Sirt1 and cell migration
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TLDR
It is revealed that cortactin, an F-actin binding protein with established roles in protrusive actin dynamics, is a Sirt1 substrate, and its deacetylations may be an important additional aspect of its tumorigenic activity.Abstract:
Sirt1 is a type III histone deacetylase implicated in a wide range of physiological and pathophysiological roles Acting though a myriad of non-histone substrates, Sirt1 modulates transcriptional regulation of energy metabolism and stress response, with important consequences on cell survival and a myriad of human pathologies Sirt1 has an apparent (albeit context- and tissue type-dependent) role in tumorigenesis, acting particularly through its deacetylation of tumor suppressor gene products such as p53 and Rb Recent works have now revealed that cortactin, an F-actin binding protein with established roles in protrusive actin dynamics, is a Sirt1 substrate Cortactin could be acetylated by the acetyltransferase p300, and its deacetylation by Sirt1, either directly or indirectly, retards cell migration In conjunction with deacetylation of other oncogenic targets, Sirt1’s modulation of cell migration and invasion may be an important additional aspect of its tumorigenic activityread more
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Sirtuin 1 attenuates oxidative stress via upregulation of superoxide dismutase 2 and catalase in astrocytes
Yi Cheng,Hideyuki Takeuchi,Yoshifumi Sonobe,Shijie Jin,Yue Wang,Hiroshi Horiuchi,Bijay Parajuli,Jun Kawanokuchi,Tetsuya Mizuno,Akio Suzumura +9 more
TL;DR: The data suggest that astrocytic SIRT1 may elicit neuroprotective effects through its anti-oxidative and anti-inflammatory functions.
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Expression of SIRT1 and cortactin is associated with progression of non-small cell lung cancer.
Sang Jae Noh,Hyun Ah Baek,Ho Sung Park,Kyu Yun Jang,Woo Sung Moon,Myoung Jae Kang,Dong Geun Lee,Min Ho Kim,Ju-Hyung Lee,Myoung Ja Chung +9 more
TL;DR: The findings suggest that SIRT1 and cortactin may play a role in the progression of NSCLC and may cooperate during tumor progression in NSCLE and shorter overall survival in a univariate analysis.
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SIRT1 inhibits rheumatoid arthritis fibroblast-like synoviocyte aggressiveness and inflammatory response via suppressing NF-κB pathway
Guoqing Li,Zhongbing Xia,Ying Liu,Ying Liu,Fanru Meng,Fanru Meng,Xia Wu,Xia Wu,Yuxuan Fang,Yuxuan Fang,Chunwang Zhang,Chunwang Zhang,Dan Liu +12 more
TL;DR: The results suggest SIRT1 is a key regulator in RA pathogenesis by suppressing aggressive phenotypes and inflammatory response of FLS by inhibiting synovial hyperplasia and inflammation.
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Roles of SIRT1 in granulosa cell apoptosis during the process of follicular atresia in porcine ovary
TL;DR: The results suggest that SIRT1 may play important roles in the regulation of granulosa cell apoptosis during follicular atresia in porcine ovary.
Journal ArticleDOI
Inhibition of sirtuins 1 and 2 impairs cell survival and migration and modulates the expression of P-glycoprotein and MRP3 in hepatocellular carcinoma cell lines.
María Paula Ceballos,Giulia Decándido,Ariel D. Quiroga,Carla G. Comanzo,Verónica Inés Livore,Florencia Lorenzetti,Flavia Lambertucci,Lorena Chazarreta-Cifre,Claudia Banchio,María de Luján Alvarez,Aldo D. Mottino,María Cristina Carrillo +11 more
TL;DR: Both drugs decreased HCC cells survival and migration, suggesting SIRTs 1 and 2 activities blockage could be beneficial during HCC therapy, and downregulation of the expression of P-gp and MRP3 supports the potential application of SIRTB inhibitions in combination with conventional chemotherapy.
References
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Journal ArticleDOI
Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1.
Joseph T. Rodgers,Carlos Lerin,Wilhelm Haas,Steven P. Gygi,Bruce M. Spiegelman,Pere Puigserver +5 more
TL;DR: It is shown that the Sir2 homologue, SIRT1 controls the gluconeogenic/glycolytic pathways in liver in response to fasting signals through the transcriptional coactivator PGC-1α, and this findings have strong implications for the basic pathways of energy homeostasis, diabetes and lifespan.
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Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase
Fan Yeung,Jamie E. Hoberg,Catherine S. Ramsey,Michael D Keller,David R. Jones,Roy A. Frye,Marty W. Mayo +6 more
TL;DR: It is demonstrated that SIRT1, a nicotinamide adenosine dinucleotide‐dependent histone deacetylase, regulates the transcriptional activity of NF‐κB and activity augments apoptosis in response to TNFα.
Journal ArticleDOI
HDAC6 is a microtubule-associated deacetylase
Charlotte Hubbert,Amaris Guardiola,Rong Shao,Yoshiharu Kawaguchi,Akihiro Ito,Andrew B. Nixon,Minoru Yoshida,Xiao-Fan Wang,Tso-Pang Yao +8 more
TL;DR: The results show that HDAC6 is the tubulin deacetylase, and provide evidence that reversible acetylation regulates important biological processes beyond histone metabolism and gene transcription, including microtubule-dependent cell motility.
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Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma.
Frederic Picard,Martin Kurtev,Namjin Chung,Acharawan Topark-Ngarm,Thanaset Senawong,Rita Machado de Oliveira,Rita Machado de Oliveira,Mark Leid,Michael W. McBurney,Leonard Guarente +9 more
TL;DR: It is shown that the mammalian SIR2 orthologue, Sirt1 (sirtuin 1), activates a critical component of calorie restriction in mammals; that is, fat mobilization in white adipocytes.
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The Sir2 Family of Protein Deacetylases
Gil Blander,Leonard Guarente +1 more
TL;DR: The role of NAD+, the unusual products of the deacetylation reaction, the Sir2 structure, and the Sir1 and Sir2 chemical inhibitors and activators that were recently identified are discussed.