICAL-c343t-60b83f0d8dd64041d3495a1cfa3d3f3fc8fc66bbeef83bc78e9c074a8d55ea0e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1331077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cardarelli, P M</creatorcontrib><creatorcontrib>Yamagata, S</creatorcontrib><creatorcontrib>Taguchi, I</creatorcontrib><creatorcontrib>Gorcsan, F</creatorcontrib><creatorcontrib>Chiang, S L</creatorcontrib><creatorcontrib>Lobl, T</creatorcontrib><title>The collagen receptor alpha 2 beta 1, from MG-63 and HT1080 cells, interacts with a cyclic RGD peptide</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Several receptors for the extracellular matrix protein collagen have been described which belong to the superfamily of receptors
collectively known as integrins. Although several integrins have been shown to interact with extracellular matrix molecules
via a common recognition site, arginine-glycine-aspartic Acid (RGD), within the beta 1 integrin subfamily, only the fibronectin
receptor (alpha 5 beta 1) has been convincingly shown to interact with RGD. In the present study, we tested whether a collagen
receptor could interact with RGD. Adhesion of an osteosarcoma cell line, MG-63, to immobilized collagen I was inhibited by
the cyclic RGD-containing peptide, C*GRGDSPC* (where C* indicates that Cys participates in disulfide), and not by the linear
GRGDSP or the non-RGD-containing cyclic peptide, C*GKGESPC*. Similarly, using collagen-Sepharose affinity chromatography,
a heterodimeric protein could be specifically eluted from the column by the cyclic RGD peptide. Immunoprecipitations of the
eluted material with monoclonal antibodies showed reactivity with the collagen receptor alpha 2 beta 1 and not alpha 3 beta
1. Our data demonstrate that RGD peptides can interact with the collagen receptor, and the differences seen with the linear
and cyclic peptide suggest that the cyclic C*GRGDSPC* has a higher avidity for the receptor than the more flexible linear
GRGDSP. In this paper, we provide supportive evidence that one possible mode of collagen interaction with alpha 2 beta 1 is
via the RGD recognition sequence.</description><subject>Amino Acid Sequence</subject><subject>Cell Adhesion - drug effects</subject><subject>Chromatography, Affinity</subject><subject>collagen</subject><subject>Collagen - metabolism</subject><subject>Fibrosarcoma</subject><subject>HT1080 cells</subject><subject>Humans</subject><subject>integrin</subject><subject>interaction</subject><subject>Kinetics</subject><subject>man</subject><subject>membrane proteins</subject><subject>MG-63 cells</subject><subject>Molecular Sequence Data</subject><subject>Oligopeptides - chemical synthesis</subject><subject>Oligopeptides - metabolism</subject><subject>Oligopeptides - pharmacology</subject><subject>Osteosarcoma</subject><subject>peptides</subject><subject>Peptides, Cyclic - chemical synthesis</subject><subject>Peptides, Cyclic - metabolism</subject><subject>Peptides, Cyclic - pharmacology</subject><subject>receptors</subject><subject>Receptors, Cell Surface - drug effects</subject><subject>Receptors, Cell Surface - isolation & purification</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Collagen</subject><subject>Tumor Cells, Cultured</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUU1v1DAQtRBV2RZ-QiUfEAKpKeNM7DhHVOgWqRUSLBI3y7HHjVGyCXZWVf99s90KjsxlDvM-Ru8xdibgQoBQH38AlKJoSqnfC_1BAtRQ4Au2EqCxQCl-vWSrv5BX7CTn37BM1YhjdiwQBdT1ioVNR9yNfW_vaMsTOZrmMXHbT53lJW9ptlyc85DGgd-uC4Xcbj2_3iwuwB31fT7ncTtTsm7O_D7OHbfcPbg-Ov59_ZlPi1709JodBdtnevO8T9nPqy-by-vi5tv66-Wnm8JhhXOhoNUYwGvvVQWV8Fg10goXLHoMGJwOTqm2JQoaW1drahzUldVeSrJAeMreHXSnNP7ZUZ7NEPP-TbulcZdNjWVTI8j_AoWSVamqagHKA9ClMedEwUwpDjY9GAFmX4R5KsLsUzZCm6ciDC68s2eDXTuQ_8c6JL_c3x7uXbzr7mMi08bRdTSYUtUGS1OikA0-Atz2jRE</recordid><startdate>19921115</startdate><enddate>19921115</enddate><creator>Cardarelli, P M</creator><creator>Yamagata, S</creator><creator>Taguchi, I</creator><creator>Gorcsan, F</creator><creator>Chiang, S L</creator><creator>Lobl, T</creator><general>American Society for Biochemistry and Molecular Biology</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19921115</creationdate><title>The collagen receptor alpha 2 beta 1, from MG-63 and HT1080 cells, interacts with a cyclic RGD peptide</title><author>Cardarelli, P M ; Yamagata, S ; Taguchi, I ; Gorcsan, F ; Chiang, S L ; Lobl, T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c343t-60b83f0d8dd64041d3495a1cfa3d3f3fc8fc66bbeef83bc78e9c074a8d55ea0e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Cell Adhesion - drug effects</topic><topic>Chromatography, Affinity</topic><topic>collagen</topic><topic>Collagen - metabolism</topic><topic>Fibrosarcoma</topic><topic>HT1080 cells</topic><topic>Humans</topic><topic>integrin</topic><topic>interaction</topic><topic>Kinetics</topic><topic>man</topic><topic>membrane proteins</topic><topic>MG-63 cells</topic><topic>Molecular Sequence Data</topic><topic>Oligopeptides - chemical synthesis</topic><topic>Oligopeptides - metabolism</topic><topic>Oligopeptides - pharmacology</topic><topic>Osteosarcoma</topic><topic>peptides</topic><topic>Peptides, Cyclic - chemical synthesis</topic><topic>Peptides, Cyclic - metabolism</topic><topic>Peptides, Cyclic - pharmacology</topic><topic>receptors</topic><topic>Receptors, Cell Surface - drug effects</topic><topic>Receptors, Cell Surface - isolation & purification</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Collagen</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cardarelli, P M</creatorcontrib><creatorcontrib>Yamagata, S</creatorcontrib><creatorcontrib>Taguchi, I</creatorcontrib><creatorcontrib>Gorcsan, F</creatorcontrib><creatorcontrib>Chiang, S L</creatorcontrib><creatorcontrib>Lobl, T</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cardarelli, P M</au><au>Yamagata, S</au><au>Taguchi, I</au><au>Gorcsan, F</au><au>Chiang, S L</au><au>Lobl, T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The collagen receptor alpha 2 beta 1, from MG-63 and HT1080 cells, interacts with a cyclic RGD peptide</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-11-15</date><risdate>1992</risdate><volume>267</volume><issue>32</issue><spage>23159</spage><epage>23164</epage><pages>23159-23164</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Several receptors for the extracellular matrix protein collagen have been described which belong to the superfamily of receptors
collectively known as integrins. Although several integrins have been shown to interact with extracellular matrix molecules
via a common recognition site, arginine-glycine-aspartic Acid (RGD), within the beta 1 integrin subfamily, only the fibronectin
receptor (alpha 5 beta 1) has been convincingly shown to interact with RGD. In the present study, we tested whether a collagen
receptor could interact with RGD. Adhesion of an osteosarcoma cell line, MG-63, to immobilized collagen I was inhibited by
the cyclic RGD-containing peptide, C*GRGDSPC* (where C* indicates that Cys participates in disulfide), and not by the linear
GRGDSP or the non-RGD-containing cyclic peptide, C*GKGESPC*. Similarly, using collagen-Sepharose affinity chromatography,
a heterodimeric protein could be specifically eluted from the column by the cyclic RGD peptide. Immunoprecipitations of the
eluted material with monoclonal antibodies showed reactivity with the collagen receptor alpha 2 beta 1 and not alpha 3 beta
1. Our data demonstrate that RGD peptides can interact with the collagen receptor, and the differences seen with the linear
and cyclic peptide suggest that the cyclic C*GRGDSPC* has a higher avidity for the receptor than the more flexible linear
GRGDSP. In this paper, we provide supportive evidence that one possible mode of collagen interaction with alpha 2 beta 1 is
via the RGD recognition sequence.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1331077</pmid><doi>10.1016/S0021-9258(18)50070-3</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1992-11, Vol.267 (32), p.23159-23164 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73297305 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Amino Acid Sequence Cell Adhesion - drug effects Chromatography, Affinity collagen Collagen - metabolism Fibrosarcoma HT1080 cells Humans integrin interaction Kinetics man membrane proteins MG-63 cells Molecular Sequence Data Oligopeptides - chemical synthesis Oligopeptides - metabolism Oligopeptides - pharmacology Osteosarcoma peptides Peptides, Cyclic - chemical synthesis Peptides, Cyclic - metabolism Peptides, Cyclic - pharmacology receptors Receptors, Cell Surface - drug effects Receptors, Cell Surface - isolation & purification Receptors, Cell Surface - metabolism Receptors, Collagen Tumor Cells, Cultured |
| title | The collagen receptor alpha 2 beta 1, from MG-63 and HT1080 cells, interacts with a cyclic RGD peptide |
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