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dc.contributor.authorBassols, Anna
dc.contributor.authorMassague, Joan
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:54:43Z
dc.date.available2022-08-23T16:54:43Z
dc.date.issued1988-02-25
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1988 Feb 25;263(6):3039-45.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid3422640
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42565
dc.description.abstractTransforming growth factor beta (TGF-beta) increases up to 20-fold the expression of various forms of chondroitin/dermatan sulfate proteoglycan, the major type of sulfated proteoglycan present in the extracellular matrix and culture medium of various human, rodent, and mink cell types including kidney and lung fibroblasts, lung epithelial cells, preadipocytes, and skeletal muscle myoblasts. TGF-beta regulates the level and molecular size of these proteoglycans by acting simultaneously at two levels: it elevates the biosynthetic rate of the 45-kDa proteoglycan core protein in a cycloheximide- and actinomycin D-sensitive manner, and it induces an increase in the molecular mass of the glycosaminoglycan chains. These cellular responses correlate with occupancy of type III TGF-beta receptors by TGF-beta 1 and TGF-beta 2 and are not induced by other growth factors tested. The parameters of this effect of TGF-beta in kidney fibroblasts and myoblasts are ED50 = 5-10 pM TGF-beta 1 or TGF-beta 2, and t 1/2 = 6-8 h. These results identify the chondroitin/dermatan sulfate proteoglycans as a major component of mammalian mesenchymal and epithelial extracellular matrices whose expression and structure are regulated by TGF-beta.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=3422640&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/263/6/3039.full.pdf+html
dc.subjectBlood Platelets
dc.subjectChondroitin
dc.subjectCycloheximide
dc.subjectDactinomycin
dc.subjectDermatan Sulfate
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectExtracellular Matrix
dc.subjectHumans
dc.subjectPeptides
dc.subjectProteochondroitin Sulfates
dc.subjectProteoglycans
dc.subjectTransforming Growth Factors
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleTransforming growth factor beta regulates the expression and structure of extracellular matrix chondroitin/dermatan sulfate proteoglycans
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume263
dc.source.issue6
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/901
dc.identifier.contextkey579790
html.description.abstract<p>Transforming growth factor beta (TGF-beta) increases up to 20-fold the expression of various forms of chondroitin/dermatan sulfate proteoglycan, the major type of sulfated proteoglycan present in the extracellular matrix and culture medium of various human, rodent, and mink cell types including kidney and lung fibroblasts, lung epithelial cells, preadipocytes, and skeletal muscle myoblasts. TGF-beta regulates the level and molecular size of these proteoglycans by acting simultaneously at two levels: it elevates the biosynthetic rate of the 45-kDa proteoglycan core protein in a cycloheximide- and actinomycin D-sensitive manner, and it induces an increase in the molecular mass of the glycosaminoglycan chains. These cellular responses correlate with occupancy of type III TGF-beta receptors by TGF-beta 1 and TGF-beta 2 and are not induced by other growth factors tested. The parameters of this effect of TGF-beta in kidney fibroblasts and myoblasts are ED50 = 5-10 pM TGF-beta 1 or TGF-beta 2, and t 1/2 = 6-8 h. These results identify the chondroitin/dermatan sulfate proteoglycans as a major component of mammalian mesenchymal and epithelial extracellular matrices whose expression and structure are regulated by TGF-beta.</p>
dc.identifier.submissionpathoapubs/901
dc.contributor.departmentDepartment of Biochemistry
dc.source.pages3039-45


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