Retracted: Effects of Chlorotoxin on Matrix Metalloproteinase-2 (MMP-2) in Melanoma and Breast Cancer Cell Lines
Sowale O. Ayomide
Department of Biological Sciences, Faculty of Natural Sciences, Ajayi Crowther University, Oyo State, Nigeria
Gregory E. Oko
Department of Biochemistry, College of Medical Sciences, University of Calabar, P.M.B. 1115 Calabar, Nigeria
Collins C. Chukwu
Department of Biosciences and Chemistry, Sheffield Hallam University, Sheffield, S1 1WB, UK
Khuyen T. K. Vo *
Department of Biosciences and Chemistry, Sheffield Hallam University, Sheffield, S1 1WB, UK
Emmanuel P. Okoi
Department of Genetics and Biotechnology, Faculty of Biological Sciences, University of Calabar, P.M.B. 1115 Calabar, Nigeria
*Author to whom correspondence should be addressed.
Abstract
Matrix metalloproteinases-2 belongs to gelatinase group of MMP family which are endopeptidases involved in the degradation of extracellular matrix proteins such as collagen, elastin, fibronectin or proteoglycans. MMPs play crucial functions in physiological processes such as embryogenesis, wound healing, and pathogenesis of many diseases such as cancer inflammatory, liver and neurological diseases. Scorpion venom peptides are promising drug candidates for cancer treatment, especially chlorotoxin commonly extracted from Israeli Leiurus quinquestriatus scorpion giant. Chlorotoxin specifically binds to the surface of glioma cells through its principal Cltx receptor – MMP-2 and impairs their ability to invade. This study investigated the expression of MMP-2 in breast cancer cell lines (MDA-MB-436) and melanoma cancer cell lines (A375). Although both of cell lines (A375 and MDA-MB-463) were cultured in DMEM and RPMI media containing fetal calf serum and penicillin/streptomycin, A375 cells grew faster than MDA-MB-436 cells because A375 cells covered 80% of the area of the T-75 culture flash within only 2 culture days compared to 3 days of MDA-MB-436 cells. Enzyme collagenase was used in gel electrophoresis with pre-made zymogram gel. The catalytic cleavage of the collagen in gel zymography indicated pro-MMP-2 at 72 kDa and activated MMP-2 at 68 kDa. In addition, there was no active response of MMP-2 in the presence of chlorotoxin recorded on pre-made zymogram gel, which highlights inhibitory action of chlorotoxin on MMP-2.
This paper has been retracted.