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MAGE-A Tumor Antigens Target p53 Transactivation Function through Histone Deacetylase Recruitment and Confer Resistance to Chemotherapeutic Agents
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MAGE-A Tumor Antigens Target p53 Transactivation Function through Histone Deacetylase Recruitment and Confer Resistance to Chemotherapeutic Agents
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Journal Article
MAGE-A Tumor Antigens Target p53 Transactivation Function through Histone Deacetylase Recruitment and Confer Resistance to Chemotherapeutic Agents
2006
Overview
The MAGE gene family is characterized by a conserved domain (MAGE Homology Domain). A subset of highly homologous MAGE genes (group A; MAGE-A) belong to the chromosome X-clustered cancer/testis antigens. MAGE-A genes are normally expressed in the human germ line and overexpressed in various tumor types; however, their biological function is largely unknown. Here we present evidence indicating that MageA2 protein, belonging to the MAGE-A subfamily, confers wild-type-p53-sensitive resistance to etoposide (ET) by inducing a novel p53 inhibitory loop involving recruitment of histone deacetylase 3 (HDAC3) to MageA2/p53 complex, thus strongly down-regulating p53 transactivation function. In fact, enhanced MageA2 protein levels, in addition to ET resistance, correlate with impaired acetylation of both p53 and histones surrounding p53-binding sites. Association between MAGE-A expression levels and resistance to ET treatment is clearly shown in short-term cell lines obtained from melanoma biopsies harboring wild-type-p53, whereas cells naturally, or siRNAmediated expressing low MAGE-A levels, correlate with enhanced p53-dependent sensitivity to ET. In addition, combined trichostatin A/ET treatment in melanoma cells expressing high MAGE-A levels reestablishes p53 response and reverts the chemoresistance.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Antigens
/ Antigens, Neoplasm - physiology
/ Antineoplastic Agents - pharmacology
/ Gene Expression Regulation, Neoplastic
/ Histone Deacetylases - chemistry
/ Histone Deacetylases - metabolism
/ Histones
/ Humans
/ Hydroxamic Acids - pharmacology
/ Melanoma
/ Melanoma-Specific Antigens - biosynthesis
/ Melanoma-Specific Antigens - metabolism
/ Neoplasm Proteins - biosynthesis
/ Neoplasm Proteins - metabolism
/ Proteins
/ Tumor Suppressor Protein p53 - metabolism
/ Tumors
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