Thrombospondin 1 and thrombospondin 2 are expressed as both homo- and heterotrimers
There exist two distinct thrombospondin molecules (designated TSP1 and TSP2) which are encoded by separate genes. TSP1 is a trimeric cell surface and extracellular matrix molecule. Sequence comparison reveals that the 2 cysteines involved in interchain disulfide linkage and trimer assembly in TSP1 a...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-12, Vol.267 (35), p.24921-24924 |
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| creator | O'ROURKE, K. M LAHERTY, C. D DIXIT, V. M |
| description | There exist two distinct thrombospondin molecules (designated TSP1 and TSP2) which are encoded by separate genes. TSP1 is
a trimeric cell surface and extracellular matrix molecule. Sequence comparison reveals that the 2 cysteines involved in interchain
disulfide linkage and trimer assembly in TSP1 are conserved in TSP2 (Laherty, C. D., O'Rourke, K., Wolf, F. W., Katz, R.,
Seldin, M. F., and Dixit, V. M. (1992) J. Biol. Chem. 267, 3274-3281). Swiss 3T3 fibroblasts express both TSP1 and TSP2, and,
therefore, an important question is whether TSP in such cells is expressed as homotrimers or as heterotrimers. We find that
Swiss 3T3 cells and epithelial cells transfected with TSP expression vectors express both homo- and heterotrimeric forms of
TSP. In addition, homotrimeric TSP2 has a lower affinity for heparin than homotrimeric TSP1. Thus, the heparin affinity of
TSP can be modulated by the expression of TSP as homo- or heterotrimers. |
| doi_str_mv | 10.1016/S0021-9258(19)73983-0 |
| format | Article |
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a trimeric cell surface and extracellular matrix molecule. Sequence comparison reveals that the 2 cysteines involved in interchain
disulfide linkage and trimer assembly in TSP1 are conserved in TSP2 (Laherty, C. D., O'Rourke, K., Wolf, F. W., Katz, R.,
Seldin, M. F., and Dixit, V. M. (1992) J. Biol. Chem. 267, 3274-3281). Swiss 3T3 fibroblasts express both TSP1 and TSP2, and,
therefore, an important question is whether TSP in such cells is expressed as homotrimers or as heterotrimers. We find that
Swiss 3T3 cells and epithelial cells transfected with TSP expression vectors express both homo- and heterotrimeric forms of
TSP. In addition, homotrimeric TSP2 has a lower affinity for heparin than homotrimeric TSP1. Thus, the heparin affinity of
TSP can be modulated by the expression of TSP as homo- or heterotrimers.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)73983-0</identifier><identifier>PMID: 1459996</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>3T3 Cells ; Analytical, structural and metabolic biochemistry ; Animals ; Antibody Specificity ; Biological and medical sciences ; Blotting, Western ; Chromatography, Affinity ; Cloning, Molecular ; Cysteine - metabolism ; Escherichia coli - genetics ; expression ; extracellular matrix ; Fundamental and applied biological sciences. Psychology ; Genetic Vectors ; Glycoproteins ; Immunoassay ; Lectins - biosynthesis ; Lectins - genetics ; Macromolecular Substances ; Methionine - metabolism ; Mice ; Platelet Membrane Glycoproteins - biosynthesis ; Platelet Membrane Glycoproteins - genetics ; Proteins ; Recombinant Fusion Proteins - biosynthesis ; thrombospondin 1 ; thrombospondin 2 ; Thrombospondins ; Transfection</subject><ispartof>The Journal of biological chemistry, 1992-12, Vol.267 (35), p.24921-24924</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3550-e489adf745111de22c849e86c1941d8db8588d3bf3a68a02e92ee0f16264f6563</citedby><cites>FETCH-LOGICAL-c3550-e489adf745111de22c849e86c1941d8db8588d3bf3a68a02e92ee0f16264f6563</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4510360$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1459996$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>O'ROURKE, K. M</creatorcontrib><creatorcontrib>LAHERTY, C. D</creatorcontrib><creatorcontrib>DIXIT, V. M</creatorcontrib><title>Thrombospondin 1 and thrombospondin 2 are expressed as both homo- and heterotrimers</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>There exist two distinct thrombospondin molecules (designated TSP1 and TSP2) which are encoded by separate genes. TSP1 is
a trimeric cell surface and extracellular matrix molecule. Sequence comparison reveals that the 2 cysteines involved in interchain
disulfide linkage and trimer assembly in TSP1 are conserved in TSP2 (Laherty, C. D., O'Rourke, K., Wolf, F. W., Katz, R.,
Seldin, M. F., and Dixit, V. M. (1992) J. Biol. Chem. 267, 3274-3281). Swiss 3T3 fibroblasts express both TSP1 and TSP2, and,
therefore, an important question is whether TSP in such cells is expressed as homotrimers or as heterotrimers. We find that
Swiss 3T3 cells and epithelial cells transfected with TSP expression vectors express both homo- and heterotrimeric forms of
TSP. In addition, homotrimeric TSP2 has a lower affinity for heparin than homotrimeric TSP1. Thus, the heparin affinity of
TSP can be modulated by the expression of TSP as homo- or heterotrimers.</description><subject>3T3 Cells</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antibody Specificity</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Chromatography, Affinity</subject><subject>Cloning, Molecular</subject><subject>Cysteine - metabolism</subject><subject>Escherichia coli - genetics</subject><subject>expression</subject><subject>extracellular matrix</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Vectors</subject><subject>Glycoproteins</subject><subject>Immunoassay</subject><subject>Lectins - biosynthesis</subject><subject>Lectins - genetics</subject><subject>Macromolecular Substances</subject><subject>Methionine - metabolism</subject><subject>Mice</subject><subject>Platelet Membrane Glycoproteins - biosynthesis</subject><subject>Platelet Membrane Glycoproteins - genetics</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - biosynthesis</subject><subject>thrombospondin 1</subject><subject>thrombospondin 2</subject><subject>Thrombospondins</subject><subject>Transfection</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>eNqFkE1LxDAQhoMoun78BKEHET1UM_lqcpTFLxA8qOAtpM3UVrbNmnRR_711d1E8OZcMmeedkIeQQ6BnQEGdP1DKIDdM6hMwpwU3mud0g0yAjg2X8LxJJj_IDtlN6ZWOJQxsk20Q0hijJuThsYmhK0Oah963fQaZ6302_L1kmYuY4cc8YkroM5eyMgxN1oQu5MtAgwPGMMS2w5j2yVbtZgkP1uceebq6fJze5Hf317fTi7u84lLSHIU2zteFkADgkbFKC4NaVWAEeO1LLbX2vKy5U9pRhoYh0hoUU6JWUvE9crzaO4_hbYFpsF2bKpzNXI9hkWzBuWGG6X9BULxQRrARlCuwiiGliLWdj19y8dMCtd_W7dK6_VZqwdildUvH3OH6gUXZof9NrTSP86P13KXKzero-qpNP9hogHJFf7GmfWne24i2bEPVYGeZKiyXlgnDgH8B3J6VFg</recordid><startdate>19921215</startdate><enddate>19921215</enddate><creator>O'ROURKE, K. 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M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3550-e489adf745111de22c849e86c1941d8db8588d3bf3a68a02e92ee0f16264f6563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>3T3 Cells</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antibody Specificity</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Chromatography, Affinity</topic><topic>Cloning, Molecular</topic><topic>Cysteine - metabolism</topic><topic>Escherichia coli - genetics</topic><topic>expression</topic><topic>extracellular matrix</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Vectors</topic><topic>Glycoproteins</topic><topic>Immunoassay</topic><topic>Lectins - biosynthesis</topic><topic>Lectins - genetics</topic><topic>Macromolecular Substances</topic><topic>Methionine - metabolism</topic><topic>Mice</topic><topic>Platelet Membrane Glycoproteins - biosynthesis</topic><topic>Platelet Membrane Glycoproteins - genetics</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - biosynthesis</topic><topic>thrombospondin 1</topic><topic>thrombospondin 2</topic><topic>Thrombospondins</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>O'ROURKE, K. M</creatorcontrib><creatorcontrib>LAHERTY, C. D</creatorcontrib><creatorcontrib>DIXIT, V. M</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>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>O'ROURKE, K. M</au><au>LAHERTY, C. D</au><au>DIXIT, V. M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thrombospondin 1 and thrombospondin 2 are expressed as both homo- and heterotrimers</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-12-15</date><risdate>1992</risdate><volume>267</volume><issue>35</issue><spage>24921</spage><epage>24924</epage><pages>24921-24924</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>There exist two distinct thrombospondin molecules (designated TSP1 and TSP2) which are encoded by separate genes. TSP1 is
a trimeric cell surface and extracellular matrix molecule. Sequence comparison reveals that the 2 cysteines involved in interchain
disulfide linkage and trimer assembly in TSP1 are conserved in TSP2 (Laherty, C. D., O'Rourke, K., Wolf, F. W., Katz, R.,
Seldin, M. F., and Dixit, V. M. (1992) J. Biol. Chem. 267, 3274-3281). Swiss 3T3 fibroblasts express both TSP1 and TSP2, and,
therefore, an important question is whether TSP in such cells is expressed as homotrimers or as heterotrimers. We find that
Swiss 3T3 cells and epithelial cells transfected with TSP expression vectors express both homo- and heterotrimeric forms of
TSP. In addition, homotrimeric TSP2 has a lower affinity for heparin than homotrimeric TSP1. Thus, the heparin affinity of
TSP can be modulated by the expression of TSP as homo- or heterotrimers.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1459996</pmid><doi>10.1016/S0021-9258(19)73983-0</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 3T3 Cells Analytical, structural and metabolic biochemistry Animals Antibody Specificity Biological and medical sciences Blotting, Western Chromatography, Affinity Cloning, Molecular Cysteine - metabolism Escherichia coli - genetics expression extracellular matrix Fundamental and applied biological sciences. Psychology Genetic Vectors Glycoproteins Immunoassay Lectins - biosynthesis Lectins - genetics Macromolecular Substances Methionine - metabolism Mice Platelet Membrane Glycoproteins - biosynthesis Platelet Membrane Glycoproteins - genetics Proteins Recombinant Fusion Proteins - biosynthesis thrombospondin 1 thrombospondin 2 Thrombospondins Transfection |
| title | Thrombospondin 1 and thrombospondin 2 are expressed as both homo- and heterotrimers |
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