Genomic Counter-Stress Changes Induced by the Relaxation Response Jeffery A
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Autism Multiplex Family with 16P11.2P12.2 Microduplication Syndrome in Monozygotic Twins and Distal 16P11.2 Deletion in Their Brother
European Journal of Human Genetics (2012) 20, 540–546 & 2012 Macmillan Publishers Limited All rights reserved 1018-4813/12 www.nature.com/ejhg ARTICLE Autism multiplex family with 16p11.2p12.2 microduplication syndrome in monozygotic twins and distal 16p11.2 deletion in their brother Anne-Claude Tabet1,2,3,4, Marion Pilorge2,3,4, Richard Delorme5,6,Fre´de´rique Amsellem5,6, Jean-Marc Pinard7, Marion Leboyer6,8,9, Alain Verloes10, Brigitte Benzacken1,11,12 and Catalina Betancur*,2,3,4 The pericentromeric region of chromosome 16p is rich in segmental duplications that predispose to rearrangements through non-allelic homologous recombination. Several recurrent copy number variations have been described recently in chromosome 16p. 16p11.2 rearrangements (29.5–30.1 Mb) are associated with autism, intellectual disability (ID) and other neurodevelopmental disorders. Another recognizable but less common microdeletion syndrome in 16p11.2p12.2 (21.4 to 28.5–30.1 Mb) has been described in six individuals with ID, whereas apparently reciprocal duplications, studied by standard cytogenetic and fluorescence in situ hybridization techniques, have been reported in three patients with autism spectrum disorders. Here, we report a multiplex family with three boys affected with autism, including two monozygotic twins carrying a de novo 16p11.2p12.2 duplication of 8.95 Mb (21.28–30.23 Mb) characterized by single-nucleotide polymorphism array, encompassing both the 16p11.2 and 16p11.2p12.2 regions. The twins exhibited autism, severe ID, and dysmorphic features, including a triangular face, deep-set eyes, large and prominent nasal bridge, and tall, slender build. The eldest brother presented with autism, mild ID, early-onset obesity and normal craniofacial features, and carried a smaller, overlapping 16p11.2 microdeletion of 847 kb (28.40–29.25 Mb), inherited from his apparently healthy father. -
Airway Inflammation Mitochondrial Dysfunction Increases Allergic
Mitochondrial Dysfunction Increases Allergic Airway Inflammation Leopoldo Aguilera-Aguirre, Attila Bacsi, Alfredo Saavedra-Molina, Alexander Kurosky, Sanjiv Sur and Istvan This information is current as Boldogh of October 1, 2021. J Immunol 2009; 183:5379-5387; Prepublished online 28 September 2009; doi: 10.4049/jimmunol.0900228 http://www.jimmunol.org/content/183/8/5379 Downloaded from References This article cites 61 articles, 11 of which you can access for free at: http://www.jimmunol.org/content/183/8/5379.full#ref-list-1 http://www.jimmunol.org/ Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication by guest on October 1, 2021 *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2009 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Mitochondrial Dysfunction Increases Allergic Airway Inflammation1 Leopoldo Aguilera-Aguirre,*§ Attila Bacsi,*¶ Alfredo Saavedra-Molina,§ Alexander Kurosky,† Sanjiv Sur,‡ and Istvan Boldogh*2 The prevalence of allergies and asthma among the world’s population has been steadily increasing due to environmental factors. -
Multi-Targeted Mechanisms Underlying the Endothelial Protective Effects of the Diabetic-Safe Sweetener Erythritol
Multi-Targeted Mechanisms Underlying the Endothelial Protective Effects of the Diabetic-Safe Sweetener Erythritol Danie¨lle M. P. H. J. Boesten1*., Alvin Berger2.¤, Peter de Cock3, Hua Dong4, Bruce D. Hammock4, Gertjan J. M. den Hartog1, Aalt Bast1 1 Department of Toxicology, Maastricht University, Maastricht, The Netherlands, 2 Global Food Research, Cargill, Wayzata, Minnesota, United States of America, 3 Cargill RandD Center Europe, Vilvoorde, Belgium, 4 Department of Entomology and UCD Comprehensive Cancer Center, University of California Davis, Davis, California, United States of America Abstract Diabetes is characterized by hyperglycemia and development of vascular pathology. Endothelial cell dysfunction is a starting point for pathogenesis of vascular complications in diabetes. We previously showed the polyol erythritol to be a hydroxyl radical scavenger preventing endothelial cell dysfunction onset in diabetic rats. To unravel mechanisms, other than scavenging of radicals, by which erythritol mediates this protective effect, we evaluated effects of erythritol in endothelial cells exposed to normal (7 mM) and high glucose (30 mM) or diabetic stressors (e.g. SIN-1) using targeted and transcriptomic approaches. This study demonstrates that erythritol (i.e. under non-diabetic conditions) has minimal effects on endothelial cells. However, under hyperglycemic conditions erythritol protected endothelial cells against cell death induced by diabetic stressors (i.e. high glucose and peroxynitrite). Also a number of harmful effects caused by high glucose, e.g. increased nitric oxide release, are reversed. Additionally, total transcriptome analysis indicated that biological processes which are differentially regulated due to high glucose are corrected by erythritol. We conclude that erythritol protects endothelial cells during high glucose conditions via effects on multiple targets. -
UQCRC2 Antibody Order 021-34695924 [email protected] Support 400-6123-828 50Ul [email protected] 100 Ul √ √ Web
TD12339 UQCRC2 Antibody Order 021-34695924 [email protected] Support 400-6123-828 50ul [email protected] 100 uL √ √ Web www.ab-mart.com.cn Description: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b- c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (By similarity). The 2 core subunits UQCRC1/QCR1 and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they seem to have preserved their MPP processing properties (By similarity). May be involved in the in situ processing of UQCRFS1 into the mature Rieske protein and its mitochondrial -
Aneuploidy: Using Genetic Instability to Preserve a Haploid Genome?
Health Science Campus FINAL APPROVAL OF DISSERTATION Doctor of Philosophy in Biomedical Science (Cancer Biology) Aneuploidy: Using genetic instability to preserve a haploid genome? Submitted by: Ramona Ramdath In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Science Examination Committee Signature/Date Major Advisor: David Allison, M.D., Ph.D. Academic James Trempe, Ph.D. Advisory Committee: David Giovanucci, Ph.D. Randall Ruch, Ph.D. Ronald Mellgren, Ph.D. Senior Associate Dean College of Graduate Studies Michael S. Bisesi, Ph.D. Date of Defense: April 10, 2009 Aneuploidy: Using genetic instability to preserve a haploid genome? Ramona Ramdath University of Toledo, Health Science Campus 2009 Dedication I dedicate this dissertation to my grandfather who died of lung cancer two years ago, but who always instilled in us the value and importance of education. And to my mom and sister, both of whom have been pillars of support and stimulating conversations. To my sister, Rehanna, especially- I hope this inspires you to achieve all that you want to in life, academically and otherwise. ii Acknowledgements As we go through these academic journeys, there are so many along the way that make an impact not only on our work, but on our lives as well, and I would like to say a heartfelt thank you to all of those people: My Committee members- Dr. James Trempe, Dr. David Giovanucchi, Dr. Ronald Mellgren and Dr. Randall Ruch for their guidance, suggestions, support and confidence in me. My major advisor- Dr. David Allison, for his constructive criticism and positive reinforcement. -
Inherited Variants in Mitochondrial Biogenesis Genes May Influence Epithelial Ovarian Cancer Risk Jennifer Permuth-Wey1,2, Y. An
Author Manuscript Published OnlineFirst on March 29, 2011; DOI: 10.1158/1055-9965.EPI-10-1224 Author manuscripts have been peer reviewed and accepted for publication but have not yet been edited. Inherited Variants in Mitochondrial Biogenesis Genes May Influence Epithelial Ovarian Cancer Risk Jennifer Permuth-Wey1,2, Y. Ann Chen3 ,Ya-Yu Tsai1, Zhihua Chen4, Xiaotao Qu4, Johnathan M. Lancaster5, Heather Stockwell2, Getachew Dagne2, Edwin Iversen6, Harvey Risch7, Jill Barnholtz-Sloan8, Julie M. Cunningham9, Robert A. Vierkant10, Brooke L. Fridley10, Rebecca Sutphen11, John McLaughlin12, Steven A. Narod13, Ellen L. Goode10, Joellen M. Schildkraut14, David Fenstermacher4, Catherine M. Phelan1, and Thomas A. Sellers1 1Department of Cancer Epidemiology, Moffitt Cancer Center, Tampa, FL, USA. 2 Department of Epidemiology and Biostatistics, College of Public Health, University of South Florida, Tampa, FL, USA. 3 Department of Biostatistics, Moffitt Cancer Center, Tampa, FL, USA. 4 Department of Biomedical Informatics, Moffitt Cancer Center, Tampa, FL, USA. 5 Department of Women’s Oncology, Moffitt Cancer Center, Tampa, FL, USA. 6 Department of Statistical Science, Duke University Medical Center, Durham, NC, USA. 7Department of Epidemiology and Public Health, Yale University School of Medicine, New Haven, CT, USA. 8Case Comprehensive Cancer Center, Case School of Medicine, Cleveland, OH, USA. 9 Department of Laboratory Medicine and Pathology, Mayo Clinic College of Medicine, Rochester, MN, USA. 10Department of Health Sciences Research, Mayo Clinic College of Medicine, Rochester, MN, USA. 11Pediatrics Epidemiology Center, College of Medicine, University of South Florida, Tampa, FL, USA. 12Samuel Lunenfeld Research Institute, Toronto, Ontario, Canada. 13Center for Research in Women’s Health, Toronto, ON, Canada. 14Department of Community and Family Medicine, Duke University Medical Center, Durham, NC, USA. -
UQCRFS1N Assembles Mitochondrial Respiratory Complex-III Into an Asymmetric 21-Subunit Dimer
Protein Cell 2018, 9(6):586–591 https://doi.org/10.1007/s13238-018-0515-x Protein & Cell LETTER TO THE EDITOR UQCRFS1N assembles mitochondrial respiratory complex-III into an asymmetric 21-subunit dimer Dear Editor, Although several structures have been solved with very high resolution, the full length N-terminal processed peptide (1– Mitochondrial respiratory chain consists of four multimeric 78 amino acids, UQCRFS1N) of the iron-sulfur Rieske pro- protein complexes, Complex I-IV (CI, NADH dehydroge- tein (UQCRFS1) subunit has not been assigned in all of nase; CII, succinate:ubiquinone oxidoreductase; CIII, cyto- these structures (Table 1). UQCRFS1N is the N-terminal chrome bc1 complex; and CIV, cytochrome c oxidase). Cell mitochondrial targeting sequence of UQCRFS1, and after its These four complexes transfer electrons from NADH or cleavage from the precursor, this small peptide remains & FADH to oxygen and pump protons from mitochondrial 2 bound to CIII with unknown functions. In this letter, we show matrix to intermembrane space, generating electrochemical that one UQCRFS1N links the two 10-subunit CIII protomers gradient across the inner membrane which is harnessed by together to form the intact CIII, which resultantly contains complex V to synthesize ATP, providing the majority of only 21 subunits rather than previously assumed 22 subunits energy acquired by living organisms. Respiratory chain Protein (Fig. 1A and 1B). complexes were reported to interact with each other to form Firstly, we rebuilt the high-resolution crystal structures of supercomplexes, even megacomplex (Guo et al., 2017). bovine CIII (PDB: 2A06) (Huang et al., 2005) and chicken However, despite decades of intensive research, many CIII (PDB:3TGU) (Hao et al., 2012). -
Differential Expression of Multiple Disease-Related Protein Groups
brain sciences Article Differential Expression of Multiple Disease-Related Protein Groups Induced by Valproic Acid in Human SH-SY5Y Neuroblastoma Cells 1,2, 1, 1 1 Tsung-Ming Hu y, Hsiang-Sheng Chung y, Lieh-Yung Ping , Shih-Hsin Hsu , Hsin-Yao Tsai 1, Shaw-Ji Chen 3,4 and Min-Chih Cheng 1,* 1 Department of Psychiatry, Yuli Branch, Taipei Veterans General Hospital, Hualien 98142, Taiwan; [email protected] (T.-M.H.); [email protected] (H.-S.C.); [email protected] (L.-Y.P.); fi[email protected] (S.-H.H.); [email protected] (H.-Y.T.) 2 Department of Future Studies and LOHAS Industry, Fo Guang University, Jiaosi, Yilan County 26247, Taiwan 3 Department of Psychiatry, Mackay Medical College, New Taipei City 25245, Taiwan; [email protected] 4 Department of Psychiatry, Taitung Mackay Memorial Hospital, Taitung County 95064, Taiwan * Correspondence: [email protected]; Tel.: +886-3888-3141 (ext. 475) These authors contributed equally to this work. y Received: 10 July 2020; Accepted: 8 August 2020; Published: 12 August 2020 Abstract: Valproic acid (VPA) is a multifunctional medication used for the treatment of epilepsy, mania associated with bipolar disorder, and migraine. The pharmacological effects of VPA involve a variety of neurotransmitter and cell signaling systems, but the molecular mechanisms underlying its clinical efficacy is to date largely unknown. In this study, we used the isobaric tags for relative and absolute quantitation shotgun proteomic analysis to screen differentially expressed proteins in VPA-treated SH-SY5Y cells. We identified changes in the expression levels of multiple proteins involved in Alzheimer’s disease, Parkinson’s disease, chromatin remodeling, controlling gene expression via the vitamin D receptor, ribosome biogenesis, ubiquitin-mediated proteolysis, and the mitochondrial oxidative phosphorylation and electron transport chain. -
UQCRC2 Antibody
Efficient Professional Protein and Antibody Platforms UQCRC2 Antibody Basic information: Catalog No.: UPA60311 Source: Rabbit Size: 50ul/100ul Clonality: Polyclonal Concentration: 1mg/ml Isotype: Rabbit IgG Purification: Protein affinity purified. Useful Information: WB:1:1000-2000 ICC:1:50-1:200 Applications: IHC:1:50-1:200 FC:1:50-1:100 Reactivity: Human, Mouse, Rat Specificity: This antibody recognizes UQCRC2 protein. Immunogen: Recombinant protein within human UQCRC2 aa 100-350. Cytochrome c is a well characterized, mobile electron transport protein that is essential to energy conversion in all aerobic organisms. Cytochrome b as- sociates with cytochrome c subunit 1 and the Rieske protein to form com- plex III (also designated cytochrome bc1 complex), which is involved in cel- lular respiration. Ubiquinol cytochrome c reductase (UQCRFS1), also re- ferred to as Rieske iron-sulfur protein, represents an important subunit of Description: complex III of the mitochondrial respiratory chain that transfers electrons from ubiquinol to cytochrome c. The UQCRFS1 complex is made up of 3 res- piratory subunits (cytochrome b, cytochrome c1, Rieske protein), 2 core proteins, and 6 low-molecular weight proteins. Ubiquinol cytochrome-c re- ductase complex core protein 2 (UQCRC2) represents one of the core pro- teins of UQCRFS1, and it is required for the assembly of the complex. Uniprot: P22695(Human) Q9DB77(Mouse) P32551(Rat) BiowMW: 48 kDa Buffer: 1*TBS (pH7.4), 0.5%BSA, 50%Glycerol. Preservative: 0.05% Sodium Azide. Storage: Store at 4°C short term and -20°C long term. Avoid freeze-thaw cycles. Note: For research use only, not for use in diagnostic procedure. -
Gene Expression in the Mouse Eye: an Online Resource for Genetics Using 103 Strains of Mice
Molecular Vision 2009; 15:1730-1763 <http://www.molvis.org/molvis/v15/a185> © 2009 Molecular Vision Received 3 September 2008 | Accepted 25 August 2009 | Published 31 August 2009 Gene expression in the mouse eye: an online resource for genetics using 103 strains of mice Eldon E. Geisert,1 Lu Lu,2 Natalie E. Freeman-Anderson,1 Justin P. Templeton,1 Mohamed Nassr,1 Xusheng Wang,2 Weikuan Gu,3 Yan Jiao,3 Robert W. Williams2 (First two authors contributed equally to this work) 1Department of Ophthalmology and Center for Vision Research, Memphis, TN; 2Department of Anatomy and Neurobiology and Center for Integrative and Translational Genomics, Memphis, TN; 3Department of Orthopedics, University of Tennessee Health Science Center, Memphis, TN Purpose: Individual differences in patterns of gene expression account for much of the diversity of ocular phenotypes and variation in disease risk. We examined the causes of expression differences, and in their linkage to sequence variants, functional differences, and ocular pathophysiology. Methods: mRNAs from young adult eyes were hybridized to oligomer microarrays (Affymetrix M430v2). Data were embedded in GeneNetwork with millions of single nucleotide polymorphisms, custom array annotation, and information on complementary cellular, functional, and behavioral traits. The data include male and female samples from 28 common strains, 68 BXD recombinant inbred lines, as well as several mutants and knockouts. Results: We provide a fully integrated resource to map, graph, analyze, and test causes and correlations of differences in gene expression in the eye. Covariance in mRNA expression can be used to infer gene function, extract signatures for different cells or tissues, to define molecular networks, and to map quantitative trait loci that produce expression differences. -
Impact of the Mitochondrial Genetic Background in Complex III Deficiency
Impact of the Mitochondrial Genetic Background in Complex III Deficiency Mari Carmen Gil Borlado1., David Moreno Lastres1,2., Maritza Gonzalez Hoyuela1., Maria Moran1,2, Alberto Blazquez1,2, Rosa Pello1, Lorena Marin Buera1,2, Toni Gabaldon3, Juan Jose Garcia Pen˜ as4, Miguel A. Martı´n1,2, Joaquin Arenas1,2, Cristina Ugalde1,2* 1 Centro de Investigacio´n, Hospital Universitario 12 de Octubre, Madrid, Spain, 2 Centro de Investigacio´n Biome´dica en Red de Enfermedades Raras-CIBERER, U723, Madrid, Spain, 3 Centre for Genomic Regulation-CRG, Barcelona, Spain, 4 Servicio de Neurologı´a, Hospital Universitario Nin˜o Jesu´s, Madrid, Spain Abstract Background: In recent years clinical evidence has emphasized the importance of the mtDNA genetic background that hosts a primary pathogenic mutation in the clinical expression of mitochondrial disorders, but little experimental confirmation has been provided. We have analyzed the pathogenic role of a novel homoplasmic mutation (m.15533 A.G) in the cytochrome b (MT-CYB) gene in a patient presenting with lactic acidosis, seizures, mild mental delay, and behaviour abnormalities. Methodology: Spectrophotometric analyses of the respiratory chain enzyme activities were performed in different tissues, the whole muscle mitochondrial DNA of the patient was sequenced, and the novel mutation was confirmed by PCR-RFLP. Transmitochondrial cybrids were constructed to confirm the pathogenicity of the mutation, and assembly/stability studies were carried out in fibroblasts and cybrids by means of mitochondrial translation inhibition in combination with blue native gel electrophoresis. Principal Findings: Biochemical analyses revealed a decrease in respiratory chain complex III activity in patient’s skeletal muscle, and a combined enzyme defect of complexes III and IV in fibroblasts. -
Datasheet Blank Template
SAN TA C RUZ BI OTEC HNOL OG Y, INC . UQCRC2 (H-135): sc-292924 BACKGROUND RECOMMENDED SECONDARY REAGENTS Cytochrome c is a well characterized, mobile electron transport protein that To ensure optimal results, the following support (secondary) reagents are is essential to energy conversion in all aerobic organisms. Cytochrome b asso - recommended: 1) Western Blotting: use goat anti-rabbit IgG-HRP: sc-2004 ciates with cytochrome c subunit 1 and the Rieske protein to form complex III (dilution range: 1:2000-1:100,000) or Cruz Marker™ compatible goat anti- (also designated cytochrome bc1 complex), which is involved in cellular res - rabbit IgG-HRP: sc-2030 (dilution range: 1:2000-1:5000), Cruz Marker™ piration. Ubiquinol cytochrome c reductase (UQCRFS1), also referred to as Molecular Weight Standards: sc-2035, TBS Blotto A Blocking Reagent: Rieske iron-sulfur protein, represents an important subunit of complex III of sc-2333 and Western Blotting Luminol Reagent: sc-2048. 2) Immunoprecip- the mitochondrial respiratory chain that transfers electrons from ubiquinol to itation: use Protein A/G PLUS-Agarose: sc-2003 (0.5 ml agarose/2.0 ml). cytochrome c. The UQCRFS1 complex is made up of three respiratory sub - 3) Immunofluorescence: use goat anti-rabbit IgG-FITC: sc-2012 (dilution units (cytochrome b, cytochrome c1, Rieske protein), two core proteins, and range: 1:100-1:400) or goat anti-rabbit IgG-TR: sc-2780 (dilution range: six low-molecular weight proteins. Ubiquinol cytochrome-c reductase com plex 1:100-1:400) with UltraCruz™ Mounting Medium: sc-24941. core protein 2 (UQCRC2) represents one of the core proteins of UQCRFS1, and it is required for the assembly of the complex.