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Histone deacetylase inhibitors target diabetes via chromatin remodeling or as chemical chaperones?

Lawless, M. W., O'Byrne, Kenneth J., & Gray, Stephen G. (2009) Histone deacetylase inhibitors target diabetes via chromatin remodeling or as chemical chaperones? Current Diabetes Reviews, 5(3), pp. 201-209.

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Abstract

Globally, obesity and diabetes (particularly type 2 diabetes) represents a major challenge to world health. Despite decades of intense research efforts, the genetic basis involved in diabetes pathogenesis & conditions associated with obesity are still poorly understood. Recent advances have led to exciting new developments implicating epigenetics as an important mechanism underpinning diabetes and obesity related disease. One epigenetic mechanism known as the "histone code" describes the idea that specific patterns of post-translational modifications to histones act like a molecular "code" recognised and used by non-histone proteins to regulate specific chromatin functions. One modification which has received significant attention is that of histone acetylation. The enzymes which regulate this modification are described as lysine acetyltransferases or KATs and histone deacetylases or HDACs. Due to their conserved catalytic domain HDACs have been actively targeted as a therapeutic target. Some of the known inhibitors of HDACs (HDACi) have also been shown to act as "chemical chaperones" to alleviate diabetic symptoms. In this review, we discuss the available evidence concerning the roles of HDACs in regulating chaperone function and how this may have implications in the management of diabetes. © 2009 Bentham Science Publishers Ltd.

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ID Code: 65180
Item Type: Journal Article
Additional URLs:
Keywords: 4 phenylbutyric acid, amino acid acetyltransferase, butyric acid, chaperone, glucose regulated protein 78, glucose regulated protein 94, heat shock protein 70, heat shock protein 90, histone deacetylase, histone deacetylase inhibitor, insulin, leptin, lysine acetyltransferase, resveratrol, romidepsin, sirtuin 1, theophylline, trichostatin A, unclassified drug, valproic acid, 4-phenylbutyric acid, acyltransferase, antidiabetic agent, arylbutyric acid derivative, enzyme inhibitor, kinamycin acetyltransferase I, anemia, cataract, chromatin assembly and disassembly, clinical trial, cystic fibrosis, diabetes mellitus, diabetic nephropathy, drug dose escalation, ECG abnormality, emphysema, endoplasmic reticulum, endoplasmic reticulum stress, enzyme activity, fatigue, gene expression regulation, gene mutation, gene targeting, glaucoma, heart arrhythmia, heart atrium fibrillation, human, hypoglycemia, kidney cancer, nausea, nonhuman, priority journal, protein binding, protein cross linking, protein expression, protein folding, protein function, protein localization, respiratory distress, retinitis, review, side effect, solid tumor, sudden death, T cell lymphoma, tachycardia, thrombocytopenia, vomiting, drug antagonism, drug delivery system, enzymology, metabolism, non insulin dependent diabetes mellitus, obesity, Acetyltransferases, Diabetes Mellitus, Type 2, Drug Delivery Systems, Enzyme Inhibitors, Gene Expression Regulation, Enzymologic, Histone Deacetylases, Humans, Hypoglycemic Agents, Molecular Chaperones, Phenylbutyrates
DOI: 10.2174/157339909788920956
ISSN: 1573-3998
Divisions: Current > Schools > School of Biomedical Sciences
Current > QUT Faculties and Divisions > Faculty of Health
Current > Institutes > Institute of Health and Biomedical Innovation
Copyright Owner: Copyright 2009 Bentham Science Publishers Ltd.
Deposited On: 06 Dec 2013 13:20
Last Modified: 12 Mar 2014 15:40

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