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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Shen, Shao-Ming Li, Cai-Xia Wang, Li-Shun Yu, Yun |
| Description | Author Affiliation: Li CX ( Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Center of Molecular Medicine, RuiJin Hospital, Shanghai JiaoTong University School of Medicine, Shanghai 200025, P.R. China.); Shen SM ( Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Center of Molecular Medicine, RuiJin Hospital, Shanghai JiaoTong University School of Medicine, Shanghai 200025, P.R. China.); Wang LS ( Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Center of Molecular Medicine, RuiJin Hospital, Shanghai JiaoTong University School of Medicine, Shanghai 200025, P.R. China.); Yu Y ( Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education, Center of Molecular Medicine, RuiJin Hospital, Shanghai JiaoTong University School of Medicine, Shanghai 200025, P.R. China.) |
| Abstract | One member of the highly conserved acidic leucinerich nuclear phosphoprotein 32 kDa (ANP32) family of proteins, ANP32B, is critical for normal development, as demonstrated by a study in ANP32Bdeficient mice. Another study indicated that ANP32B was a direct substrate of caspase3, and was primarily cleaved at the sequence AlaGluValAsp, following Asp163. To investigate the significance of ANP32B cleavage in apoptosis, leukemic U937T cell lines were generated with inducible expression of ANP32B(wild type; WT), the uncleavable mutant ANP32B(D163A) and the Nterminal fragment ANP32B(1163). Notably, overexpression of ANP32B(WT) and ANP32B(D163A) moderately increased and significantly enhanced etoposideinduced apoptosis and caspase3 activation, whereas expression of ANP32B(1163) produced no effect. Two hypotheses have been generated, which may explain the distinct roles of the various ANP32B forms: i) ANP32B(WT) and ANP32B(D163A) localize in the nucleus while ANP32B(1163) mainly resides in the cytosol; or ii) ANP32B(WT) and ANP32B(D163A), but not ANP32B(1163), inhibit the expression of the antiapoptotic protein Bcl2. Based on these observations, caspase3resistant uncleavable ANP32B(D163A) is hypothesized to be proapoptotic in leukemic cells. |
| ISSN | 17912997 |
| e-ISSN | 17913004 |
| Journal | Molecular Medicine Reports |
| Issue Number | 4 |
| Volume Number | 11 |
| Language | English |
| Publisher | Spandidos Publications |
| Publisher Date | 2015-04-01 |
| Publisher Place | Greece |
| Access Restriction | Open |
| Subject Keyword | Apoptosis Caspase 3 Metabolism Leukemia Nuclear Proteins Protein Interaction Domains And Motifs Genetics Cell Line, Tumor Gene Expression Leucine Mutation Chemistry Protein Kinase C-delta Proteolysis Proto-oncogene Proteins C-bcl-2 Research Support, Non-u.s. Gov't Discipline Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Genetics Biochemistry Molecular Biology Cancer Research Molecular Medicine Oncology |
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