DNAzyme as an efficient tool to modulate invasiveness of human carcinoma cells.
Author(s) -
Magdalena Wiktorska,
Izabela PapiewskaPająk,
And̀rzej Okruszek,
Izabela SacewiczHofman,
Jolanta Niewiarowska
Publication year - 2010
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2010_2405
Subject(s) - integrin , fibronectin , laminin , cancer research , cell adhesion , chemistry , urokinase receptor , receptor , cancer cell , flow cytometry , metastasis , cell culture , microbiology and biotechnology , cell migration , biology , in vitro , cell , cancer , extracellular matrix , biochemistry , genetics
In this study we evaluated efficiency of DNAzymes to modulate motility of cancer cells, an important factor in the progression and metastasis of cancers. For this purpose we targeted β1 integrins that are predominant adhesive receptors in various carcinoma cell lines (CX1.1, HT29, LOVO, LS180, PC-3). To evaluate invasiveness of cancer cells, we used a transwell migration assay that allowed analyzing chemotactic migration of colon carcinoma cell lines across an ECM-coated membrane. Their adhesive properties were also characterized by the analysis of adhesion to fibronectin, laminin and collagen. In addition, the expression of major integrin subunits, selected intact β1 integrins, and other adhesive receptors (ICAM, E-selectin, uPAR) was analyzed by flow cytometry. Inhibition of β1 integrin expression by DNAzyme to β1 mRNA almost abolished the invasiveness of the CX1.1, HT29, LS180, LOVO and PC-3 cells in vitro. These data show that DNAzymes to β1 integrin subunit can be used to inhibit invasiveness of carcinoma cells.
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