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miR (show MLXIP Proteins)-15b is a negative regulator of stress-induced SIRT4 expression, thereby counteracting senescence associated mitochondrial dysfunction and regulating the SASP (show ASPRV1 Proteins) and possibly organ aging, such as photoaging of human skin.
SIRT4 overexpression inhibits the proliferation of colorectal cancer cells in vitro and in vivo.
Data indicate that compared to non-neoplastic endometria (NNE (show ENO1 Proteins)), endometrial cancer (EC) showed SIRT7 (show SIRT7 Proteins) mRNA overexpression, whereas SIRT1 (show SIRT1 Proteins), SIRT2 (show SIRT2 Proteins), SIRT4 and SIRT5 (show SIRT5 Proteins) were underexpressed, and no significant differences were observed for SIRT3 (show SIRT3 Proteins) and SIRT6 (show SIRT6 Proteins).
Thus, these results suggest that SIRT4 has essential roles in stress resistance and may be an important therapeutic target for cancer treatment.
SIRT4 behaves as a tumor suppressor at the human tissue protein level.
Overexpression of SIRT4 attenuated inflammation mediators in umbilical vein endothelial cells.
Results show that mitochondrial sirtuins SIRT3 (show SIRT3 Proteins), SIRT4, and SIRT5 (show SIRT5 Proteins) can promote increased mitochondrial respiration and cellular metabolism and respond to excess glucose by inducing a coordinated increase of glycolysis and respiration.
SIRT4 has a tumour-suppressive function and may serve as a novel therapeutic target in colorectal cancer.
Serum Sirt4 was inversely related to anthropometric and metabolic parameters and positively related to peak GH and IGF-1 (show IGF1 Proteins).
C-terminal-binding protein (CtBP (show CTBP2 Proteins)) was found to have an essential role in promoting glutaminolysis by directly repressing the expression of SIRT4.
Until now, a mammalian cellular lipoamidase has not been characterized; this study discovered that SIRT4 can function with this enzymatic capacity in the mitochondria, and that PDH (show PDP Proteins) is a biological substrate; compared to its catalytic efficiency for deacetylation, SIRT4 exhibits far superior enzymatic activity for lipoyl- and biotinyl-lysine modifications.
The results of this study indicated a critical and novel stress response role for SIRT4 in promoting proper glutamate (show GRIN1 Proteins) transport capacity and protecting against excitotoxicity
regulates ATP levels via ANT2 (show SLC25A5 Proteins) and a feedback loop involving AMPK (show PRKAA1 Proteins)
these results highlight the tumor-suppressive role of SIRT4 in Myc-induced B cell lymphoma and suggest that SIRT4 may be a potential target against Myc-induced and/or glutamine-dependent cancers.
The enhanced fatty acid oxidation observed in SIRT4 knockout hepatocytes requires functional SIRT1 (show SIRT1 Proteins), demonstrating a clear cross talk between mitochondrial and nuclear sirtuins.
Data uncover SIRT4 as an important component of the DNA damage response pathway that orchestrates a metabolic block in glutamine metabolism, cell cycle arrest, and tumor suppression.
SIRT4 represses fatty acid oxidation and stimulates lipogenesis. SIRT4 deacetylates and represses malonyl CoA decarboxylase, regulating malonyl coA levels.
Data demonstrate that SIRT4 inhibition increases fat oxidative capacity in liver and mitochondrial function in muscle.
controls insulin secretion in pancreatic beta cells; also transfers an ADP-ribosyl group from NAD to histones
NAD analogues and 32P-NAD were used to study the ADP-ribosyltransferase activity of several different sirtuins, including yeast Sir2 (show SIRT1 Proteins), human SirT1 (show SIRT1 Proteins), mouse SirT4, and mouse SirT6 (show SIRT6 Proteins).
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 IV of the sirtuin family.
sirtuin (silent mating type information regulation 2 homolog) 4 (S. cerevisiae)
, sirtuin 4
, NAD-dependent ADP-ribosyltransferase sirtuin-4
, NAD-dependent protein deacetylase sirtuin-4
, SIR2-like protein 4
, regulatory protein SIR2 homolog 4
, sir2-like 4
, sirtuin type 4
, NAD-dependent deacetylase sirtuin-4