Down-regulation of CK2 activity results in a decrease in the level of cdc25C phosphatase in different prostate cancer cell lines

被引：15

作者：

Schneider, Carolin C. ^{[1
]}

Goetz, Claudia ^{[1
]}

Hessenauer, Andrea ^{[1
]}

Guenther, Juergen ^{[1
]}

Kartarius, Sabine ^{[1
]}

Montenarh, Mathias ^{[1
]}

机构：

[1] Univ Saarland, D-66421 Homburg, Germany

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 2011年 / 356卷 / 1-2期

关键词：

Cell cycle; Apoptosis; Protein phosphatase; Protein kinase CK2; Phosphorylation; PROTEIN-KINASE CK2; PHOSPHORYLATION SITE; BETA-SUBUNIT; IN-VITRO; LOCALIZATION; INHIBITION; P34(CDC2); CYCLE; APOPTOSIS; HOMOLOG;

D O I：

10.1007/s11010-011-0946-7

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Protein kinase CK2 is implicated in the regulation of the cell cycle. In addition to a variety of functions, CK2 has anti-apoptotic properties. So far the role of CK2 linking both pathways in the cell is not clear. Some years ago we found that CK2 phosphorylates cdc25C, one member of the cdc25 family of proteins. In this study, we showed that inhibition of CK2 activity by three different inhibitors led to a down-regulation of the level of cdc25C. Inhibition of CK2 activity by transfecting the dominant-negative CK2 alpha subunit also resulted in a down-regulation of the level of cdc25C whereas inhibition of CK2 alpha' had no effect on the cdc25C level. In both cases, we observed apoptosis by PARP cleavage as well as by an increase in gamma H2AX phosphorylation. These results show that down-regulation of the level of cdc25C is not a prerequisite for the induction of apoptosis.

引用

页码：177 / 184

页数：8

共 24 条

[1] Down-regulation of CK2 activity results in a decrease in the level of cdc25C phosphatase in different prostate cancer cell lines
Carolin C. Schneider
Claudia Götz
Andrea Hessenauer
Jürgen Günther
Sabine Kartarius
Mathias Montenarh
Molecular and Cellular Biochemistry, 2011, 356 : 177 - 184
[2] Increased CDC25C phosphatase activity in prostate cancer: Correlation to biochemical recurrence
Ozen, M
Ittmann, M
DeBakey, ME
JOURNAL OF MOLECULAR DIAGNOSTICS, 2004, 6 (04): : 431 - 431
[3] Increased expression and activity of CDC25C phosphatase and an alternatively spliced variant in prostate cancer
Ozen, M
Ittmann, M
CLINICAL CANCER RESEARCH, 2005, 11 (13) : 4701 - 4706
[4] Mutation of a CK2 phosphorylation site in cdc25C impairs importin α/β binding and results in cytoplasmic retention
Schwindling, SL
Noll, A
Montenarh, M
Gotz, C
ONCOGENE, 2004, 23 (23) : 4155 - 4165
[5] Mutation of a CK2 phosphorylation site in cdc25C impairs importin α/β binding and results in cytoplasmic retention
Sandra L Schwindling
Andreas Noll
Mathias Montenarh
Claudia Götz
Oncogene, 2004, 23 : 4155 - 4165
[6] Genotoxic stress modulates CDC25C phosphatase alternative splicing in human breast cancer cell lines
Albert, Helene
Battaglia, Eric
Monteiro, Carolino
Bagrel, Denyse
MOLECULAR ONCOLOGY, 2012, 6 (05): : 542 - 552
[7] Allyl isothiocyanate induces G2/M arrest in human colorectal adenocarcinoma SW620 cells through down-regulation of Cdc25B and Cdc25C
Lau, Wing-Sze
Chen, Tianfeng
Wong, Yum-Shing
MOLECULAR MEDICINE REPORTS, 2010, 3 (06) : 1023 - 1030
[8] Hsp90 inhibitors cause G2/M arrest associated with the reduction of Cdc25C and Cdc2 in lung cancer cell lines
Senju, M
Sueoka, N
Sato, A
Iwanaga, K
Sakao, Y
Tomimitsu, S
Tominaga, M
Irie, K
Hayashi, S
Sueoka, E
JOURNAL OF CANCER RESEARCH AND CLINICAL ONCOLOGY, 2006, 132 (03) : 150 - 158
[9] Hsp90 inhibitors cause G2/M arrest associated with the reduction of Cdc25C and Cdc2 in lung cancer cell lines
Megumi Senju
Naoko Sueoka
Akemi Sato
Kentaro Iwanaga
Yukinori Sakao
Shinji Tomimitsu
Masaki Tominaga
Koji Irie
Shinichiro Hayashi
Eisaburo Sueoka
Journal of Cancer Research and Clinical Oncology, 2006, 132 : 150 - 158
[10] Down-regulation of protein kinase C activity by sorbitol rapidly induces apoptosis in human gastric cancer cell lines
Izawa, M
Teramachi, K
APOPTOSIS, 2001, 6 (05) : 353 - 358

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