The high molecular weight receptor to transforming growth factor-beta contains glycosaminoglycan chains
Proteoglycans are constituents of the cell surface that may play important roles in the regulation of cell behavior. Here we report that the 250-kDa receptor subunit that binds the multifunctional protein, transforming growth factor-beta 1 (TGF-beta 1), contains chains of heparan sulfate and chondro...
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| Veröffentlicht in: | The Journal of biological chemistry 1988-06, Vol.263 (17), p.8366-8370 |
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| container_title | The Journal of biological chemistry |
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| creator | Segarini, P R Seyedin, S M |
| description | Proteoglycans are constituents of the cell surface that may play important roles in the regulation of cell behavior. Here we report that the 250-kDa receptor subunit that binds the multifunctional protein, transforming growth factor-beta 1 (TGF-beta 1), contains chains of heparan sulfate and chondroitin sulfate and thus is a proteoglycan. Digestion of TGF-beta 1-receptor complexes with glycosaminoglycan (GAG)-specific degradative enzymes yield core proteins of 115-140 kDa. Cell monolayers that had been predigested with GAG-specific degradative enzymes were capable of binding high levels of TGF-beta 1, but the size of the binding components was shifted from the high molecular weight species to the lower molecular weight core proteins, indicating that GAG chains are not necessary for TGF-beta 1 binding to the cell. The presence of GAG chains on the receptor subunit indicates that it has the potential for interaction with the extracellular matrix. |
| doi_str_mv | 10.1016/S0021-9258(18)68486-8 |
| format | Article |
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The presence of GAG chains on the receptor subunit indicates that it has the potential for interaction with the extracellular matrix.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)68486-8</identifier><identifier>PMID: 2897367</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; Cattle ; Cell receptors ; Cell structures and functions ; Electrophoresis, Polyacrylamide Gel ; Extracellular Matrix - metabolism ; fibroblasts ; Fundamental and applied biological sciences. 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Here we report that the 250-kDa receptor subunit that binds the multifunctional protein, transforming growth factor-beta 1 (TGF-beta 1), contains chains of heparan sulfate and chondroitin sulfate and thus is a proteoglycan. Digestion of TGF-beta 1-receptor complexes with glycosaminoglycan (GAG)-specific degradative enzymes yield core proteins of 115-140 kDa. Cell monolayers that had been predigested with GAG-specific degradative enzymes were capable of binding high levels of TGF-beta 1, but the size of the binding components was shifted from the high molecular weight species to the lower molecular weight core proteins, indicating that GAG chains are not necessary for TGF-beta 1 binding to the cell. The presence of GAG chains on the receptor subunit indicates that it has the potential for interaction with the extracellular matrix.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Extracellular Matrix - metabolism</subject><subject>fibroblasts</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycosaminoglycans - analysis</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>Receptors, Cell Surface - analysis</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Receptors, Transforming Growth Factor beta</subject><subject>transforming growth factor- beta</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>eNqFkUtr3DAUhUVpSKdpf0JA0FLahVvJsvVYhRL6CASyaArdCUm-tlVsayppOuTfR84Ms402uuJ8V1c6B6FLSj5TQvmXX4TUtFJ1Kz9S-YnLRvJKvkAbSiSrWEv_vESbE_IKvU7pLymrUfQcnddSCcbFBg33I-DRDyOewwRuN5mI91DOGUdwsM0h4hxwjmZJfYizXwY8xLDPI-6NK2plIRvswpKNXxIepgcXkilcWEuzYDeuwht01pspwdvjfoF-f_92f_2zur37cXP99bZyjWpzZUmvrJW17a1lfac6KmopwYKhoJQBQVxLG9oqIpQxjFulpGASSsXBtJxdoA-He7cx_NtBynr2ycE0mQXCLmkha1ZTJp4FaaMkYZwVsD2ALoaUIvR6G_1s4oOmRK9J6Kck9GqzplI_JaFl6bs8DtjZGbpT19H6or8_6iY5M_XFYefTCeNKUFKv498dsDWkvY-grQ9uhFnXnGkqyiS-fvvqQEHx9r-HqJPzsDjoSofLugv-mec-Amkgsuo</recordid><startdate>19880615</startdate><enddate>19880615</enddate><creator>Segarini, P R</creator><creator>Seyedin, S M</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19880615</creationdate><title>The high molecular weight receptor to transforming growth factor-beta contains glycosaminoglycan chains</title><author>Segarini, P R ; Seyedin, S M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c495t-b0f9bb82bfbb3fd9d17288ebea1e99ae70c514159079aa36b998738e36b6ea563</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Extracellular Matrix - metabolism</topic><topic>fibroblasts</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycosaminoglycans - analysis</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>Receptors, Cell Surface - analysis</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Receptors, Transforming Growth Factor beta</topic><topic>transforming growth factor- beta</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Segarini, P R</creatorcontrib><creatorcontrib>Seyedin, S M</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>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>Segarini, P R</au><au>Seyedin, S M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The high molecular weight receptor to transforming growth factor-beta contains glycosaminoglycan chains</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-06-15</date><risdate>1988</risdate><volume>263</volume><issue>17</issue><spage>8366</spage><epage>8370</epage><pages>8366-8370</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Proteoglycans are constituents of the cell surface that may play important roles in the regulation of cell behavior. Here we report that the 250-kDa receptor subunit that binds the multifunctional protein, transforming growth factor-beta 1 (TGF-beta 1), contains chains of heparan sulfate and chondroitin sulfate and thus is a proteoglycan. Digestion of TGF-beta 1-receptor complexes with glycosaminoglycan (GAG)-specific degradative enzymes yield core proteins of 115-140 kDa. Cell monolayers that had been predigested with GAG-specific degradative enzymes were capable of binding high levels of TGF-beta 1, but the size of the binding components was shifted from the high molecular weight species to the lower molecular weight core proteins, indicating that GAG chains are not necessary for TGF-beta 1 binding to the cell. 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| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1988-06, Vol.263 (17), p.8366-8370 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Biological and medical sciences Cattle Cell receptors Cell structures and functions Electrophoresis, Polyacrylamide Gel Extracellular Matrix - metabolism fibroblasts Fundamental and applied biological sciences. Psychology Glycosaminoglycans - analysis Molecular and cellular biology Molecular Weight Receptors, Cell Surface - analysis Receptors, Cell Surface - metabolism Receptors, Transforming Growth Factor beta transforming growth factor- beta |
| title | The high molecular weight receptor to transforming growth factor-beta contains glycosaminoglycan chains |
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