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

Joan Roig; Andreas Krehan; Dolors Colomer; Walter Pyerin; Emilio Itarte; Maria Plana

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

Joan Roig, Andreas Krehan, Dolors Colomer, Walter Pyerin, Emilio Itarte, Maria Plana

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

11 Citations (Scopus)

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 CK 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, analogues 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.

Original language	English
Pages (from-to)	229-234
Journal	Molecular and Cellular Biochemistry
Volume	191
Issue number	1-2
Publication status	Published - 2 Mar 1999

Keywords

Calcium activated protease
Leukemia
m-calpain
Proteasome
Protein kinase CK2

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title = "Multiple forms of protein kinase CK2 present in leukemic cells: In vitro study of its origin by proteolysis",

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 CK 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, analogues 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.",

keywords = "Calcium activated protease, Leukemia, m-calpain, Proteasome, Protein kinase CK2",

author = "Joan Roig and Andreas Krehan and Dolors Colomer and Walter Pyerin and Emilio Itarte and Maria Plana",

year = "1999",

month = mar,

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language = "English",

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journal = "Molecular and Cellular Biochemistry",

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T1 - Multiple forms of protein kinase CK2 present in leukemic cells: In vitro study of its origin by proteolysis

AU - Roig, Joan

AU - Krehan, Andreas

AU - Colomer, Dolors

AU - Pyerin, Walter

AU - Itarte, Emilio

AU - Plana, Maria

PY - 1999/3/2

Y1 - 1999/3/2

N2 - 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 CK 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, analogues 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.

AB - 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 CK 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, analogues 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.

KW - Calcium activated protease

KW - Leukemia

KW - m-calpain

KW - Proteasome

KW - Protein kinase CK2

M3 - Article

VL - 191

SP - 229

EP - 234

JO - Molecular and Cellular Biochemistry

JF - Molecular and Cellular Biochemistry

SN - 0300-8177

IS - 1-2

ER -