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dc.contributor.authorShaw, Leslie M.
dc.contributor.authorChao, Celia
dc.contributor.authorWewer, Ulla M.
dc.contributor.authorMercurio, Arthur M.
dc.date2022-08-11T08:08:01.000
dc.date.accessioned2022-08-23T15:39:40Z
dc.date.available2022-08-23T15:39:40Z
dc.date.issued1996-03-01
dc.date.submitted2010-11-07
dc.identifier.citationCancer Res. 1996 Mar 1;56(5):959-63.
dc.identifier.issn0008-5472 (Linking)
dc.identifier.pmid8640785
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26225
dc.description.abstractThe involvement of the alpha 6 beta a integrin, a laminin receptor, in breast carcinoma progression needs to be addressed rigorously. We report that a human breast carcinoma cell line, MDA-MB-435, known to be highly invasive and metastatic, expresses three potential integrin laminin receptors: alpha 2 beta 1, alpha 3 beta 1, and alpha 6 beta 1, but uses only alpha 6 beta 1 to mediate adhesion and migration on laminin matrices. To investigate the contribution of alpha 6 beta 1 to the aggressive behavior of these cells, we developed a dominant-negative strategy for knocking out alpha 6 beta 1 function that involved expression of a cytoplasmic domain deletion mutant of the beta 4 integrin subunit by cDNA transfection. Stable transfectants of MDA-MB-435 cells that expressed this mutant beta 4 subunit were inhibited dramatically in their ability to adhere and migrate on laminin matrices, and their capacity to invade Matrigel was reduced significantly. These findings support the hypothesis that alpha 6 beta 1 is important for breast cancer progression. Moreover, this approach is a powerful method that should be useful in assessing the role of alpha 6 beta 1 in other cells.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=8640785&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://cancerres.aacrjournals.org/content/56/5/959.full.pdf+html
dc.subjectBreast Neoplasms
dc.subjectCell Adhesion
dc.subjectCell Movement
dc.subjectDNA, Complementary
dc.subjectFemale
dc.subjectGene Transfer Techniques
dc.subjectHumans
dc.subjectIntegrin alpha6beta1
dc.subjectIntegrins
dc.subjectLaminin
dc.subjectReceptors, Laminin
dc.subjectTumor Cells, Cultured
dc.subjectCancer Biology
dc.subjectNeoplasms
dc.titleFunction of the integrin alpha 6 beta 1 in metastatic breast carcinoma cells assessed by expression of a dominant-negative receptor
dc.typeArticle
dc.source.journaltitleCancer research
dc.source.volume56
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cancerbiology_pp/139
dc.identifier.contextkey1633364
html.description.abstract<p>The involvement of the alpha 6 beta a integrin, a laminin receptor, in breast carcinoma progression needs to be addressed rigorously. We report that a human breast carcinoma cell line, MDA-MB-435, known to be highly invasive and metastatic, expresses three potential integrin laminin receptors: alpha 2 beta 1, alpha 3 beta 1, and alpha 6 beta 1, but uses only alpha 6 beta 1 to mediate adhesion and migration on laminin matrices. To investigate the contribution of alpha 6 beta 1 to the aggressive behavior of these cells, we developed a dominant-negative strategy for knocking out alpha 6 beta 1 function that involved expression of a cytoplasmic domain deletion mutant of the beta 4 integrin subunit by cDNA transfection. Stable transfectants of MDA-MB-435 cells that expressed this mutant beta 4 subunit were inhibited dramatically in their ability to adhere and migrate on laminin matrices, and their capacity to invade Matrigel was reduced significantly. These findings support the hypothesis that alpha 6 beta 1 is important for breast cancer progression. Moreover, this approach is a powerful method that should be useful in assessing the role of alpha 6 beta 1 in other cells.</p>
dc.identifier.submissionpathcancerbiology_pp/139
dc.contributor.departmentDepartment of Cancer Biology
dc.source.pages959-63


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