Lysine acetylation in obesity, diabetes and metabolic disease

Iyer, Abishek, Fairlie, David P. and Brown, Lindsay (2012) Lysine acetylation in obesity, diabetes and metabolic disease. Immunology and Cell Biology, 90 1: 39-46. doi:10.1038/icb.2011.99

Author Iyer, Abishek
Fairlie, David P.
Brown, Lindsay
Title Lysine acetylation in obesity, diabetes and metabolic disease
Journal name Immunology and Cell Biology   Check publisher's open access policy
ISSN 0818-9641
Publication date 2012-01
Year available 2011
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1038/icb.2011.99
Volume 90
Issue 1
Start page 39
End page 46
Total pages 8
Editor David P. Fairlie
Matthew J. Sweet
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Collection year 2012
Language eng
Abstract Histone acetyltransferases (HATs) and histone deacetylases (HDACs) mediate acetylation and deacetylation of histone proteins and transcription factors. There is abundant evidence that these enzymes regulate the acetylation state of many cytoplasmic proteins, including lysine residues in important metabolic enzymes. Lysine acetylation regulates major cellular functions as a common post-transcriptional modification of proteins, conserved from prokaryotes to humans. In this article, we refer to HATs and HDACs broadly as lysine acetyltransferases (KATs) and deacetylases (KDACs). Lysine acetylation is vitally important in both immunological and metabolic pathways and may regulate the balance between energy storage and expenditure. Obesity, type II diabetes and cardiovascular disease (metabolic syndrome) are widely recognised as features of a chronic low-grade inflammatory state, involving significant alterations in primary immunometabolism. Identifying effective therapeutic and preventive options to treat this multi-factorial syndrome has proven to be very challenging, with an emerging focus on developing anti-inflammatory agents that can combat adiposity and metabolic disease. Here, we summarise current evidence and understanding of innate immune and metabolic pathways relevant to adiposity and metabolic disease regulated by lysine acetylation. Developing this understanding in greater detail may facilitate strategic development of novel and enzyme-specific lysine deacetylase modulators that regulate both metabolic and immune systems.
Keyword HDAC inhibitor
Metabolic syndrome
Q-Index Code CX
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Published online 15 November 2011. Published under section SPECIAL FEATURE: Histone Deacetylases and their Inhibitors in Immunology.

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Sub-type: Critical review of research, literature review, critical commentary
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