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Histone deacetylase in carcinogenesis and its inhibitors as anti-cancer agents Kim DH; Kim M; Kwon HJJ Biochem Mol Biol 2003[Jan]; 36 (1): 110-9The acetylation state of histone is reversibly regulated by histone acetyltransferase (HAT) and deacetylase (HDAC). An imbalance of this reaction leads to an aberrant behavior of the cells in morphology, cell cycle, differentiation, and carcinogenesis. Recently, these key enzymes in the gene expression were cloned. They revealed a broad use of this modification, not only in histone, but also other proteins that involved transcription, nuclear transport, and cytoskeleton. These results suggest that HAT/HDAC takes charge of multiple-functions in the cell, not just the gene expression. HDAC is especially known to play an important role in carcinogenesis. The enzyme has been considered a target molecule for cancer therapy. The inhibition of HDAC activity by a specific inhibitor induces growth arrest, differentiation, and apoptosis of transformed or several cancer cells. Some of these inhibitors are in a clinical trial at phase I or phase II. The discovery and development of specific HDAC inhibitors are helpful for cancer therapy, and decipher the molecular mode of action for HDAC.|*Cell Transformation, Neoplastic[MESH]|*Histone Deacetylase Inhibitors[MESH]|Acetyltransferases/metabolism[MESH]|Animals[MESH]|Antineoplastic Agents/*pharmacology[MESH]|Enzyme Inhibitors/*pharmacology[MESH]|Eukaryotic Cells[MESH]|Gene Expression Regulation[MESH]|Histone Acetyltransferases[MESH]|Histone Deacetylases/chemistry/*physiology[MESH]|Humans[MESH]|Neoplasms/*drug therapy/*enzymology[MESH]|Neovascularization, Pathologic[MESH]|Promoter Regions, Genetic[MESH]|Saccharomyces cerevisiae Proteins/metabolism[MESH]|Substrate Specificity[MESH] |
