Literature DB >> 2159876

Casein kinase II is elevated in solid human tumours and rapidly proliferating non-neoplastic tissue.

U Münstermann1, G Fritz, G Seitz, Y P Lu, H R Schneider, O G Issinger.   

Abstract

Protein kinase CKII (i.e. casein kinase II, CKII, NII) is expressed at a higher level in rapidly proliferating tissues and in solid human tumours (e.g. colorectal carcinomas) when compared to the corresponding non-neoplastic colorectal mucosa. This could be shown by (a) Western blotting of cellular extracts from solid tumours followed by immunostaining with an anti-CKII polyclonal antibody, (b) immunohistochemical staining of cells from tissue sections and (c) by activity measurements using the CKII-specific synthetic peptide (RRRDDDSDDD). The maximum observed activity in the colorectal carcinomas investigated was up to eightfold higher in the tumour specimens than in the non-neoplastic tissue (i.e. colorectal mucosa). The activity range was between 33-350 U/mg protein and in the case of colorectal mucosa 13-106 U/mg protein. The amount of CKII determined in the individual tumours was in the range 0.4-1.6 nmol/g tissue.

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Year:  1990        PMID: 2159876     DOI: 10.1111/j.1432-1033.1990.tb15484.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  61 in total

1.  Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins.

Authors:  M Kusk; R Ahmed; B Thomsen; C Bendixen; O G Issinger; B Boldyreff
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

2.  Protein kinase CK2alpha may induce gene expression but unlikely acts directly as a DNA-binding transcription-activating factor.

Authors:  K Ackermann; W Pyerin
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

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

Authors:  J Roig; A Krehan; D Colomer; W Pyerin; E Itarte; M Plana
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

4.  Protein kinase CK2 interacts with a multi-protein binding domain of p53.

Authors:  C Götz; P Scholtes; A Prowald; N Schuster; W Nastainczyk; M Montenarh
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

5.  Characterization of CK2 holoenzyme variants with regard to crystallization.

Authors:  B Guerra; K Niefind; I Ermakowa; O G Issinger
Journal:  Mol Cell Biochem       Date:  2001-11       Impact factor: 3.396

6.  Transcriptional coordination of the genes encoding catalytic (CK2alpha) and regulatory (CK2beta) subunits of human protein kinase CK2.

Authors:  W Pyerin; K Ackermann
Journal:  Mol Cell Biochem       Date:  2001-11       Impact factor: 3.396

Review 7.  Protein kinase CK2: structure, regulation and role in cellular decisions of life and death.

Authors:  David W Litchfield
Journal:  Biochem J       Date:  2003-01-01       Impact factor: 3.857

8.  Expression, purification and characterisation of a novel mutant of the human protein kinase CK2.

Authors:  Elena Grasselli; Graziano Noviello; Cristina Rando; Claudio Nicolini; Laura Vergani
Journal:  Mol Biol Rep       Date:  2003-06       Impact factor: 2.316

9.  FW2.2 and cell cycle control in developing tomato fruit: a possible example of gene co-option in the evolution of a novel organ.

Authors:  Bin Cong; Steven D Tanksley
Journal:  Plant Mol Biol       Date:  2006-08-29       Impact factor: 4.076

Review 10.  Regulation of cellular proliferation in acute lymphoblastic leukemia by Casein Kinase II (CK2) and Ikaros.

Authors:  Chandrika Gowda; Chunhua Song; Malika Kapadia; Jonathon L Payne; Tommy Hu; Yali Ding; Sinisa Dovat
Journal:  Adv Biol Regul       Date:  2016-09-18
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