SIRT4 Protein SIRT4 Protein

Total Page:16

File Type:pdf, Size:1020Kb

SIRT4 Protein SIRT4 Protein Catalogue # Aliquot Size S38-30EG-50 50 µg S38-30EG-200 200 µg SIRT4 Protein Full-length recombinant protein expressed in E. coli cells Catalog # S38-30EG Lot # M334 -4 Product Description Purity Full-length recombinant human SIRT4 was expressed in E. coli cells using an N-terminal GST tag. The gene accession number is NM_012240 . The purity was determined to be Gene Aliases >70% by densitometry. Approx. MW 62kDa . SIR2L4, MGC57437, MGC130046, MGC130047, sirtuin 4 Formulation Recombinant protein stored in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol. Storage and Stability o Store product at –70 C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles. Scientific Background SIRT4 is a member of the sirtuin family of proteins which are homologs to the yeast Sir2 protein. Sirtuin family contain a sirtuin core domain and are grouped into four SIRT4 Protein classes with SIRT4 being a member of class IV. SIRT4 lacks Full-length recombinant protein expressed in E. coli cells deacetylase activity but has ADP-ribosyltransferase Catalog Number activity (1). Immunoprecipitation analysis shows that SIRT4 S38-30EG interacts with the mitochondrial enzyme glutamate Specific Lot Number M334-4 dehydrogenase (GDH), and functional analysis show that Purity >70% SIRT4 ADP-ribosylates and inhibits GDH (2). Concentration 0.2µg/ µl Stability 1yr at –70 oC from date of shipment Downregulation of SIRT4 by RNA interference activates Storage & Shipping Store product at –70 oC. For optimal GDH, thereby upregulating insulin secretion in response to storage, aliquot target into smaller glucose and amino acids. quantities after centrifugation and store at recommended temperature. For References most favorable performance, avoid repeated handling and multiple 1. Frye, R. A. Characterization of five human cDNAs with freeze/thaw cycles. Product shipped on homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) dry ice. metabolize NAD and may have protein ADP- ribosyltransferase activity. Biochem. Biophys. Res. Commun. 260: 273-279, 1999. 2. Haigis, M. C. et al: SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126: 941-954, 2006. To place your order, please contact us by phone 1-(604)-232-4600, fax 1-604-232-4601 or by email: [email protected] www.signalchem.com FOR IN VITRO RESEARCH PURPOSES ONLY. NOT INTENDED FOR USE IN HUMAN OR ANIMALS. .
Recommended publications
  • Subcellular Localization and Mitotic Interactome Analyses Identify SIRT4 As a Centrosomally Localized and Microtubule Associated Protein
    cells Article Subcellular Localization and Mitotic Interactome Analyses Identify SIRT4 as a Centrosomally Localized and Microtubule Associated Protein 1 1, 1 1 Laura Bergmann , Alexander Lang y , Christoph Bross , Simone Altinoluk-Hambüchen , Iris Fey 1, Nina Overbeck 2, Anja Stefanski 2, Constanze Wiek 3, Andreas Kefalas 1, Patrick Verhülsdonk 1, Christian Mielke 4, Dennis Sohn 5, Kai Stühler 2,6, Helmut Hanenberg 3,7, Reiner U. Jänicke 5, Jürgen Scheller 1, Andreas S. Reichert 8 , Mohammad Reza Ahmadian 1 and Roland P. Piekorz 1,* 1 Institute of Biochemistry and Molecular Biology II, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany; [email protected] (L.B.); [email protected] (A.L.); [email protected] (C.B.); [email protected] (S.A.-H.); [email protected] (I.F.); [email protected] (A.K.); [email protected] (P.V.); [email protected] (J.S.); [email protected] (M.R.A.) 2 Molecular Proteomics Laboratory, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany; [email protected] (N.O.); [email protected] (A.S.); [email protected] (K.S.) 3 Department of Otolaryngology and Head/Neck Surgery, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany; [email protected] (C.W.); [email protected] (H.H.) 4 Institute of Clinical Chemistry and Laboratory Diagnostics, Medical Faculty, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany; [email protected]
    [Show full text]
  • Barrea Sirtuin.Pdf
    Growth Hormone & IGF Research 25 (2015) 28–33 Contents lists available at ScienceDirect Growth Hormone & IGF Research journal homepage: www.elsevier.com/locate/ghir Preliminary data on the relationship between circulating levels of Sirtuin 4, anthropometric and metabolic parameters in obese subjects according to growth hormone/insulin-like growth factor-1 status☆ Silvia Savastano a,⁎,CarolinaDiSommab, Annamaria Colao a, Luigi Barrea c, Francesco Orio d, Carmine Finelli e, Fabrizio Pasanisi a, Franco Contaldo a,GiovanniTarantinof a Dipartimento di Medicina Clinica e Chirurgia, Università Federico II di Napoli, Italy b IRCCS SDN, Napoli, Italy c Coleman & IOS srl, Naples, Italy d Dipartimento di Scienze Motorie e del Benessere Università Parthenope Napoli, Italy e Center of Obesity and Eating Disorders, Stella Maris Mediterraneum Foundation, C/da S. Lucia, Chiaromonte, 80035 Potenza, Italy f Centro Ricerche Oncologiche di Mercogliano, Istituto Nazionale Per Lo Studio e La Cura Dei Tumori “Fondazione Giovanni Pascale”,IRCCS,Italy article info abstract Article history: Background: The main components of GH/insulin-like growth factor (IGF)-1 axis and Sirtuin 4 (Sirt4), highly Received 28 July 2014 expressed in liver and skeletal muscle mitochondria, serve as active regulators of mitochondrial oxidative capac- Received in revised form 20 October 2014 ity with opposite functions. In obesity both GH/IGF-1 status and serum Sirt4 levels, likely mirroring its reduced Accepted 21 October 2014 mitochondrial expression, might be altered. Available online 28 October 2014 Objective: To evaluate the association between circulating levels of Sirt4, body composition, metabolic parame- ters and cardio-metabolic risk profile in obese patients according to their different GH/IGF-1 status.
    [Show full text]
  • Charakterisierung Der Interaktion Der Merkelzell-Polyomavirus Kodierten T-Antigene Mit Dem Wirtsfaktor Kap1 Svenja Siebels
    Charakterisierung der Interaktion der Merkelzell-Polyomavirus kodierten T-Antigene mit dem Wirtsfaktor Kap1 DISSERTATION zur Erlangung des Doktorgrades (Dr. rer. nat.) an der Fakultät für Mathematik, Informatik und Naturwissenschaften Fachbereich Biologie der Universität Hamburg vorgelegt von Svenja Siebels Hamburg, Juli 2018 Gutachter: Prof. Dr. Nicole Fischer Prof. Dr. Thomas Dobner Disputation: 19. Oktober 2018 Für meine Familie. Zusammenfassung Das Merkelzell-Polyomavirus (MCPyV) ist nachweislich für ca. 80 % aller Merkelzellkarzinome (Merkel cell carcinoma (MCC)) verantwortlich. Das virale Genom ist dabei monoklonal in die DNA der Wirtszelle integriert und trägt zusätzlich charakteristische Mutationen im T-Lokus. Das MCPyV kodiert wie alle Polyomaviren (PyV) die Tumor-Antigene (T-Ag) Large T-Ag und small T-Ag, die transformierende Eigenschaften besitzen. Dennoch sind viele Fragen zur MCC-Entstehung weiterhin ungeklärt. Insbesondere die Ursprungszelle, aus der das MCC hervorgeht, ist ungewiss. Das unvollständige Wissen um den viralen Lebenszyklus sowie die kontroversen Modelle hinsichtlich des Reservoirs des Virus erschweren zusätzlich das Verständnis zur Tumorentstehung. Um das transformierende Potential des MCPyV LT-Ags zu beleuchten, wurden vor Beginn dieser Arbeit neue zelluläre Interaktionspartner des LT-Ags mithilfe von Tandem-Affinitäts-Aufreinigung und anschließender multidimensionaler Protein-Interaktions-Technologie (MudPIT) identifiziert (M. Czech-Sioli, Manuskript in Arbeit). Unter den Kandidaten befand sich das Chromatin-modifizierende Protein, Zellzyklusregulator und Korepressor Kap1 (KRAB-associated protein 1) als putativer Interaktionspartner des LT-Ags. Die Interaktion des LT-Ags, sT-Ags und des verkürzten tLT-Ags (tLT-Ags) mit dem Wirtsfaktor Kap1 wurde in dieser Arbeit mithilfe von Koimmunpräzipitationen in unterschiedlichen Tumorzelllinien bestätigt. Weiterhin wurde die Bindung des LT-Ags an Kap1 auf den N-Terminus des LT-Ags und die RBCC-Domäne von Kap1 eingegrenzt.
    [Show full text]
  • Sirtuins and Diabetes: Optimizing the Sweetness in the Blood Abhinav Kanwal1* and Liston Augustine Dsouza2
    Kanwal and Dsouza Translational Medicine Communications (2019) 4:3 Translational Medicine https://doi.org/10.1186/s41231-019-0034-7 Communications REVIEW Open Access Sirtuins and diabetes: optimizing the sweetness in the blood Abhinav Kanwal1* and Liston Augustine Dsouza2 Abstract Diabetes Mellitus (DM) is a chronic disease characterized by elevated levels of glucose in the blood. With time it becomes uncontrollable and invites other complex metabolic diseases. The propensity of the people for this disease is age independent. However, sirtuins, which get activate typically during calorie restriction plays a pivotal role in optimizing effect of blood glucose levels in diabetic patients. Among different sirtuin homologs, some of the sirtuins are known for regulating pathophysiology of diabetic condition. Still the role of other sirtuins in understanding the function and regulatory mechanism in DM is still emerging. In this review, we focused on recent studies which help us to understand about the role of sirtuins and how they regulate the pathophysiology in diabetic condition. Keywords: Sirtuins, Diabetes, Diseases, Mitochondria, Exercise, Deacetylation Background deacetylation status and regulates various factors affect- SIRTUINS are the NAD+ dependent enzymes having an ing disease conditions associated with energy metabol- ability to alter the acetaylation/deacetylation status of ism, aging and oxidative stress [9]. Initially, most of the various proteins present in the body. Mammalian sir- studies on sirtuins were focused on cancer biology but tuins consists of 7 members, Sirt1-Sirt7, that are differ- now the paradigm is shifted to unveil their role in other entiated based on their subcellular localization, substrate disease conditions including diabetes. On the other selectivity etc.
    [Show full text]
  • Assessment of Sirtuin 3 and Sirtuin 4 Level in Patients with Diabetes
    JCDP Sirtuins10.5005/jp-journals-10024-2405 in Diabetes and Periodontitis ORIGINAL RESEARCH Assessment of Sirtuin 3 and Sirtuin 4 Level in Patients with Diabetes Mellitus and Periodontitis: A Clinical Study 1Rashmi Laddha, 2Monica Mahajania, 3Amruta Khadse, 4Rajat Bajaj, 5Rashmi Jawade, 6Shashwati Choube ABSTRACT (6.37 ± 0.30). Mean fasting blood sugar (mg/dL) in group I was 80.40 ± 13.05, in group II, it was 160.40 ± 27.20, in group III, it Aim: Periodontitis is considered as infection in periodontal was 77.00 ± 12.78, and in group IV, it was 264.20 ± 53.17. The supporting structure leading to tooth mobility and ulcerated nonsignificant mean expression of SIRT 3 was seen in group I periodontal pockets. The present study was conducted to assess (29.20 ± 3.14), group II (29.19 ± 2.18), group III (28.89 ± 2.77), Sirtuin 3 (SIRT 3) and SIRT 4 level in patients with diabetes and group IV (29.59 ± 5.82). In group I, the mean level of SIRT mellitus (DM) and periodontitis. 4 was 28.93 ± 12.55, in group II, it was 28.82 ± 9.14, in group Materials and methods: The present study was conducted on III, it was 28.88 ± 6.03, and in group IV, it was 29.05 ± 10.68. 60 subjects. Subjects were divided into four groups, groups I to Conclusion: Association of DM and periodontitis is well known. IV. Each group comprised of 15 subjects. In all subjects, fasting The SIRT 3 and SIRT 4 are useful indicators of glycemic level blood glucose level was assessed.
    [Show full text]
  • SIRT4 Blocking Peptide (CDBP6122) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
    SIRT4 blocking peptide (CDBP6122) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Antigen Description 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. [provided by RefSeq, Jul 2008] Immunogen 17 amino acids near the amino terminus of human SIRT4. Nature Synthetic Expression System N/A Species Reactivity Rat, human, mouse Conjugate Unconjugated Applications Used as a blocking peptide in immunoblotting applications. Procedure None Format Liquid Concentration 200 μg/mL Size 0.05mg Preservative None Storage -20°C ANTIGEN GENE INFORMATION Gene Name SIRT4 sirtuin 4 [ Homo sapiens (human) ] Official Symbol SIRT4 Synonyms SIRT4; sirtuin 4; SIR2L4; NAD-dependent protein deacetylase sirtuin-4; sir2-like 4; sirtuin type 4; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 1 © Creative Diagnostics All Rights Reserved SIR2-like protein 4; regulatory protein SIR2 homolog 4; NAD-dependent ADP-ribosyltransferase sirtuin-4 Entrez Gene ID 23409 mRNA Refseq NM_012240 Protein Refseq NP_036372 UniProt ID Q9Y6E7 Pathway Signaling events mediated by HDAC Class I Function NAD+ ADP-ribosyltransferase activity; NAD+ ADP-ribosyltransferase activity; NAD+ binding; NOT NAD-dependent protein deacetylase activity; protein binding; zinc ion binding 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved.
    [Show full text]
  • Novel Mutations in the GLUD1 Gene
    European Journal of Endocrinology (2009) 161 731–735 ISSN 0804-4643 CLINICAL STUDY Hyperinsulinism–hyperammonaemia syndrome: novel mutations in the GLUD1 gene and genotype–phenotype correlations Ritika R Kapoor, Sarah E Flanagan1, Piers Fulton1, Anupam Chakrapani2, Bernadette Chadefaux3, Tawfeg Ben-Omran4, Indraneel Banerjee5, Julian P Shield6, Sian Ellard1 and Khalid Hussain Developmental Endocrinology Research Group, Molecular Genetics Unit, London Centre for Paediatric Endocrinology and Metabolism, Great Ormond Street Hospital for Children NHS Trust, and The Institute of Child Health, University College London, 30 Guilford Street, London WC1N 1EH, UK, 1Institute of Biomedical and Clinical Science, Peninsula Medical School, Exeter EX2 5DW, UK, 2Department of Inherited Metabolic Disorders, Birmingham Children’s Hospital, Birmingham B4 6NH, UK, 3Metabolic Biochemistry, Hoˆpital Necker – Enfants Malades, Universite´ Paris Descartes, Paris, France, 4Clinical and Metabolic Genetics, Department of Pediatrics, Hamad Medical Corporation and Weil-Cornell Medical College, Doha, Qatar, 5Department of Paediatric Endocrinology, Royal Manchester Children’s Hospital and Alder Hey Children’s Hospital, Manchester M27 4HA, UK and 6Department of Child Health, Bristol Royal Hospital for Children, Bristol BS2 8BJ, UK (Correspondence should be addressed to K Hussain; Email: [email protected]) Abstract Background: Activating mutations in the GLUD1 gene (which encodes for the intra-mitochondrial enzyme glutamate dehydrogenase, GDH) cause the hyperinsulinism–hyperammonaemia (HI/HA) syndrome. Patients present with HA and leucine-sensitive hypoglycaemia. GDH is regulated by another intra-mitochondrial enzyme sirtuin 4 (SIRT4). Sirt4 knockout mice demonstrate activation of GDH with increased amino acid-stimulated insulin secretion. Objectives: To study the genotype–phenotype correlations in patients with GLUD1 mutations.
    [Show full text]
  • Integrative Systems Biology Applied to Toxicology
    Integrative Systems Biology Applied to Toxicology Kristine Grønning Kongsbak PhD Thesis January 2015 Integrative Systems Biology Applied to Toxicology Kristine Grønning Kongsbak Søborg 2015 FOOD-PHD-2015 PhD Thesis 2015 Supervisors Professor Anne Marie Vinggaard Senior Scientist Niels Hadrup Division of Toxicology and Risk Assessment National Food Institute Technical University of Denmark Associate Professor Aron Charles Eklund Center for Biological Sequence Analysis Department for Systems Biology Technical University of Denmark Associate Professor Karine Audouze Mol´ecules Th´erapeutiques In Silico Paris Diderot University Funding This project was supported financially by the Ministry of Food, Agriculture and Fisheries of Denmark and the Technical University of Denmark. ©Kristine Grønning Kongsbak FOOD-PHD: ISBN 978-87-93109-30-8 Division of Toxicology and Risk Assessment National Food Institute Technical University of Denmark DK-2860 Søborg, Denmark www.food.dtu.dk 4 Summary Humans are exposed to various chemical agents through food, cosmetics, pharma- ceuticals and other sources. Exposure to chemicals is suspected of playing a main role in the development of some adverse health effects in humans. Additionally, European regulatory authorities have recognized the risk associated with combined exposure to multiple chemicals. Testing all possible combinations of the tens of thousands environmental chemicals is impractical. This PhD project was launched to apply existing computational systems biology methods to toxicological research. In this thesis, I present in three projects three different approaches to using com- putational toxicology to aid classical toxicological investigations. In project I, we predicted human health effects of five pesticides using publicly available data. We obtained a grouping of the chemical according to their potential human health ef- fects that were in concordance with their effects in experimental animals.
    [Show full text]
  • Sirtuins in Tumorigenesis
    PERIODICUM BIOLOGORUM UDC 57:61 VOL. 116, No 4, 381–386, 2014 CODEN PDBIAD ISSN 0031-5362 Overview Sirtuins in tumorigenesis Abstract ANA KULIĆ1 MAJA SIROTKOVIĆ-SKERLEV1 Sirtuins (SIRT) are group of enzymes that require nicotinamide adenine NATALIJA DEDIĆ PLAVETIĆ2 dinucleotide (NAD+) to catalyze their reactions. These chemical compounds 2 BORISLAV BELEV have mono (ADP-ribosyl) transferase or deacetylases activities, and they can 3 SAŠA KRALIK-OGUIĆ be found in nearly all species. The mammalian sirtuin family is described MARIJA IVIĆ4 DAMIR VRBANEC2 by seven proteins, namely. Every group of sirtuins can be found in the dif- ferent regions of the cells; SIRT1 is predominantly nuclear, SIRT2 is lo- 1 Department of Oncology, Division of cated mainly in the cytoplasm (but it can shuttle between the nucleus and Pathophysiology and Experimental Oncology, the cytoplasm), SIRT3, SIRT4, and SIRT5 are mitochondrial proteins, University Hospital Center, Zagreb, Croatia, (SIRT3 can move from the nucleus to mitochondria during cellular stress), 2 Department of Oncology, Division of Medical SIRT6 and SIRT7 are nuclear sirtuins. Sirtuins have a lot of functions in Oncology, University Hospital Center and Zagreb different physiological processes such as gene repression, metabolic control, Medical School, Zagreb, Croatia apoptosis and cell survival, DNA repair, development, inflammation, neu- 3 Department of Laboratory Diagnostic, University roprotection, and healthy aging. Because of so many roles in physiological Hospital Center, Zagreb, Croatia, processes there is a huge interest not just in their functions but also in the 4 University Hospital Center and Zagreb Medical different compounds which can modify their functions. In this article we School, Zagreb, Croatia will focus on the role of sirtuins in tumorigenesis.
    [Show full text]
  • Loss of SIRT4 Promotes the Self-Renewal of Breast Cancer Stem Cells
    Theranostics 2020, Vol. 10, Issue 21 9458 Ivyspring International Publisher Theranostics 2020; 10(21): 9458-9476. doi: 10.7150/thno.44688 Research Paper Loss of SIRT4 promotes the self-renewal of Breast Cancer Stem Cells Lutao Du1, Xiaoyan Liu1, Yidan Ren1, Juan Li1, Peilong Li1, Qinlian Jiao1, 2, Peng Meng3, Fang Wang4, Yuli Wang1, Yun-shan Wang1 and Chuanxin Wang1 1. Department of Clinical Laboratory, The Second Hospital, Cheeloo College of Medicine, Shandong University, 247 Beiyuan Street, Jinan, Shandong, 250033, China. 2. International Biotechnology R&D Center, Shandong University School of Ocean, 180 Wenhua Xi Road, Weihai, Shandong 264209, China. 3. The Medical Department of IVD Division, 3D Medicines, Inc., Pujiang Hi‑tech Park, Shanghai 201114, China. 4. Institute of basic medicine, The Second Hospital, Cheeloo College of Medicine, Shandong University, 247 Beiyuan Street, Jinan, Shandong, 250033, China. Corresponding authors: Yun-shan Wang, Department of Clinical Laboratory, The Second Hospital, Cheeloo College of Medicine, Shandong University, 247 Beiyuan Street, Jinan, Shandong, 250033, China. E-mail: [email protected]; Phone Number: 86-531-85875118; Chuanxin Wang, Department of Clinical Laboratory, The Second Hospital, Cheeloo College of Medicine, Shandong University, 247 Beiyuan Street, Jinan, Shandong, 250033, China. E-mail: [email protected]; Phone Number: 86-531-85875118. © The author(s). This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/). See http://ivyspring.com/terms for full terms and conditions. Received: 2020.02.08; Accepted: 2020.07.07; Published: 2020.07.25 Abstract Rationale: It has been proposed that cancer stem/progenitor cells (or tumor-initiating cells, TICs) account for breast cancer initiation and progression.
    [Show full text]
  • Emerging Role of SIRT2 in Non-Small Cell Lung Cancer (Review)
    ONCOLOGY LETTERS 22: 732, 2021 Emerging role of SIRT2 in non-small cell lung cancer (Review) MENGGE ZHENG, CHANGYONG HU, MENG WU and YUE EUGENE CHIN Institute of Biology and Medical Sciences, Soochow University Medical College, Suzhou, Jiangsu 215123, P.R. China Received October 31, 2020; Accepted April 16, 2021 DOI: 10.3892/ol.2021.12992 Abstract. Non‑small cell lung cancer (NSCLC) is one of the characteristics of NSCLC, the context‑specific function of most devastating cancer types, accounting for >80% of lung SIRT2 remains to be determined. The current review investi‑ cancer cases. The median relative survival time of patients with gated the functions of SIRT2 during NSCLC progression with NSCLC is <1 year. Lysine acetylation is a major post‑trans‑ regard to its regulation of metabolism, stem cell‑like features lational modification that is required for various biological and autophagy. processes, and abnormal protein acetylation is associated with various diseases, including NSCLC. Protein deacetylases are currently considered cancer permissive partly due to malig‑ Contents nant cells being sensitive to deacetylase inhibition. Sirtuin 2 (SIRT2), a primarily cytosolic nicotinamide adenine dinucle‑ 1. Introduction otide‑dependent class III protein deacetylase, has been shown 2. SIRT2 gene and protein to catalyze the removal of acetyl groups from a wide range of 3. SIRT2 biological functions proteins, including tubulin, ribonucleotide reductase regula‑ 4. SIRT2 function in various tumor types tory subunit M2 and glucose‑6‑phosphate dehydrogenase. In 5. Emerging roles of SIRT2 in NSCLC addition, SIRT2 is also known to possess lysine fatty deacyla‑ 6. SIRT2 targeting therapeutic strategy tion activity.
    [Show full text]
  • SIRT4 Overexpression Protects Against Diabetic Nephropathy by Inhibiting Podocyte Apoptosis
    342 EXPERIMENTAL AND THERAPEUTIC MEDICINE 13: 342-348, 2017 SIRT4 overexpression protects against diabetic nephropathy by inhibiting podocyte apoptosis JIAN-XIA SHI, QI-JIN WANG, HUI LI and QIN HUANG Department of Endocrinology, Changhai Hospital, The Second Military Medical University, Shanghai 200433, P.R. China Received June 29, 2015; Accepted September 22, 2016 DOI: 10.3892/etm.2016.3938 Abstract. Diabetic nephropathy is a diabetic complication contribute to the progression of diabetic nephropathy; hyper- associated with capillary damage and increased mortality. glycemia, hypertension, obesity and advancing age have been Sirtuin 4 (SIRT4) plays an important role in mitochondrial extensively characterized (2,3). However, the precise mecha- function and the pathogenesis of metabolic diseases, including nism for this condition remains unclear. Diabetic nephropathy aging kidneys. The aim of the present study was to investigate is characterized by changes in kidney morphology and ultra- the association between SIRT4 and diabetic nephropathy in structure, resulting in an increased glomerular filtration rate, a glucose-induced mouse podocyte model. A CCK-8 assay increased glucose level and blockade of the renin-angiotensin showed that glucose simulation significantly inhibited podo- system (4-6). cyte proliferation in a time- and concentration-dependent Although maintaining control of the glycemic index is chal- manner. Reverse transcription-quantitative polymerase lenging, it lightens the symptoms of diabetic complications, chain reaction and western blot analysis showed that the suggesting that hyperglycemia is the critical induction factor mRNA and protein levels of SIRT4 were notably decreased in the development and progression of diabetic complications, in a concentration-dependent manner in glucose-simulated including diabetic nephropathy (7,8).
    [Show full text]