Human Protein Kinase CK2 Phosphorylates Matrix Metalloproteinase 2 and Inhibits its Activity. Issue 13 (8th July 2014)

• Record Type: Journal Article
• Authors: Filipiak, Kamila; Kubiński, Konrad; Hellman, Ulf; Ramos, Ana; de Pascual‐Teresa, Beatriz
• Is Part Of: Chembiochem. Volume 15:Issue 13(2014)
• Page Start: 1873
• Page End: 1876
• Publication Date: 2014-07-08
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201402036
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Matrix metalloproteinase 2 (MMP‐2) is involved in cancer development and is overexpressed in a variety of malignant tumors. MMP‐2 activity is controlled mainly by transcription, proteolytic activation, and inhibition by endogenous inhibitors. It had previously been demonstrated that MMP‐2 activity is also regulated by phosphorylation at several sites by protein kinase C. Here we demonstrate, by means of bioinformatics and biochemical and cellular assays, that protein kinase CK2 also acts as a modulator of MMP‐2 activity. CK2 down‐regulates MMP‐2 in vitro, and inhibition of CK2 in human fibrosarcoma cells results in up‐regulation of MMP‐2. The discovery of the crosstalk between MMP‐2 and CK2 opens the possibility of new combined anticancer therapies.</p> </abstract>