title: Diverse roles of SIRT1 in cancer biology and lipid metabolism.
abstract: SIRT1, an NAD(+)-dependent deacetylase, has been described in the literature as a major player in the regulation of cellular stress responses. Its expression has been shown to be altered in cancer cells, and it targets both histone and non-histone proteins for deacetylation and thereby alters metabolic programs in response to diverse physiological stress. Interestingly, many of the metabolic pathways that are influenced by SIRT1 are also altered in tumor development. Not only does SIRT1 have the potential to regulate oncogenic factors, it also orchestrates many aspects of metabolism and lipid regulation and recent reports are beginning to connect these areas. SIRT1 influences pathways that provide an alternative means of deriving energy (such as fatty acid oxidation and gluconeogenesis) when a cell encounters nutritive stress, and can therefore lead to altered lipid metabolism in various pathophysiological contexts. This review helps to show the various connections between SIRT1 and major pathways in cellular metabolism and the consequence of SIRT1 deregulation on carcinogenesis and lipid metabolism.
authors.affiliation: Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. glenn.simmons@utsouthwestern.edu.
authors.forename: Glenn E
authors.initials: GE
authors.lastname: Simmons
authors.affiliation: Department of Immunology and Molecular Microbiology, Texas Tech University Health Sciences Center, 3601 4th Street, STOP 6591, Lubbock, TX 79430-6591, USA. wendy.pruitt@ttuhsc.edu.
authors.forename: Wendy M
authors.initials: WM
authors.lastname: Pruitt
authors.affiliation: Department of Immunology and Molecular Microbiology, Texas Tech University Health Sciences Center, 3601 4th Street, STOP 6591, Lubbock, TX 79430-6591, USA. kevin.pruitt@ttuhsc.edu.
authors.forename: Kevin
authors.initials: K
authors.lastname: Pruitt
mesh_terms: D000091162:AMP-Activated Protein Kinase Kinases; D004734:Energy Metabolism; D005227:Fatty Acids / Q000096:biosynthesis; D000071161:Forkhead Box Protein O1; D051858:Forkhead Transcription Factors / Q000378:metabolism; D006801:Humans; D050356:Lipid Metabolism / Q000502:physiology*; D009369:Neoplasms / Q000378:metabolism / Q000473:pathology*; D047495:PPAR gamma / Q000378:metabolism; D000071248:Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D056564:Sirtuin 1 / Q000378:metabolism*; D051780:Sterol Regulatory Element Binding Protein 1 / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism
chemical_list: C085126:FOXO1 protein, human; D005227:Fatty Acids; D000071161:Forkhead Box Protein O1; D051858:Forkhead Transcription Factors; D047495:PPAR gamma; C486497:PPARGC1A protein, human; D000071248:Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; D051780:Sterol Regulatory Element Binding Protein 1; D014157:Transcription Factors; D017346:Protein Serine-Threonine Kinases; C109790:STK11 protein, human; D000091162:AMP-Activated Protein Kinase Kinases; D056564:Sirtuin 1