Molecular Cancer
| Autor: | Jack E. Dixon, Frederick A. Derheimer, Liwu Li, Michelle T. Paulsen, Mats Ljungman, Sheela Hanasoge, Adrienne M Starks |
|---|---|
| Přispěvatelé: | Biological Sciences |
| Rok vydání: | 2006 |
| Předmět: |
p53
Cancer Research Cyclin B medicine.disease_cause Models 2.1 Biological and endogenous factors Aetiology Phosphorylation Cancer Tumor biology Histone deacetylase inhibitor lcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogens Gene Expression Regulation Neoplastic Oncology 5.1 Pharmaceuticals Azacitidine Molecular Medicine Development of treatments and therapeutic interventions Proteasome Inhibitors CDC2 Protein Kinase Protein Binding medicine.drug_class Cytidine Triphosphate Oncology and Carcinogenesis Mitosis lcsh:RC254-282 Models Biological Cell Line Cell Line Tumor medicine Humans Centrosome duplication Oncology & Carcinogenesis Cyclin-dependent kinase 1 Neoplastic Research Biological Genes p53 Phosphoric Monoester Hydrolases Gene Expression Regulation Genes Cancer cell Cancer research biology.protein Protein Tyrosine Phosphatases Carcinogenesis |
| Zdroj: | Molecular Cancer Molecular Cancer, Vol 5, Iss 1, p 25 (2006) Molecular cancer, vol 5, iss 1 |
| ISSN: | 1476-4598 |
| Popis: | Background The evolutionary conserved cyclin-dependent kinase phosphatase hCdc14A has been shown to play potential roles in the regulation of mitotic exit and in the centrosome duplication cycle. We have recently shown that hCdc14A also can interact with the tumor suppressor p53 both in vitro and in vivo and specifically dephosphorylates the ser315 site of p53 in vitro. In this study we developed antibodies against hCdc14A to investigate the expression and regulation of hCdc14A in human tissues and cancer cells. Results We show that hCdc14A is differentially expressed in human tissues and in 75 cancer cell lines examined. Treatments with the histone deacetylase inhibitor TSA, the demethylating agent 5-aza-2'-deoxycytodine or the proteasome inhibitor MG132 significantly induced expression of hCdc14A in cell lines expressing low or undetectable levels of hCdc14A. There was a strong bias for low expression of hCdc14A in cancer cell lines harboring wild-type p53, suggesting that high Cdc14A expression is not compatible with wild-type p53 expression. We present evidence for a role for hCdc14A in the dephosphorylation of the ser315 site of p53 in vivo and that hCdc14A forms a complex with Cdk1/cyclin B during interphase but not during mitosis. Conclusion Our results that hCdc14A is differentially expressed in human cancer cells and that hCdc14A can interact with both p53 and the Cdk1/cyclin B complex may implicate that dysregulation of hCdc14A expression may play a role in carcinogenesis. |
| Databáze: | OpenAIRE |
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