Description

The p53 protein is critical to regulation of normal cell growth and proliferation and is a suppressor of tumor cell proliferation. Inactivation of p53 by a number of mechanisms, such as missense mutations or interaction with oncogenic viral or cellular proteins, can result in tumor progression. Mutations and/or allelic loss of the p53 gene are associated with a wide variety of human tumors. Known to have a role in transcriptional regulation, p53 suppresses various promoters containing TATA elements in an apparently sequence-independent fashion. p53 also binds to DNA in a sequence-specific manner via recognition of a 20-bp consensus-binding site. This interaction stimulates the expression of genes downstream of the p53 binding site. A number of genes that contain p53-binding sites have been identified, including MDM2, GADD45, and muscle creatine kinase. Post-translational acetylation of p53 enhances its DNA-binding activity. There are multiple factors that affect p53 acetylation, thereby modulating cellular proliferation and apoptosis. The L82-51 monoclonal antibody recognizes acetylated lysine 382 (acK382) in the C-terminal region of p53. Analysis of p53 (acK382) in lymphocytes. Human peripheral blood mononuclear cells (PBMC) were either treated with 0.4 μM Trichostatin A (Sigma, Cat. No. T8552) plus 0.4 μM Adriamycin (Doxorubicin hydrochloride