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

Content Provider	Springer Nature Link
Author	Roig, Joan Krehan, Andreas Colomer, Dolors Pyerin, Walter Itarte, Emilio Plana, Maria
Copyright Year	1999
Abstract	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, CK2α′ was more resistant to these proteases than CK2α. When these proteases were assayed on the reconstituted (α2β2 holoenzyme, a 37 kDa α-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 CK2α deletion mutants showed that m-calpain and the 20 S proteasome acted on the C-terminus end of CK2α. 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.
Starting Page	229
Ending Page	234
Page Count	6
File Format	PDF
ISSN	03008177
Journal	Molecular and Cellular Biochemistry
Volume Number	191
Issue Number	1-2
e-ISSN	15734919
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1999-01-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Cardiology Medical Biochemistry Oncology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Clinical Biochemistry Molecular Biology

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