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A NOVEL FORMULATION of HERBS with POTENT ANTI-AGEING ACTIVITY Mohit M
European Journal of Bioinformatics, Vol. 2:1-5, 2014 A NOVEL FORMULATION OF HERBS WITH POTENT ANTI-AGEING ACTIVITY Mohit M. Jaina, Nirmala Kumaria, Geeta Raib* aNEISS Wellness India Limited, Mumbai, India. bDepartment of Molecular and Human Genetics, Banaras Hindu University, Varanasi 221005, India. ABSTRACT Ageing is characterized by a progressive deterioration of physiological functions and metabolic processes. Sirtuin (SIRT1) is a NAD+-dependent protein deacetylase which is a human ortholog of the yeast SIR2 protein. The activation of SIRr2 affects wide variety of cellular processes ranging from metabolism, cell cycle, growth and differentiation, inflammation, senescence, apoptosis, stress response and ageing. There are natural anti- ageing drugs in the market like Resveraterol but some studies suggest that due to its interaction with contraceptive pills it should not be consumed by women taking them. Although, a diet rich in antioxidants seems to offer hope in delaying the onset of unhealthy disorders that accompany ageing, however no clinical treatment using natural herbs has yet been developed and natural anti-aging drugs are still unavailable. In the present study, we evaluated the binding of active ligands present in real grass with the SIRT1 and SIRT5 receptor and compared their binding energy and affinity with other reference anti-ageing drugs present in the market. A high throughput screening comprising of molecular docking, absorption, distribution, metabolism, excretion and toxicity predictions, logP values and percentage of human oral absorption value led to the identification of three potential compounds present in ‘Live Green Real Grass’ which could be considered for anti–ageing activity with better binding affinities than the reference drugs used. -
Cps1) for Studying This Enzyme’S
PhD THESIS USING RECOMBINANT HUMAN CARBAMOYL PHOSPHATE SYNTHETASE 1 (CPS1) FOR STUDYING THIS ENZYME’S FUNCTION, REGULATION, PATHOLOGY AND STRUCTURE Author: CARMEN DÍEZ FERNÁNDEZ Directors: Drs. Vicente Rubio Zamora y Javier Cervera Miralles May 2015 INSTITUTO DE BIOMEDICINA DE VALENCIA (IBV) Vicente Rubio Zamora, Doctor en Medicina, Profesor de Investigación del Consejo Superior de Investigaciones Científicas (CSIC) y Profesor Titular de Bioquímica (en Excedencia) de la Universidad de Valencia, y Javier Cervera Miralles, Doctor en Biología, Investigador jubilado del Centro de Investigación Príncipe Felipe de Valencia, de la Fundación Valenciana de Investigaciones Biomédicas de Valencia, CERTIFICAN: Que Dª, Carmen Díez Fernández, Ingeniera Agrónoma por la Universidad Politécnica de Valencia, con DNI 29208872E, ha realizado bajo su dirección el trabajo de Tesis Doctoral que lleva por título (en lengua inglesa): “Using recombinant human carbamoyl phosphate synthetase 1 (CPS1) for studying this enzyme’s function, regulation, pathology and structure”. Que están de acuerdo con los contenidos del trabajo, realizado en la modalidad de acopio de publicaciones. Que entienden que el trabajo reúne los requisitos para ser susceptible de defensa ante el Tribunal apropiado, por incluir dos publicaciones ya aparecidas y una sometida a evaluación, en revistas internacionales de amplia difusión y en las que la doctoranda es primera autora; así como porque el contenido de las otras secciones de dicho trabajo de tesis reflejan adecuadamente el estado del conocimiento y discuten apropiadamente el contenido y las implicaciones del trabajo realizado; porque las conclusiones recogen un avance suficiente en el campo objeto de estudio como para hacer a la candidata merecedora del doctorado; y, finalmente, porque les consta que ninguno de los coautores de dichas publicaciones, todos ellos ya doctores, han utilizado ni utilizarán las mismas para confeccionar otro trabajo de tesis doctoral. -
Granulosa-Lutein Cell Sirtuin Gene Expression Profiles Differ Between Normal Donors and Infertile Women
International Journal of Molecular Sciences Article Granulosa-Lutein Cell Sirtuin Gene Expression Profiles Differ between Normal Donors and Infertile Women Rebeca González-Fernández 1, Rita Martín-Ramírez 1, Deborah Rotoli 1,2, Jairo Hernández 3, Frederick Naftolin 4, Pablo Martín-Vasallo 1 , Angela Palumbo 3,4 and Julio Ávila 1,* 1 Laboratorio de Biología del Desarrollo, UD de Bioquímica y Biología Molecular and Centro de Investigaciones Biomédicas de Canarias (CIBICAN), Universidad de La Laguna, Av. Astrofísico Sánchez s/n, 38206 La Laguna, Tenerife, Spain; [email protected] (R.G.-F.); [email protected] (R.M.-R.); [email protected] (D.R.); [email protected] (P.M.-V.) 2 Institute of Endocrinology and Experimental Oncology (IEOS), CNR-National Research Council, 80131 Naples, Italy 3 Centro de Asistencia a la Reproducción Humana de Canarias, 38202 La Laguna, Tenerife, Spain; jairoh@fivap.com (J.H.); apalumbo@fivap.com (A.P.) 4 Department of Obstetrics and Gynecology, New York University, New York, NY 10016, USA; [email protected] * Correspondence: [email protected] Received: 13 November 2019; Accepted: 29 December 2019; Published: 31 December 2019 Abstract: Sirtuins are a family of deacetylases that modify structural proteins, metabolic enzymes, and histones to change cellular protein localization and function. In mammals, there are seven sirtuins involved in processes like oxidative stress or metabolic homeostasis associated with aging, degeneration or cancer. We studied gene expression of sirtuins by qRT-PCR in human mural granulosa-lutein cells (hGL) from IVF patients in different infertility diagnostic groups and in oocyte donors (OD; control group). Study 1: sirtuins genes’ expression levels and correlations with age and IVF parameters in women with no ovarian factor. -
Cloning, Chromosomal Characterization and FISH Mapping of the NAD+-Dependent Histone Deacetylase Gene Sirtuin 5 in the Mouse
INTERNATIONAL JOURNAL OF ONCOLOGY 43: 237-245, 2013 Cloning, chromosomal characterization and FISH mapping of the NAD+-dependent histone deacetylase gene sirtuin 5 in the mouse SUSANNE VOELTER-MAHLKNECHT1 and ULRICH MAHLKNECHT2 1Institute of Occupational and Social Medicine and Health Services Research, University of Tuebingen, D-72074 Tuebingen; 2Department of Hematology/Oncology, St. Lukas Klinik Solingen, D-42697 Solingen, Germany Received February 24, 2013; Accepted March 22, 2013 DOI: 10.3892/ijo.2013.1939 Abstract. Sirtuin 5 (SIRT5) is a nicotinamide adenine multiple organisms ranging from bacteria to humans. The dinucleotide (NAD+)-dependent deacetylase, belonging to the sirtuin domain is composed of two distinct motifs binding silent information regulator 2 (Sir2) family of sirtuin histone NAD+ and the acetyl-lysine substrate, respectively (3,4). deacetylases (sirtuins). The yeast Sir2 protein and its mamma- They catalyse the deacetylation of acetylated lysine residues lian derivatives are important in epigenetic gene silencing, of histone substrates and act on non-histone substrates, e.g., DNA repair and recombination, cell cycle, microtubule orga- several transcription factors such as the p53 tumor suppres sor nization and in the regulation of aging. In mammals, 7 sirtuin protein (5), the cytoskeletal protein α-tubulin (6) or the acetyl- isoforms have been identified to date of which three (SIRT3, CoA synthetase (7). Besides the deacetylation reaction, some SIRT4 and SIRT5) are localized in the mitochondria, which sirtuins show ADP ribosyltransferase activity (8,9). serve as the center of energy management and the initiation A dysregulation of the tightly regulated equilibrium of of cellular apoptosis. In the study presented herein, we report acetylation and deacetylation plays an important role both, the genomic organization and chromosomal localization of in the pathogenesis and in the suppression of cancer (10). -
Sirtuin 5 Levels Are Limiting in Preserving Cardiac Function and Suppressing Fibrosis In
bioRxiv preprint doi: https://doi.org/10.1101/2021.06.15.448619; this version posted June 16, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Sirtuin 5 levels are limiting in preserving cardiac function and suppressing fibrosis in response to pressure overload Angela H. Guo1,2, Rachael K. Baliira3,4, Mary E. Skinner1, Surinder Kumar1, Anthony Andren5, Li Zhang5, Shaday Michan6, Norma J. Davis1,7, Merissa W. Maccani1,8, Sharlene M. Day9, David A. Sinclair10, Costas A. Lyssiotis5,10,11, Adam B. Stein11, David B. Lombard1, 12, 13* 1Department of Pathology, University of Michigan, Ann Arbor, Michigan 48109 2Molecular and Cellular Pathology Graduate Program, University of Michigan, Ann Arbor, Michigan 48109 3Cancer Biology Graduate Program, University of Michigan, Ann Arbor, Michigan 48109 4Department of Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109 5Department of Molecular & Integrative Physiology, University of Michigan, Ann Arbor, Michigan 48109 6Independent Researcher, San Diego, CA 92122 7Department of Biomedical Sciences, Duke University School of Medicine, Durham, NC, 27710 8Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia PA 19107 9Department of Internal Medicine, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA 19104 10Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115 11Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109 USA 12Rogel Cancer Center, University of Michigan, Ann Arbor, MI 48109 USA 13Institute of Gerontology, University of Michigan, Ann Arbor, MI 48109 USA 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.06.15.448619; this version posted June 16, 2021. -
Deglutarylation of GCDH by SIRT5 Controls Lysine Metabolism in Mice
bioRxiv preprint doi: https://doi.org/10.1101/2020.06.28.176677; this version posted June 30, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Deglutarylation of GCDH by SIRT5 controls lysine metabolism in mice Dhaval P. Bhatt1†, C. Allie Mills1†, Kristin A. Anderson1,2,3, Bárbara J. Henriques4,5, Tânia G. Lucas4,5, Sara Francisco4,5, Juan Liu3, Olga R. Ilkayeva1, Alexander E. Adams1, Shreyas R. Kulkarni1, Donald S. Backos6, Paul A. Grimsrud1, Cláudio M. Gomes4,5, Matthew D. Hirschey1,2,3* 1Duke Molecular Physiology Institute, Duke University School of Medicine, Durham, NC. 2Sarah W. Stedman Nutrition and Metabolism Center, Duke University School of Medicine, Durham, NC 3Departments of Medicine and Pharmacology & Cancer Biology, Duke University School of Medicine, Durham, NC 4 Biosystems and Integrative Sciences Institute, Faculdade de Ciências, Universidade de Lisboa, 1749- 016 Lisboa, Portugal 5 Departmento de Química e Bioquimica, Faculdade de Ciências, Universidade de Lisboa, 1749-016 Lisboa, Portugal 6 Computational Chemistry and Biology Core Facility, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA †These authors contributed equally to this work *Corresponding author: [email protected] Running Title: SIRT5 deacylates GCDH Keywords: Sirtuin, post-translational modification (PTM), liver, amino acid, cell metabolism, Sirtuin 5 (SIRT5), glutarylation, glutaryl-CoA dehydrogenase (GCDH), lysine metabolism bioRxiv preprint doi: https://doi.org/10.1101/2020.06.28.176677; this version posted June 30, 2020. -
Sirtuin 5: a Review of Structure, Known Inhibitors and Clues for Developing New Inhibitors
SCIENCE CHINA Life Sciences • REVIEW • March 2017 Vol.60 No.3:249–256 doi: 10.1007/s11427-016-0060-7 Sirtuin 5: a review of structure, known inhibitors and clues for developing new inhibitors Lingling Yang1, Xiaobo Ma1, Yanying He1, Chen Yuan1, Quanlong Chen1, Guobo Li2* & Xianggui Chen1** 1College of Food and Bioengineering, Xihua University, Sichuan 610039, China; 2Key Laboratory of Drug Targeting and Drug Delivery System of Ministry of Education, West China School of Pharmacy, Sichuan University, Chengdu 610041, China Received March 21, 2016; accepted May 23, 2016; published online November 17, 2016 Sirtuins (SIRTs) are nicotinamide adenine dinucleotide (NAD+)-dependent protein deacetylases, which regulate important biological processes ranging from apoptosis, age-associated pathophysiologies, adipocyte and muscle differentiation, and energy expenditure to gluconeogenesis. Very recently, sirtuin 5 (SIRT5) has received considerable attention due to that it was found to have weak deacetylase activity but strong desuccinylase, demalonylase and deglutarylase activities, and it was also found to be associated with several human diseases such as cancer, Alzheimer’s disease, and Parkinson’s disease. In this review, we for the first time summarized the structure characteristics, known peptide and small-molecule inhibitors of SIRT5, extracted someclues from current available information and introduced some feasible, practical in silico methods, which might be useful in further efforts to develop new SIRT5 inhibitors. Sirtuin, SIRT5 inhibitor, crystal structure, small-molecule inhibitors, computer-aided drug design Citation: Yang, L., Ma, X., He, Y., Yuan, C., Chen, Q., Li, G., and Chen, X. (2017). Sirtuin 5: a review of structure, known inhibitors and clues for developing new inhibitors. -
Sirtuin 5 Levels Are Limiting in Preserving Cardiac Function and Suppressing Fibrosis In
bioRxiv preprint doi: https://doi.org/10.1101/2021.06.15.448619; this version posted June 16, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Sirtuin 5 levels are limiting in preserving cardiac function and suppressing fibrosis in response to pressure overload Angela H. Guo1,2, Rachael K. Baliira3,4, Mary E. Skinner1, Surinder Kumar1, Anthony Andren5, Li Zhang5, Shaday Michan6, Norma J. Davis1,7, Merissa W. Maccani1,8, Sharlene M. Day9, David A. Sinclair10, Costas A. Lyssiotis5,10,11, Adam B. Stein11, David B. Lombard1, 12, 13* 1Department of Pathology, University of Michigan, Ann Arbor, Michigan 48109 2Molecular and Cellular Pathology Graduate Program, University of Michigan, Ann Arbor, Michigan 48109 3Cancer Biology Graduate Program, University of Michigan, Ann Arbor, Michigan 48109 4Department of Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109 5Department of Molecular & Integrative Physiology, University of Michigan, Ann Arbor, Michigan 48109 6Independent Researcher, San Diego, CA 92122 7Department of Biomedical Sciences, Duke University School of Medicine, Durham, NC, 27710 8Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia PA 19107 9Department of Internal Medicine, University of Pennsylvania, Perelman School of Medicine, Philadelphia, PA 19104 10Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115 11Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109 USA 12Rogel Cancer Center, University of Michigan, Ann Arbor, MI 48109 USA 13Institute of Gerontology, University of Michigan, Ann Arbor, MI 48109 USA 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.06.15.448619; this version posted June 16, 2021. -
Download Special Issue
International Journal of Genomics Noncoding RNAs in Health and Disease Lead Guest Editor: Michele Purrello Guest Editors: Massimo Romani and Davide Barbagallo Noncoding RNAs in Health and Disease International Journal of Genomics Noncoding RNAs in Health and Disease Lead Guest Editor: Michele Purrello Guest Editors: Massimo Romani and Davide Barbagallo Copyright © 2018 Hindawi. All rights reserved. This is a special issue published in “International Journal of Genomics.” All articles are open access articles distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Editorial Board Andrea C. Belin, Sweden M. Hadzopoulou-Cladaras, Greece Ferenc Olasz, Hungary Jacques Camonis, France Sylvia Hagemann, Austria Elena Pasyukova, Russia Prabhakara V. Choudary, USA Henry Heng, USA Graziano Pesole, Italy Martine A. Collart, Switzerland Eivind Hovig, Norway Giulia Piaggio, Italy Monika Dmitrzak-Weglarz, Poland Hieronim Jakubowski, USA Mohamed Salem, USA Marco Gerdol, Italy B.-H. Jeong, Republic of Korea Wilfred van IJcken, Netherlands João Paulo Gomes, Portugal Atsushi Kurabayashi, Japan Brian Wigdahl, USA Soraya E. Gutierrez, Chile Giuliana Napolitano, Italy Jinfa Zhang, USA Contents Noncoding RNAs in Health and Disease Davide Barbagallo, Gaetano Vittone, Massimo Romani , and Michele Purrello Volume 2018, Article ID 9135073, 2 pages Circular RNAs: Biogenesis, Function, and a Role as Possible Cancer Biomarkers Luka Bolha, -
The Deacylase SIRT5 Supports Melanoma Viability by Regulating Chromatin Dynamics
bioRxiv preprint doi: https://doi.org/10.1101/2020.09.07.286526; this version posted September 7, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. The deacylase SIRT5 supports melanoma viability by regulating chromatin dynamics William Giblin1,2, Lauren Bringman-Rodenbarger1, Surinder Kumar1, Mary E. Skinner1, Angela Guo1, Ahmed M. Mostafa1,3, Michelle Azar1, Ahmed S.A. Mady1, Carolina H. Chung4, Namrata Kadambi1, Keith-Allen Melong1, Ho-Joon Lee4, Li Zhang5, Peter SaJJakulnukit5, Sophie Trefely6,7, Erika L. Varner7, Sowmya Iyer8, Min Wang1, James S. Wilmott9, H. Peter Soyer10,11, Richard A. Sturm10, Antonia L. Pritchard12,13, Aleodor Andea1,14, Richard A. Scolyer9,15, Mitchell S. Stark10, David A. Scott16, Douglas R. Fullen1,14, Marcus W. Bosenberg17, Sriram Chandrasekaran4,18,19,20, Zaneta Nikolovska-Coleska1,20, Monique Verhaegen14, Nathaniel W. Snyder7, Miguel N. Rivera8,21, Andrei L. Osterman16, Costas Lyssiotis5,20,22, and David B. Lombard1,20,23* 1Department of Pathology, University of Michigan, Ann Arbor, MI 48109 USA 2Department of Human Genetics, University of Michigan, Ann Arbor, MI 48109 USA 3Department of Biochemistry, Faculty of Pharmacy, Ain Shams University, Cairo, Egypt 4Department of Biomedical Engineering, University of Michigan, Ann Arbor, MI 48109 USA 5Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI 48109 USA 6Department of Cancer Biology, University of Pennsylvania, -
SIRT5 Promotes Hepatocellular Carcinoma Progression by Regulating Mitochondrial Apoptosis
1 SIRT5 Promotes Hepatocellular Carcinoma 2 Progression by Regulating Mitochondrial Apoptosis 3 Rixin Zhang1*, Chengye Wang1*, Yu Tian1,2, Yifan Yao1, Jiakai Mao1, Haibo Wang1, 4 Zhenghan Li1, Yakun Xu1, Mingliang Ye3, Liming Wang1 5 6 1. Division of Hepatobiliary and Pancreatic Surgery, Department of Surgery, The Second Hospital of 7 Dalian Medical University, NO.467, Zhongshan Road, Dalian, Liaoning 116023, China. 8 2. Department of Vascular Surgery, The Second Hospital of Dalian Medical University, NO.467, 9 Zhongshan Road, Dalian, Liaoning 116023, China. 10 3. CAS Key Lab of Separation Sciences for Analytical Chemistry, National Chromatographic Research 11 and Analysis Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, NO.457, 12 Zhongshan Road, Dalian, Liaoning 116023, China. 13 *These authors have contributed equally to this work. 14 Corresponding author: Liming Wang, email: [email protected],Tel # +86-17709870007 15 16 Abstract 17 SIRT5 belongs to a family of NAD+-dependent lysine deacetylases called sirtuins. 18 Although accumulating evidence indicates SIRT5 upregulation in cancers, including 19 liver cancer, the detailed roles and mechanisms remain to be revealed. Hepatocellular 20 carcinoma (HCC) is the second leading cause of cancer-related deaths among men 21 worldwide, and finding effective targets for HCC treatment and prevention is urgently 22 needed. In the present study, we confirmed that mitochondrial sirtuins, particularly 23 SIRT5, are more highly expressed in HCC cell lines than in normal liver cell lines. 24 Moreover, SIRT5 knockdown suppresses HCC cell proliferation and SIRT5 25 overexpression promotes HCC cell proliferation. Furthermore, we verified that SIRT5 26 knockdown increases HCC cell apoptosis via the mitochondrial pathway. -
Sirtuin 5 Regulates Proximal Tubule Fatty Acid Oxidation to Protect Against AKI
BASIC RESEARCH www.jasn.org Sirtuin 5 Regulates Proximal Tubule Fatty Acid Oxidation to Protect against AKI Takuto Chiba,1 Kevin D. Peasley ,1 Kasey R. Cargill,1 Katherine V. Maringer,1 Sivakama S. Bharathi,1 Elina Mukherjee,1 Yuxun Zhang ,1 Anja Holtz ,2 Nathan Basisty ,2 Shiva D. Yagobian,1 Birgit Schilling,2 Eric S. Goetzman,1 and Sunder Sims-Lucas1 1Department of Pediatrics, University of Pittsburgh School of Medicine, University of Pittsburgh Medical Center Children’s Hospital of Pittsburgh, University of Pittsburgh, Pittsburgh, Pennsylvania; and 2Buck Institute for Research on Aging, Novato, California ABSTRACT Background The primary site of damage during AKI, proximal tubular epithelial cells, are highly metabol- ically active, relying on fatty acids to meet their energy demands. These cells are rich in mitochondria and peroxisomes, the two organelles that mediate fatty acid oxidation. Emerging evidence shows that both fatty acid pathways are regulated by reversible posttranslational modifications, particularly by lysine acylation. Sirtuin 5 (Sirt5), which localizes to both mitochondria and peroxisomes, reverses post- translational lysine acylation on several enzymes involved in fatty acid oxidation. However, the role of the Sirt5 in regulating kidney energy metabolism has yet to be determined. Methods We subjected male Sirt5-deficient mice (either +/2 or 2/2) and wild-type controls, as well as isolated proximal tubule cells, to two different AKI models (ischemia-induced or cisplatin-induced AKI). We assessed kidney function and injury with standard techniques and measured fatty acid oxidation 14 14 by the catabolism of C-labeled palmitate to CO2. 2/2 Results Sirt5 was highly expressed in proximal tubular epithelial cells.