Induction of matrix metalloproteinase-9 requires a polymerized actin cytoskeleton in human malignant glioma cells

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dc.contributor.authorChintala, S. K.en
dc.contributor.authorSawaya, R.en
dc.contributor.authorAggarwal, B. B.en
dc.contributor.authorMajumder, S.en
dc.contributor.authorGiri, D. K.en
dc.contributor.authorKyritsis, A. P.en
dc.contributor.authorGokaslan, Z. L.en
dc.contributor.authorRao, J. S.en
dc.date.accessioned2015-11-24T19:10:20Z
dc.date.available2015-11-24T19:10:20Z
dc.identifier.issn0021-9258-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/20816
dc.rightsDefault Licence-
dc.subjectActins/*metabolismen
dc.subjectBiopolymersen
dc.subjectBrain Neoplasms/*enzymology/pathology/ultrastructureen
dc.subjectCell Adhesion Molecules/metabolismen
dc.subjectCollagenases/*biosynthesisen
dc.subjectCytochalasin D/pharmacologyen
dc.subjectCytoskeleton/*metabolismen
dc.subjectEnzyme Activationen
dc.subjectEnzyme Inductionen
dc.subjectEnzyme Inhibitors/pharmacologyen
dc.subjectFocal Adhesion Kinase 1en
dc.subjectFocal Adhesion Protein-Tyrosine Kinasesen
dc.subjectGlioma/*enzymology/pathology/ultrastructureen
dc.subjectHumansen
dc.subjectMatrix Metalloproteinase 9en
dc.subjectNF-kappa B/metabolismen
dc.subjectNeoplasm Invasivenessen
dc.subjectProtein Kinase C/antagonists & inhibitorsen
dc.subjectProtein-Tyrosine Kinases/metabolismen
dc.subjectTetradecanoylphorbol Acetate/pharmacologyen
dc.subjectTumor Cells, Cultureden
dc.titleInduction of matrix metalloproteinase-9 requires a polymerized actin cytoskeleton in human malignant glioma cellsen
heal.abstractAlterations in cytoskeleton and subsequent cell shape changes exert specific effects on the expression of various genes. Our previous results suggested that malignant human gliomas express elevated levels of matrix metalloproteinases compared with normal brain tissue and low grade gliomas. To understand the role of cell shape changes on matrix metalloproteinase expression in human glioma cells, we treated SNB19 cells with cytochalasin-D, an inhibitor of actin polymerization, and colchicine-B, a tubulin inhibitor, in the presence of phorbol 12-myristate 13-acetate. Cytochalasin-D treatment of SNB19 cells resulted in the loss of phorbol 12-myristate 13-acetate-induced matrix metalloproteinase-9 (also known as gelatinase-B) expression and coincided with inhibition of actin polymerization, resulting in cell rounding. Moreover, compared with monolayers, cells grown as spheroids or cell aggregates failed to express matrix metalloproteinase-9 in the presence of phorbol 12-myristate 13-acetate. Matrix metalloproteinase-9 expression was also inhibited by calphostin-C, a protein kinase inhibitor, suggesting the involvement of protein kinase C in matrix metalloproteinase-9 expression. Phorbol 12-myristate 13-acetate-induced invasion of SNB19 cells through Matrigel was inhibited by cytochalasin-D and calphostin-C. These results suggest that the actin polymerization transduces signals that modulate the expression of matrix metalloproteinase-9 expression and the subsequent invasion of human glioma cells.en
heal.accesscampus-
heal.fullTextAvailabilityTRUE-
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/9593690-
heal.identifier.secondaryhttp://www.jbc.org/content/273/22/13545.full.pdf-
heal.journalNameJournal of Biological Chemistryen
heal.journalTypepeer-reviewed-
heal.languageen-
heal.publicationDate1998-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.typejournalArticle-
heal.type.elΆρθρο Περιοδικούel
heal.type.enJournal articleen

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