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Ovarian Cancer Cell Proliferation and Motility is Induced by Engagement of Integrin alphavß3/ Vitronectin Interaction.
Biol. Chem. 384, 1073-1083 (2003)
During tumor metastasis, a fine-tuned balance between the formation and loosening of adhesive cell contacts has to occur, a process based on the regulated expression of integrins. Human ovarian OV-MZ-6 cancer cells express the integrin αvβ3, which associates with vitronectin (VN) and correlates with ovarian cancer progression. Adhesion and spreading of OV-MZ-6 cells on VN was accompanied by the formation of focal adhesion contacts and the recruitment of activated tyrosine-phosphorylated focal adhesion kinase. Cultivation of OV-MZ-6 cells on VN resulted in a significantly induced cell proliferation. This VN effect could be mimicked by cultivating cells on the immobilized αvβ3-directed peptide cyclo-Arg-Gly-Asp-D-Phe-Val (cRGDfV). VN-dependent OV-MZ-6 cell adhesion and proliferation was significantly enhanced by overexpression of αvβ3, and was accompanied by rapid and transient tyrosinephosphorylation of p44erk 1/p42erk 2 mitogen-activated protein kinase. Moreover, overexpression of αvβ3 and OV-MZ-6 cell attachment to VN increased cell motility up to 5-fold accompanied by prominent changes in cytoskeletal organization and cell morphology. Upon αvβ3/VN interaction, by cDNA expression microarray analysis we identified altered mRNA levels of cmyc, epidermal growth factor receptor (EGF-R), transcription factor Fra-1, prothymosin-α (PTMA), integrin-linked kinase (ILK), and the cell adhesion molecule SQM-1, candidates which are possibly involved in changes of the adhesive, migratory, and proliferative phenotype of human ovarian cancer cells.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Times Cited
Scopus
Cited By
Cited By
Altmetric
2.548
0.000
68
71
Anmerkungen
Besondere Publikation
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
cDNA expression microarray Cell adhesion Differential gene expression Extracellular matrix Focal adhesion RGD peptides
Sprache
deutsch
Veröffentlichungsjahr
2003
HGF-Berichtsjahr
0
ISSN (print) / ISBN
1431-6730
e-ISSN
1437-4315
Zeitschrift
Biological Chemistry
Quellenangaben
Band: 384,
Heft: 7,
Seiten: 1073-1083
Verlag
de Gruyter
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Pathology (PATH)
Erfassungsdatum
2003-10-06