Expression of MMP2 and MMP9 (Gelatinases A and B) in Human Colon Cancer Cells

• Published in: Applied biochemistry and biotechnology Vol. 165; no. 5-6; pp. 1245 - 1252
• Main Authors: Damodharan, Umadevi, Ganesan, Ravikumar, Radhakrishnan, Uma C.
• Format: Journal Article
• Language: English
• Published: New York Humana Press Inc 01.11.2011; Springer; Springer Nature B.V
• Subjects: Biochemistry; Biological and medical sciences; Biotechnology; Cell Line, Tumor; Cellular biology; Chemistry; Chemistry and Materials Science; Colonic Neoplasms - enzymology; Colonic Neoplasms - genetics; Colonic Neoplasms - metabolism; Colorectal cancer; Enzymes; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Neoplastic; Humans; Matrix Metalloproteinase 2 - genetics; Matrix Metalloproteinase 2 - metabolism; Matrix Metalloproteinase 9 - genetics; Matrix Metalloproteinase 9 - metabolism; Nitric oxide; Nitric Oxide - metabolism; Emodin; Sodium nitroprusside; Colon cancer; Matrix metalloproteinase; Nitric oxide; Human; Enzyme; Metalloendopeptidases; Gelatinase B; Gelatinase A; Peptidases; Hydrolases; Metalloproteinase; Tumor cell
• ISSN: 0273-2289; 1559-0291
• DOI: 10.1007/s12010-011-9342-8

Matrix metalloproteinases (MMPs) are a family of zinc-dependent neutral endopeptidases, collectively capable of degrading essentially all matrix components. Elevated levels of distinct MMPs are detected in tumor tissue or serum of patients with advanced cancer, and they are the major prognostic indicators in cancer. Inhibition of MMPs has been explored as a therapeutic goal for almost two decades. Nitric oxide (NO), a free radical plays an important role in signaling pathways in regulation of MMP expression. In the present study, we demonstrated the role of exogenous NO levels in the regulation of MMP2 and MMP9 (gelatinases A and B) in colon cancer cell line WiDr and its inhibition with emodin (a naturally occurring anthraquinone).