gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Sirtuin 3

SIRT3, sirtuin 3
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Two alternatively spliced transcript variants that encode different proteins have been described for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Sir2, CAN, V1a, Ros, AGE
Papers using SIRT3 antibodies
Role of Sirtuin Histone Deacetylase SIRT1 in Prostate Cancer.
Supplier
Appanna Vasu D., In PLoS ONE, 2008
... Antibodies against Acetylated Lysine (AcK), ACC, phospho-ACC (S79), AMPK, phospho-AMPK (T172), SIRT1, SIRT3 and AceCS1 were from Cell Signaling Technologies (Beverly, MA) ...
Online monitoring of cell metabolism for studying pharmacodynamic effects
Supplier
Mahlknecht Ulrich et al., In Clinical Epigenetics, 2006
... Antibodies that were used for immunoblotting: anti-Flag M2 (Sigma-Aldrich, Deisenhofen, Germany), anti-SIRT3 (Imgenex, San Diego, CA, USA) ...
The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide–dependent deacetylase
Supplier
Verdin Eric et al., In The Journal of Cell Biology, 1996
... The SIRT3 sequence was PCR amplified from human spleen Marathon cDNA library (CLONTECH Laboratories, Inc.) and cloned ...
Papers on SIRT3
Loss of Fatty Acid Binding Protein 4/aP2 Reduces Macrophage Inflammation Through Activation of SIRT3.
New
Bernlohr et al., Minneapolis, United States. In Mol Endocrinol, Feb 2016
Herein,we show that loss of FABP4/aP2 in macrophages additionally induces SIRT3 expression and that monounsaturated fatty acids (C16:1, C18:1) lead to increased SIRT3 protein expression.
Role of Sirt3 in mitochondrial biogenesis and developmental competence of human in vitro matured oocytes.
New
Qiao et al., Beijing, China. In Hum Reprod, Feb 2016
STUDY QUESTION: Does Sirt3 dysfunction result in poor developmental outcomes for human oocytes after in vitro maturation (IVM)?
Nutritional stress exacerbates hepatic steatosis induced by deletion of the histidine nucleotide binding (Hint2) mitochondrial protein.
New
St-Pierre et al., Bern, Switzerland. In Am J Physiol Gastrointest Liver Physiol, Feb 2016
Several proteins identified as substrates of sirtuin 3 and 5 and active in intermediary and ketone metabolism were hyperacetylated in liver and brown fat mitochondria after both HFD and fasting regimens.
Weight loss is associated with increased NAD(+)/SIRT1 expression but reduced PARP activity in white adipose tissue.
New
Pietiläinen et al., Helsinki, Finland. In J Clin Endocrinol Metab, Feb 2016
RESULTS: SIRT1, SIRT3, SIRT7 and NAMPT expressions were significantly lower, whereas total PARP activity was increased in obese compared with lean subjects.
Mitochondrial SIRT3 Mediates Adaptive Responses of Neurons to Exercise and Metabolic and Excitatory Challenges.
New
Impact
Mattson et al., Baltimore, United States. In Cell Metab, Feb 2016
Here we show that the mitochondrial protein deacetylase SIRT3 mediates adaptive responses of neurons to bioenergetic, oxidative, and excitatory stress.
Sirtuins-mediators of maternal obesity-induced complications in offspring?
Review
New
Saad et al., Sydney, Australia. In Faseb J, Jan 2016
Sirtuins (SIRTs), particularly SIRT1 and SIRT3, are NAD(+)-dependent deacetylases that regulate metabolic balance and stress responses in both central and peripheral tissues, of which dysregulation is a well-established mediator for the development and effects of obesity.
Loss of Mitochondrial Tumor Suppressor Genes Expression Is Associated with Unfavorable Clinical Outcome in Head and Neck Squamous Cell Carcinoma: Data from Retrospective Study.
New
Kayani et al., Islamabad, Pakistan. In Plos One, Dec 2015
A family of orthologues of yeast silent information regulator 3 (SIRT3), 4 (SIRT4) and mitochondrial tumor suppressor 1 (MTUS1) are important mitochondrial tumor suppressor genes which play an important role in the progression of multiple cancers.
Sirtuin-dependent clock control: new advances in metabolism, aging and cancer.
Review
New
Masri, Irvine, United States. In Curr Opin Clin Nutr Metab Care, Nov 2015
In addition to sirtuin (SIRT)1 and SIRT3, SIRT6 has been demonstrated as a critical regulator of circadian transcription that also serves as an interface with metabolic homeostasis.
The role of sirtuins in cardiac disease.
Review
New
Sadoshima et al., Newark, United States. In Am J Physiol Heart Circ Physiol, Nov 2015
Seven sirtuin family proteins (Sirt1-7) have been identified as mammalian SIR2 orthologs, localized in different subcellular compartments, namely, the cytoplasm (Sirt1, 2), the mitochondria (Sirt3, 4, 5), and the nucleus (Sirt1, 2, 6, 7).
SIRT3 regulates progression and development of diseases of aging.
Review
New
Hirschey et al., Durham, United States. In Trends Endocrinol Metab, Sep 2015
The mitochondrial sirtuin SIRT3 is a protein deacylase that influences almost every major aspect of mitochondrial biology, including nutrient oxidation, ATP generation, reactive oxygen species (ROS) detoxification, mitochondrial dynamics, and the mitochondrial unfolded protein response (UPR).
SIRT3 mediates multi-tissue coupling for metabolic fuel switching.
New
Impact
Denu et al., Madison, United States. In Cell Metab, May 2015
SIRT3 is a member of the Sirtuin family of NAD(+)-dependent deacylases and plays a critical role in metabolic regulation.
Activation of SIRT3 by the NAD⁺ precursor nicotinamide riboside protects from noise-induced hearing loss.
Impact
Jaffrey et al., New York City, United States. In Cell Metab, 2015
These effects are mediated by the NAD(+)-dependent mitochondrial sirtuin, SIRT3, since SIRT3-overexpressing mice are resistant to NIHL and SIRT3 deletion abrogates the protective effects of NR and expression of NAD(+) biosynthetic enzymes.
Boosting NAD to spare hearing.
Impact
Brenner, Iowa City, United States. In Cell Metab, 2015
Hearing protection by nicotinamide riboside depends on Sirt3.
The Role of Mitochondrial DNA in Mediating Alveolar Epithelial Cell Apoptosis and Pulmonary Fibrosis.
Review
Kamp et al., Chicago, United States. In Int J Mol Sci, 2014
We then review recent studies linking the sirtuin (SIRT) family members, especially SIRT3, to mitochondrial integrity and mtDNA damage repair and aging.
Sirtuin 3 deficiency is associated with inhibited mitochondrial function and pulmonary arterial hypertension in rodents and humans.
Impact
Michelakis et al., Edmonton, Canada. In Cell Metab, 2014
Mice lacking sirtuin 3 (SIRT3), a mitochondrial deacetylase, have increased acetylation and inhibition of many mitochondrial enzymes and complexes, suppressing mitochondrial function.
Resveratrol stimulates cortisol biosynthesis by activating SIRT-dependent deacetylation of P450scc.
GeneRIF
Sewer et al., San Diego, United States. In Endocrinology, 2012
NAD(+)-dependent SIRT deacetylase has a role in regulating the expression of mitochondrial steroidogenic P450
Sirt3 inhibits hepatocellular carcinoma cell growth through reducing Mdm2-mediated p53 degradation.
GeneRIF
Zhou et al., Chengdu, China. In Biochem Biophys Res Commun, 2012
these data suggests that Sirt3 may play an important role in hepatocellular carcinoma development and progression. Sirt3 overexpression upregulated p53 protein level through downregulating Mdm2 and thereby slowing p53 degradation.
Friedreich's ataxia reveals a mechanism for coordinate regulation of oxidative metabolism via feedback inhibition of the SIRT3 deacetylase.
GeneRIF
Payne et al., Indianapolis, United States. In Hum Mol Genet, 2012
Data show that the respiratory chain defects accompanying frataxin deficiency cause progressive hyperacetylation of cardiac mitochondrial proteins due to the inhibition of SIRT3 deacetylase.
SIRT3 is a mitochondrial tumor suppressor: a scientific tale that connects aberrant cellular ROS, the Warburg effect, and carcinogenesis.
GeneRIF
Gius et al., Boston, United States. In Cancer Res, 2012
SIRT3 is a mitochondrial tumor suppressor: a scientific tale that connects aberrant cellular ROS, the Warburg effect, and carcinogenesis.(
SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status.
GeneRIF
Denu et al., Madison, United States. In J Biol Chem, 2012
SIRT3 protein deacetylates isocitrate dehydrogenase 2 (IDH2) and regulates mitochondrial redox status
share on facebooktweetadd +1mail to friends