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Abstract 1221: Apoptosis is regulated by MCPH1 via p38 MAPK

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Abstract Microcephalin (MCPH1) is a member of the BRCA1 COOH terminal (BRCT) domain family of protein that involved in the cellular response to DNA damage. MCPH1 gene are associated with primary microcephaly (OMIM 251200), premature chromosome condensation, homologous DNA repair, chromosomal integrity, cell cycle arrest, telomerase activity and apoptosis. Recently reports, And MCPH1 is regulated the p53 phosphorylation in apoptosis, and enhanced E2F1-dependent apoptosis and the role of MCPH1 in p73 induction during DNA damage. And E2F1 activation leads to a transient increase in phosphorylation of the MAPK p38 and also leads to phosphorylation of p53 in apoptosis. But it is not unclear mechanisms that MCPH1/ E2F1 binging induced phosphorylation of p38 MAPK. We have used western blotting and immunopresipitation for detecting protein expression and also real-time PCR for RNA expression. Cell lines were used MCF7, MDA-MB231, MCF10A and U2OS. We use the anti-cancer drugs, as cisplatin and doxorubicin for induced the apoptosis. Anti-cancer drugs are induced the MCPH1 protein expression for 2h∼6h, but reduced for 24h. We show the binging between E2F1and MCPH1and p38 MAPK expressions. And MCPH1 regulates p38 expression in apoptosis. Note: This abstract was not presented at the AACR 101st Annual Meeting 2010 because the presenter was unable to attend. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 1221.
Title: Abstract 1221: Apoptosis is regulated by MCPH1 via p38 MAPK
Description:
Abstract Microcephalin (MCPH1) is a member of the BRCA1 COOH terminal (BRCT) domain family of protein that involved in the cellular response to DNA damage.
MCPH1 gene are associated with primary microcephaly (OMIM 251200), premature chromosome condensation, homologous DNA repair, chromosomal integrity, cell cycle arrest, telomerase activity and apoptosis.
Recently reports, And MCPH1 is regulated the p53 phosphorylation in apoptosis, and enhanced E2F1-dependent apoptosis and the role of MCPH1 in p73 induction during DNA damage.
And E2F1 activation leads to a transient increase in phosphorylation of the MAPK p38 and also leads to phosphorylation of p53 in apoptosis.
But it is not unclear mechanisms that MCPH1/ E2F1 binging induced phosphorylation of p38 MAPK.
We have used western blotting and immunopresipitation for detecting protein expression and also real-time PCR for RNA expression.
Cell lines were used MCF7, MDA-MB231, MCF10A and U2OS.
We use the anti-cancer drugs, as cisplatin and doxorubicin for induced the apoptosis.
Anti-cancer drugs are induced the MCPH1 protein expression for 2h∼6h, but reduced for 24h.
We show the binging between E2F1and MCPH1and p38 MAPK expressions.
And MCPH1 regulates p38 expression in apoptosis.
Note: This abstract was not presented at the AACR 101st Annual Meeting 2010 because the presenter was unable to attend.
Citation Format: {Authors}.
{Abstract title} [abstract].
In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC.
Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 1221.

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