The transforming growth factor-beta receptor type III is a membrane proteoglycan. Domain structure of the receptor
The transforming growth factor-beta (TGF-beta) receptor type III is a low abundance cell surface component that binds TGF-beta 1 and TGF-beta 2 with high affinity and specificity, and is present in many mammalian and avian cell types. Type III TGF-beta receptors affinity-labeled with 125I-TGF-beta m...
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| Veröffentlicht in: | The Journal of biological chemistry 1988-11, Vol.263 (32), p.16984-16991 |
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| container_title | The Journal of biological chemistry |
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| creator | Cheifetz, S Andres, J L Massagué, J |
| description | The transforming growth factor-beta (TGF-beta) receptor type III is a low abundance cell surface component that binds TGF-beta 1 and TGF-beta 2 with high affinity and specificity, and is present in many mammalian and avian cell types. Type III TGF-beta receptors affinity-labeled with 125I-TGF-beta migrate in sodium dodecyl sulfate-polyacrylamide electrophoresis gels as diffuse species of 250-350 kDa. Here we show that type III receptors deglycosylated by the action of trifluoromethanesulfonic acid yield affinity-labeled receptor cores of 110-130 kDa. This marked decrease in molecular weight is also achieved by combined treatment of type III receptors with heparitinase and chondroitinase ABC. Digestion of receptor-linked glycosaminoglycans by treatment of intact cell monolayers with heparitinase and chondroitinase does not prevent TGF-beta binding to the type III receptor core polypeptide and does not release the receptor polypeptide from the membrane. The type III TGF-beta receptor binds tightly to DEAE-Sephacel and coelutes with cellular proteoglycans at a characteristically high salt concentration. Thus, the type III TGF-beta receptor has the properties of a membrane proteoglycan that carries heparan and chondroitin sulfate glycosaminoglycan chains. The binding site for TGF-beta appears to reside in the 100-120-kDa core polypeptide of this receptor. The type III receptor is highly sensitive to cleavage by trypsin. Trypsin action releases the glycosaminoglycan-containing domain of the receptor leaving a 60-kDa membrane-associated domain that contains the cross-linked ligand. A model for the domain structure of the TGF-beta receptor type III is proposed based on these results. |
| doi_str_mv | 10.1016/S0021-9258(18)37487-8 |
| format | Article |
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This marked decrease in molecular weight is also achieved by combined treatment of type III receptors with heparitinase and chondroitinase ABC. Digestion of receptor-linked glycosaminoglycans by treatment of intact cell monolayers with heparitinase and chondroitinase does not prevent TGF-beta binding to the type III receptor core polypeptide and does not release the receptor polypeptide from the membrane. The type III TGF-beta receptor binds tightly to DEAE-Sephacel and coelutes with cellular proteoglycans at a characteristically high salt concentration. Thus, the type III TGF-beta receptor has the properties of a membrane proteoglycan that carries heparan and chondroitin sulfate glycosaminoglycan chains. The binding site for TGF-beta appears to reside in the 100-120-kDa core polypeptide of this receptor. The type III receptor is highly sensitive to cleavage by trypsin. 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Domain structure of the receptor</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The transforming growth factor-beta (TGF-beta) receptor type III is a low abundance cell surface component that binds TGF-beta 1 and TGF-beta 2 with high affinity and specificity, and is present in many mammalian and avian cell types. Type III TGF-beta receptors affinity-labeled with 125I-TGF-beta migrate in sodium dodecyl sulfate-polyacrylamide electrophoresis gels as diffuse species of 250-350 kDa. Here we show that type III receptors deglycosylated by the action of trifluoromethanesulfonic acid yield affinity-labeled receptor cores of 110-130 kDa. This marked decrease in molecular weight is also achieved by combined treatment of type III receptors with heparitinase and chondroitinase ABC. Digestion of receptor-linked glycosaminoglycans by treatment of intact cell monolayers with heparitinase and chondroitinase does not prevent TGF-beta binding to the type III receptor core polypeptide and does not release the receptor polypeptide from the membrane. The type III TGF-beta receptor binds tightly to DEAE-Sephacel and coelutes with cellular proteoglycans at a characteristically high salt concentration. Thus, the type III TGF-beta receptor has the properties of a membrane proteoglycan that carries heparan and chondroitin sulfate glycosaminoglycan chains. The binding site for TGF-beta appears to reside in the 100-120-kDa core polypeptide of this receptor. The type III receptor is highly sensitive to cleavage by trypsin. Trypsin action releases the glycosaminoglycan-containing domain of the receptor leaving a 60-kDa membrane-associated domain that contains the cross-linked ligand. A model for the domain structure of the TGF-beta receptor type III is proposed based on these results.</description><subject>Affinity Labels - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Membrane - analysis</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Chondroitin Lyases - metabolism</subject><subject>Chromatography, Ion Exchange</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Molecular and cellular biology</subject><subject>Polysaccharide-Lyases - metabolism</subject><subject>proteoglycans</subject><subject>Rats</subject><subject>Receptors, Cell Surface - analysis</subject><subject>Receptors, Transforming Growth Factor beta</subject><subject>transforming growth factor- beta</subject><subject>Trypsin - metabolism</subject><subject>Tunicamycin - pharmacology</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>eNqFUU2PFCEUJEazjqs_YRMOxuihV2iahj6Zzfo1ySYeXBNvhIbHNKa7GYF2M_9e5sPxuFwIeVX1iiqErii5poS2778TUtOqq7l8S-U7JhopKvkErSiRrGKc_nyKVmfIc_QipV-knKajF-ii7gijXKxQvB8A56jn5EKc_LzBmxge8oCdNjnEqoescQQD2_LCebcFvF6vsU9Y4wmmvjABb2PIEDbjzuj5Gn8Mk_YzTjkuJi8RcHA4ly3_VF6iZ06PCV6d7kv04_On-9uv1d23L-vbm7vKNF2bK-t6YVvGLYCWxulWNC2zTpK-14YLRjpGOGgjdQ-1tNZ1VEjLWgairyVv2SV6c9Qt9n4vkLKafDIwjsVyWJISsukEl82jQMopqaXcK_Ij0MSQUgSnttFPOu4UJWpfijqUovaJKyrVoRQlC-_qtGDpJ7Bn1qmFMn99mutk9OhKqManM0zUtGEN-Q8b_GZ48BFU74MZYFJ1yxSrFW27w3c-HGFQwv3jIapkPMwGbKGYrGzwj_j9C7Qstnc</recordid><startdate>19881115</startdate><enddate>19881115</enddate><creator>Cheifetz, S</creator><creator>Andres, J L</creator><creator>Massagué, J</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>19881115</creationdate><title>The transforming growth factor-beta receptor type III is a membrane proteoglycan. 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Psychology</topic><topic>Glycoside Hydrolases - metabolism</topic><topic>Molecular and cellular biology</topic><topic>Polysaccharide-Lyases - metabolism</topic><topic>proteoglycans</topic><topic>Rats</topic><topic>Receptors, Cell Surface - analysis</topic><topic>Receptors, Transforming Growth Factor beta</topic><topic>transforming growth factor- beta</topic><topic>Trypsin - metabolism</topic><topic>Tunicamycin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cheifetz, S</creatorcontrib><creatorcontrib>Andres, J L</creatorcontrib><creatorcontrib>Massagué, J</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>Cheifetz, S</au><au>Andres, J L</au><au>Massagué, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The transforming growth factor-beta receptor type III is a membrane proteoglycan. Domain structure of the receptor</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1988-11-15</date><risdate>1988</risdate><volume>263</volume><issue>32</issue><spage>16984</spage><epage>16991</epage><pages>16984-16991</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The transforming growth factor-beta (TGF-beta) receptor type III is a low abundance cell surface component that binds TGF-beta 1 and TGF-beta 2 with high affinity and specificity, and is present in many mammalian and avian cell types. Type III TGF-beta receptors affinity-labeled with 125I-TGF-beta migrate in sodium dodecyl sulfate-polyacrylamide electrophoresis gels as diffuse species of 250-350 kDa. Here we show that type III receptors deglycosylated by the action of trifluoromethanesulfonic acid yield affinity-labeled receptor cores of 110-130 kDa. This marked decrease in molecular weight is also achieved by combined treatment of type III receptors with heparitinase and chondroitinase ABC. Digestion of receptor-linked glycosaminoglycans by treatment of intact cell monolayers with heparitinase and chondroitinase does not prevent TGF-beta binding to the type III receptor core polypeptide and does not release the receptor polypeptide from the membrane. The type III TGF-beta receptor binds tightly to DEAE-Sephacel and coelutes with cellular proteoglycans at a characteristically high salt concentration. Thus, the type III TGF-beta receptor has the properties of a membrane proteoglycan that carries heparan and chondroitin sulfate glycosaminoglycan chains. The binding site for TGF-beta appears to reside in the 100-120-kDa core polypeptide of this receptor. The type III receptor is highly sensitive to cleavage by trypsin. 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| subjects | Affinity Labels - metabolism Animals Biological and medical sciences Cell Membrane - analysis Cell receptors Cell structures and functions Chondroitin Lyases - metabolism Chromatography, Ion Exchange Fundamental and applied biological sciences. Psychology Glycoside Hydrolases - metabolism Molecular and cellular biology Polysaccharide-Lyases - metabolism proteoglycans Rats Receptors, Cell Surface - analysis Receptors, Transforming Growth Factor beta transforming growth factor- beta Trypsin - metabolism Tunicamycin - pharmacology |
| title | The transforming growth factor-beta receptor type III is a membrane proteoglycan. Domain structure of the receptor |
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