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Human Protein Kinase CK2 Phosphorylates Matrix Metalloproteinase 2 and Inhibits its Activity
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Medicinska och farmaceutiska vetenskapsområdet, centrumbildningar mm, Ludwig Institute for Cancer Research.
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2014 (English)In: ChemBioChem (Print), ISSN 1439-4227, E-ISSN 1439-7633, Vol. 15, no 13, 1873-1876 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2014. Vol. 15, no 13, 1873-1876 p.
Keyword [en]
cancer, metalloproteins, MMP-2, phosphorylation, protein kinase CK2
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:uu:diva-234156DOI: 10.1002/cbic.201402036ISI: 000341586100003OAI: oai:DiVA.org:uu-234156DiVA: diva2:755868
Available from: 2014-10-15 Created: 2014-10-14 Last updated: 2014-10-15Bibliographically approved

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Ramos, Anade Pascual-Teresa, Beatriz
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Ludwig Institute for Cancer Research
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