Identification of a bone sialoprotein receptor in osteosarcoma cells
Bone sialoprotein (BSP) is an extracellular matrix glycoprotein associated with the mineral bone matrix. The amino acid sequence of BSP contains an Arg-Gly-Asp (RGD) sequence which confers to the protein cell binding properties (Oldberg, A., Franzén, A., and Heinegård, D. (1988) J. Biol. Chem. 263,...
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| Veröffentlicht in: | The Journal of biological chemistry 1988-12, Vol.263 (36), p.19433-19436 |
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| container_issue | 36 |
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| container_title | The Journal of biological chemistry |
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| creator | Oldberg, A Franzén, A Heinegård, D Pierschbacher, M Ruoslahti, E |
| description | Bone sialoprotein (BSP) is an extracellular matrix glycoprotein associated with the mineral bone matrix. The amino acid sequence of BSP contains an Arg-Gly-Asp (RGD) sequence which confers to the protein cell binding properties (Oldberg, A., Franzén, A., and Heinegård, D. (1988) J. Biol. Chem. 263, 19430-19432). When BSP was used as an affinity matrix to isolate a cell surface receptor from rat osteosarcoma cells, a protein composed of polypeptides similar in size to those of a previously characterized vitronectin receptor was obtained. This putative BSP receptor, like the vitronectin receptor, bound also to an affinity matrix made of an RGD-containing heptapeptide. Moreover, similar patterns of inhibition of cell attachment to BSP and vitronectin was obtained with variant RGD-containing peptides, with BSP and with vitronectin. Finally, an anti-vitronectin receptor antiserum immunoprecipitated a receptor identical in size to the receptor bound to a BSP affinity matrix. These results show that BSP is recognized by an RGD-directed receptor and that both vitronectin and BSP can bind to this receptor. |
| doi_str_mv | 10.1016/S0021-9258(19)77652-2 |
| format | Article |
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The amino acid sequence of BSP contains an Arg-Gly-Asp (RGD) sequence which confers to the protein cell binding properties (Oldberg, A., Franzén, A., and Heinegård, D. (1988) J. Biol. Chem. 263, 19430-19432). When BSP was used as an affinity matrix to isolate a cell surface receptor from rat osteosarcoma cells, a protein composed of polypeptides similar in size to those of a previously characterized vitronectin receptor was obtained. This putative BSP receptor, like the vitronectin receptor, bound also to an affinity matrix made of an RGD-containing heptapeptide. Moreover, similar patterns of inhibition of cell attachment to BSP and vitronectin was obtained with variant RGD-containing peptides, with BSP and with vitronectin. Finally, an anti-vitronectin receptor antiserum immunoprecipitated a receptor identical in size to the receptor bound to a BSP affinity matrix. These results show that BSP is recognized by an RGD-directed receptor and that both vitronectin and BSP can bind to this receptor.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)77652-2</identifier><identifier>PMID: 2461939</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; bone sialoprotein ; Cell Adhesion - drug effects ; Cell Line ; Cell receptors ; Cell structures and functions ; Chromatography, Affinity ; Epitopes - analysis ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - pharmacology ; Molecular and cellular biology ; Molecular Weight ; osteosarcoma ; Osteosarcoma - metabolism ; Osteosarcoma - pathology ; Rats ; Receptors, Immunologic - immunology ; Receptors, Immunologic - isolation & purification ; Receptors, Immunologic - metabolism ; Receptors, Vitronectin ; Vitronectin</subject><ispartof>The Journal of biological chemistry, 1988-12, Vol.263 (36), p.19433-19436</ispartof><rights>1988 © 1988 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3802-b8de3d05a327eaa11910cdbc21a72c0f800a3c50d600b787b479aca8da07cfdc3</citedby><cites>FETCH-LOGICAL-c3802-b8de3d05a327eaa11910cdbc21a72c0f800a3c50d600b787b479aca8da07cfdc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7245858$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2461939$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Oldberg, A</creatorcontrib><creatorcontrib>Franzén, A</creatorcontrib><creatorcontrib>Heinegård, D</creatorcontrib><creatorcontrib>Pierschbacher, M</creatorcontrib><creatorcontrib>Ruoslahti, E</creatorcontrib><title>Identification of a bone sialoprotein receptor in osteosarcoma cells</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Bone sialoprotein (BSP) is an extracellular matrix glycoprotein associated with the mineral bone matrix. The amino acid sequence of BSP contains an Arg-Gly-Asp (RGD) sequence which confers to the protein cell binding properties (Oldberg, A., Franzén, A., and Heinegård, D. (1988) J. Biol. Chem. 263, 19430-19432). When BSP was used as an affinity matrix to isolate a cell surface receptor from rat osteosarcoma cells, a protein composed of polypeptides similar in size to those of a previously characterized vitronectin receptor was obtained. This putative BSP receptor, like the vitronectin receptor, bound also to an affinity matrix made of an RGD-containing heptapeptide. Moreover, similar patterns of inhibition of cell attachment to BSP and vitronectin was obtained with variant RGD-containing peptides, with BSP and with vitronectin. Finally, an anti-vitronectin receptor antiserum immunoprecipitated a receptor identical in size to the receptor bound to a BSP affinity matrix. These results show that BSP is recognized by an RGD-directed receptor and that both vitronectin and BSP can bind to this receptor.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>bone sialoprotein</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Line</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Chromatography, Affinity</subject><subject>Epitopes - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - pharmacology</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>osteosarcoma</subject><subject>Osteosarcoma - metabolism</subject><subject>Osteosarcoma - pathology</subject><subject>Rats</subject><subject>Receptors, Immunologic - immunology</subject><subject>Receptors, Immunologic - isolation & purification</subject><subject>Receptors, Immunologic - metabolism</subject><subject>Receptors, Vitronectin</subject><subject>Vitronectin</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE2LFDEQhoMo67j6Exb6IKKH1krS6U6fRNavhQUPKngL1ZVqJ9LdGZMexX9vZmcYj-aSQD1v6uUR4krCSwmyffUZQMm6V8Y-l_2LrmuNqtU9sZFgda2N_HZfbM7IQ_Eo5x9QTtPLC3Ghmlb2ut-ItzeelzWMgXANcaniWGE1xIWrHHCKuxRXDkuVmHi3xlSVd8wrx4yJ4owV8TTlx-LBiFPmJ6f7Unx9_-7L9cf69tOHm-s3tzVpC6oerGftwaBWHSNK2UsgP5CS2CmC0QKgJgO-BRg62w1N1yOh9QgdjZ70pXh2_LfU-rnnvLo55EMDXDjus5NGGgCtCmiOIKWYc-LR7VKYMf1xEtzBnruz5w5qnOzdnT13yF2dFuyHmf05ddJV5k9Pc8yE05hwoZDPWKcaY439h23D9-3vkNgNIdKWZ6da7XRbVjZaF-z1EePi7Ffg5DIFXoh9idDqfAz_6fsXX4SXww</recordid><startdate>19881225</startdate><enddate>19881225</enddate><creator>Oldberg, A</creator><creator>Franzén, A</creator><creator>Heinegård, D</creator><creator>Pierschbacher, M</creator><creator>Ruoslahti, E</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7QP</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope></search><sort><creationdate>19881225</creationdate><title>Identification of a bone sialoprotein receptor in osteosarcoma cells</title><author>Oldberg, A ; Franzén, A ; Heinegård, D ; Pierschbacher, M ; Ruoslahti, E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3802-b8de3d05a327eaa11910cdbc21a72c0f800a3c50d600b787b479aca8da07cfdc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>bone sialoprotein</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Line</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Chromatography, Affinity</topic><topic>Epitopes - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - pharmacology</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>osteosarcoma</topic><topic>Osteosarcoma - metabolism</topic><topic>Osteosarcoma - pathology</topic><topic>Rats</topic><topic>Receptors, Immunologic - immunology</topic><topic>Receptors, Immunologic - isolation & purification</topic><topic>Receptors, Immunologic - metabolism</topic><topic>Receptors, Vitronectin</topic><topic>Vitronectin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Oldberg, A</creatorcontrib><creatorcontrib>Franzén, A</creatorcontrib><creatorcontrib>Heinegård, D</creatorcontrib><creatorcontrib>Pierschbacher, M</creatorcontrib><creatorcontrib>Ruoslahti, E</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Calcium & Calcified Tissue Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Oldberg, A</au><au>Franzén, A</au><au>Heinegård, D</au><au>Pierschbacher, M</au><au>Ruoslahti, E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of a bone sialoprotein receptor in osteosarcoma cells</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-12-25</date><risdate>1988</risdate><volume>263</volume><issue>36</issue><spage>19433</spage><epage>19436</epage><pages>19433-19436</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Bone sialoprotein (BSP) is an extracellular matrix glycoprotein associated with the mineral bone matrix. The amino acid sequence of BSP contains an Arg-Gly-Asp (RGD) sequence which confers to the protein cell binding properties (Oldberg, A., Franzén, A., and Heinegård, D. (1988) J. Biol. Chem. 263, 19430-19432). When BSP was used as an affinity matrix to isolate a cell surface receptor from rat osteosarcoma cells, a protein composed of polypeptides similar in size to those of a previously characterized vitronectin receptor was obtained. This putative BSP receptor, like the vitronectin receptor, bound also to an affinity matrix made of an RGD-containing heptapeptide. Moreover, similar patterns of inhibition of cell attachment to BSP and vitronectin was obtained with variant RGD-containing peptides, with BSP and with vitronectin. Finally, an anti-vitronectin receptor antiserum immunoprecipitated a receptor identical in size to the receptor bound to a BSP affinity matrix. These results show that BSP is recognized by an RGD-directed receptor and that both vitronectin and BSP can bind to this receptor.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2461939</pmid><doi>10.1016/S0021-9258(19)77652-2</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1988-12, Vol.263 (36), p.19433-19436 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Biological and medical sciences bone sialoprotein Cell Adhesion - drug effects Cell Line Cell receptors Cell structures and functions Chromatography, Affinity Epitopes - analysis Fundamental and applied biological sciences. Psychology Glycoproteins - pharmacology Molecular and cellular biology Molecular Weight osteosarcoma Osteosarcoma - metabolism Osteosarcoma - pathology Rats Receptors, Immunologic - immunology Receptors, Immunologic - isolation & purification Receptors, Immunologic - metabolism Receptors, Vitronectin Vitronectin |
| title | Identification of a bone sialoprotein receptor in osteosarcoma cells |
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