Research Paper Volume 2, Issue 12 pp 914—923
Regulation of the mPTP by SIRT3-mediated deacetylation of CypD at lysine 166 suppresses age-related cardiac hypertrophy
- 1 Harvard Medical School, Department of Pathology and Glenn Labs for Aging Research, Boston, MA 02115, USA
- 2 Freie University Berlin, Institute for Chemistry and Biochemistry, Berlin, 14195 Germany
- 3 University of Coimbra, Center for Neurosciences and Cell Biology, 3004-517 Coimbra, Portugal
- 4 Beth Israel Deaconess Medical Center, Cardiovascular Division, Harvard Medical School, Center for Life Science, Boston, MA 02115, USA
Received: December 23, 2010 Accepted: December 27, 2010 Published: December 29, 2010
https://doi.org/10.18632/aging.100252How to Cite
Abstract
Cardiac failure is a leading cause of age-related death, though its root cause remains unknown. Mounting evidence implicates a decline in mitochondrial function due to increased opening of the mitochondrial permeability transition pore (mPTP). Here we report that the NAD+-dependent deacetylase SIRT3 deacetylates the regulatory component of the mPTP, cyclophilin D (CypD) on lysine 166, adjacent to the binding site of cyclosporine A, a CypD inhibitor. Cardiac myocytes from mice lacking SIRT3 exhibit an age-dependent increase in mitochondrial swelling due to increased mPTP opening, a phenotype that is rescued by cyclosporine A. SIRT3 knockout mice show accelerated signs of aging in the heart including cardiac hypertrophy and fibrosis at 13 months of age. SIRT3 knockout mice are also hypersensitive to heart stress induced by transverse aortic constriction (TAC), as evidenced by cardiac hypertrophy, fibrosis, and increased mortality. Together, these data show for the first time that SIRT3 activity is necessary to prevent mitochondrial dysfunction and cardiac hypertrophy during aging and shed light on new pharmacological approaches to delaying aging and treating diseases in cardiac muscle and possibly other post-mitotic tissues.