Function of Sirtuins in Biological Tissues

Authors

  • Balaji Shoba,

    1. Department of Anatomy, Yong Loo Lin School of Medicine, National University Health System, National University of Singapore, Singapore
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  • Zin Mar Lwin,

    1. Department of Anatomy, Yong Loo Lin School of Medicine, National University Health System, National University of Singapore, Singapore
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  • Lo Soo Ling,

    1. Department of Anatomy, Yong Loo Lin School of Medicine, National University Health System, National University of Singapore, Singapore
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  • Boon-Huat Bay,

    1. Department of Anatomy, Yong Loo Lin School of Medicine, National University Health System, National University of Singapore, Singapore
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  • George W. Yip,

    Corresponding author
    1. Department of Anatomy, Yong Loo Lin School of Medicine, National University Health System, National University of Singapore, Singapore
    • Department of Anatomy, YLL SoM, NUS, 4 Medical Drive, BLK MD10, Singapore 117597
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  • Srinivasan Dinesh Kumar

    Corresponding author
    1. Department of Anatomy, Yong Loo Lin School of Medicine, National University Health System, National University of Singapore, Singapore
    • Department of Anatomy, YLL SoM, NUS, 4 Medical Drive, BLK MD10, Singapore 117597
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Abstract

Sirtuins are protein deacetylases, which are dependent on nicotine adenine dinucleotide. They are phylogenetically conserved from bacteria to humans. Seven sirtuin proteins localized in a wide variety of subcellular locations have been identified in the human genome. The most important known function of sirtuins is their regulation of transcriptional repression, mediated through binding of a complex containing sirtuins and other proteins. Studies have shown that sirtuins have pathophysiological relevance to neurodegeneration, muscle differentiation, inflammation, obesity, and cancer. In addition, sirtuin activity extends the lifespan of several organisms. In this review, we discuss the mode(s) of action of sirtuins, and their biological role(s) in health and disease. Anat Rec, 292:536–543, 2009. © 2009 Wiley-Liss, Inc.

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