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Human Protein Kinase CK2 Phosphorylates Matrix Metalloproteinase 2 and Inhibits its Activity
Author(s) -
Filipiak Kamila,
Kubiński Konrad,
Hellman Ulf,
Ramos Ana,
de PascualTeresa Beatriz
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402036
Subject(s) - matrix metalloproteinase , phosphorylation , protein kinase a , kinase , crosstalk , chemistry , matrix metalloproteinase inhibitor , microbiology and biotechnology , in vitro , biochemistry , cancer research , biology , physics , optics
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.