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Computational and Mathematical Methods in Medicine
Volume 2014 (2014), Article ID 245610, 8 pages
http://dx.doi.org/10.1155/2014/245610
Research Article

Dynamics of Posttranslational Modifications of p53

1Institute of Systems Biology, Shanghai University, 99 Shangda Road, Shanghai 200444, China
2College of Fundamental Studies, Shanghai University of Engineering Science, 333 Longteng Road, Shanghai 201620, China
3Guangxi Academy of Sciences, 98 Daling Road, Nanning, Guangxi 530007, China
4DreamSciTech, Apartment 207, Zhencaili 26, Zhujiang Road, Hexi District, Tianjin 300222, China

Received 19 February 2014; Accepted 6 April 2014; Published 12 May 2014

Academic Editor: Lei Chen

Copyright © 2014 Qing-Duan Fan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

The latest experimental evidence indicates that acetylation of p53 at K164 (lysine 164) and K120 may induce directly cell apoptosis under severe DNA damage. However, previous cell apoptosis models only studied the effects of active and/or inactive p53, that is, phosphorylation/dephosphorylation of p53. In the present paper, based partly on Geva-Zatorsky et al. (2006) and Batchelor et al. (2008), we propose a new cell apoptosis network, in which p53 has three statuses, that is, unphosphorylated p53, phosphorylated p53, and acetylated p53. The time delay differential equations (DDEs) are formulated based on our network to investigate the dynamical insights of p53-induced cell apoptosis. In agreement with experiments (Loewer et al. (2010)), our simulations indicate that acetylated p53 accumulates gradually and then induces the proapoptotic protein Bax under enough DNA damage. Moreover, phosphorylated p53 oscillates and initiates cell repair during DNA damage.