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dc.contributor.authorIgnotz, Ronald A.
dc.contributor.authorHeino, Jyrki
dc.contributor.authorMassague, Joan
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:54:38Z
dc.date.available2022-08-23T16:54:38Z
dc.date.issued1989-01-05
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1989 Jan 5;264(1):389-92.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid2462560
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42546
dc.description.abstractWe have examined the ability of transforming growth factor-beta 1 (TGF-beta 1) to regulate the expression of members of the alpha beta 2 and alpha beta 3 families of integrins. TGF-beta 1 elevates the expression of vitronectin receptors (alpha v beta 3 integrin) in all cells examined including WI-38 human lung fibroblasts, 3T3-L1 mouse fibroblasts, and MG-63 human osteogenic sarcoma cells. TGF-beta 1 action increases the level of mRNA and the synthesis of vitronectin receptor subunits with t1/2 o 3-4 h and 6 h, respectively. TGF-beta 1 up-regulates expression of the intercellular adhesion receptor, LFA-1 (alpha L beta 2), in THP-1 human monocytic leukemia cells by increasing the synthesis of alpha L subunit but not beta 2 subunit. The increase in alpha L synthesis and assembly into LFA-1 complexes induced by TGF-beta 1 occurs in parallel with elevated fibronectin receptor synthesis in THP-1 cells. These responses to TGF-beta 1 are lost upon phorbol ester-induced differentiation of THP-1 cells into the macrophage phenotype. The results suggest a role of TGF-beta in the regulation of cell-matrix interactions mediated by vitronectin receptors and cell-cell interactions mediated by LFA-1 in the immune system.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=2462560&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/264/1/389.full.pdf+html
dc.subjectAnimals
dc.subjectAntigens, Differentiation
dc.subjectAntigens, Surface
dc.subject*Cell Adhesion
dc.subjectCell Adhesion Molecules
dc.subjectCell Line
dc.subjectHumans
dc.subjectLymphocyte Function-Associated Antigen-1
dc.subjectMacromolecular Substances
dc.subjectMembrane Glycoproteins
dc.subjectMice
dc.subjectRNA, Messenger
dc.subjectReceptors, Immunologic
dc.subjectReceptors, Vitronectin
dc.subjectTransforming Growth Factors
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleRegulation of cell adhesion receptors by transforming growth factor-beta. Regulation of vitronectin receptor and LFA-1
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume264
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/885
dc.identifier.contextkey579774
html.description.abstract<p>We have examined the ability of transforming growth factor-beta 1 (TGF-beta 1) to regulate the expression of members of the alpha beta 2 and alpha beta 3 families of integrins. TGF-beta 1 elevates the expression of vitronectin receptors (alpha v beta 3 integrin) in all cells examined including WI-38 human lung fibroblasts, 3T3-L1 mouse fibroblasts, and MG-63 human osteogenic sarcoma cells. TGF-beta 1 action increases the level of mRNA and the synthesis of vitronectin receptor subunits with t1/2 o 3-4 h and 6 h, respectively. TGF-beta 1 up-regulates expression of the intercellular adhesion receptor, LFA-1 (alpha L beta 2), in THP-1 human monocytic leukemia cells by increasing the synthesis of alpha L subunit but not beta 2 subunit. The increase in alpha L synthesis and assembly into LFA-1 complexes induced by TGF-beta 1 occurs in parallel with elevated fibronectin receptor synthesis in THP-1 cells. These responses to TGF-beta 1 are lost upon phorbol ester-induced differentiation of THP-1 cells into the macrophage phenotype. The results suggest a role of TGF-beta in the regulation of cell-matrix interactions mediated by vitronectin receptors and cell-cell interactions mediated by LFA-1 in the immune system.</p>
dc.identifier.submissionpathoapubs/885
dc.contributor.departmentDepartment of Surgery
dc.contributor.departmentDepartment of Biochemistry
dc.source.pages389-92


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