Multiple forms of protein kinase CK2 present in leukemic cells: in vitro study of its origin by proteolysis

• Published in: Molecular and cellular biochemistry 1999-01, Vol.191 (1-2), p.229-234
• Main Authors: Roig, J, Krehan, A, Colomer, D, Pyerin, W, Itarte, E, Plana, M
• Format: Article
• Language: English
• Subjects: Acute Disease; Amino Acid Sequence; Animals; Calpain - metabolism; Casein Kinase II; Cysteine Endopeptidases - metabolism; HL-60 Cells; Humans; Hydrolysis; Isoenzymes - metabolism; Kinases; Leukemia, Myeloid - enzymology; Leukemia, Myeloid - pathology; Multienzyme Complexes - metabolism; Proteasome Endopeptidase Complex; Protein-Serine-Threonine Kinases - metabolism; Proteins; Rabbits; Recombinant Proteins - metabolism
• ISSN: 0300-8177; 1573-4919
• DOI: 10.1023/A:1006808816770

Human recombinant CK2 subunits were incubated for different times with the two main cytosolic proteases m-calpain and 20 S proteasome. Both, m-calpain in a calcium dependent manner and the 20 S proteasome, were able to degrade CK2 subunits in vitro. In both cases, CK2alpha' was more resistant to these proteases than CK2alpha. When these proteases were assayed on the reconstituted (alpha2beta2 holoenzyme), a 37 kDa alpha-band, analogous to that observed in AML extracts, was generated which was resistant to further degradation. No degradation was observed when the 26 S proteasome was assayed on free subunits. Studies with CK2alpha deletion mutants showed that m-calpain and the 20 S proteasome acted on the C-terminus end of CK2alpha. These results pointed to cytosolic proteases as agents involved in the control of the amount of free CK2 subunits within the cell, which becomes evident when CK2 is overexpressed as in AML cells.