Genetics of Familial Non-Medullary Thyroid Carcinoma (FNMTC)
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Nuclear and Mitochondrial Genome Defects in Autisms
UC Irvine UC Irvine Previously Published Works Title Nuclear and mitochondrial genome defects in autisms. Permalink https://escholarship.org/uc/item/8vq3278q Journal Annals of the New York Academy of Sciences, 1151(1) ISSN 0077-8923 Authors Smith, Moyra Spence, M Anne Flodman, Pamela Publication Date 2009 DOI 10.1111/j.1749-6632.2008.03571.x License https://creativecommons.org/licenses/by/4.0/ 4.0 Peer reviewed eScholarship.org Powered by the California Digital Library University of California THE YEAR IN HUMAN AND MEDICAL GENETICS 2009 Nuclear and Mitochondrial Genome Defects in Autisms Moyra Smith, M. Anne Spence, and Pamela Flodman Department of Pediatrics, University of California, Irvine, California In this review we will evaluate evidence that altered gene dosage and structure im- pacts neurodevelopment and neural connectivity through deleterious effects on synap- tic structure and function, and evidence that the latter are key contributors to the risk for autism. We will review information on alterations of structure of mitochondrial DNA and abnormal mitochondrial function in autism and indications that interactions of the nuclear and mitochondrial genomes may play a role in autism pathogenesis. In a final section we will present data derived using Affymetrixtm SNP 6.0 microar- ray analysis of DNA of a number of subjects and parents recruited to our autism spectrum disorders project. We include data on two sets of monozygotic twins. Col- lectively these data provide additional evidence of nuclear and mitochondrial genome imbalance in autism and evidence of specific candidate genes in autism. We present data on dosage changes in genes that map on the X chromosomes and the Y chro- mosome. -
Pulmonary Fibrosis Associated with TINF2 Gene Mutation: Is Somatic Reversion Required?
Pulmonary fibrosis associated with TINF2 gene mutation: is somatic reversion required? To the Editor: We read with great interest the case reported by FUKUHARA et al. [1] of a 43-year-old female patient with dyskeratosis congenita, pulmonary fibrosis and heterozygous mutation in TINF2 (telomerase repeat binding factor 1-interacting nuclear factor 2). TIN2, the TINF2 gene product, TERT (telomere reverse transcriptase) and TERC (telomerase RNA component) participate in the regulation of telomere elongation, in which mutations have been previously found to be associated with familial pulmonary fibrosis in adults [2]. Indeed mutations of SFTPC, coding for surfactant protein C, were initially described in children before being described in adults as old as 72 years of age who presented with familial pulmonary fibrosis [3]. However, we were surprised that a TINF2 mutation could be evidenced in an adult of that age. As highlighted by FUKUHARA et al. [1], patients with the TINF2 mutation present with severe haematological symptoms before 10 years of age [4]. As mentioned by FUKUHARA et al. [1], the identified mutation is probably not hypomorphic because it is a frame-shift deletion located in the mutational ‘‘hot spot’’ described previously. Furthermore, the patient presented with very short telomeres. The TINF2 mutation was probably inherited from her father because he had abnormal skin pigmentation and aplastic anaemia [1]. Re-analysis of the gene mutation sequencing could provide new hypotheses for this late disease onset. Indeed, the electrophoregram depicted in figure 1b in the study by FUKUHARA et al. [1] probably comes from a PCR product sub-cloned into an expression vector [5], and does not ensure that the deletion is at the heterozygous status usually seen in our patients (fig. -
A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated. -
Genetic Influences on Brain Gene Expression in Rats Selected for Tameness and Aggression
Genetic Influences on Brain Gene Expression in Rats Selected for Tameness and Aggression Henrike O. Heyne*,§, Susann Lautenschläger§, Ronald Nelson†, François Besnier†,‡, Maxime Rotival**, Alexander Cagan*, Rimma Kozhemyakina§§, Irina Z. Plyusnina§§, Lyudmila Trut§§, Örjan Carlborg†, Enrico Petretto**, Leonid Kruglyak††,‡‡,***, Svante Pääbo*, Torsten Schöneberg§, Frank W. Albert*,†† * Department of Evolutionary Genetics, Max Planck Institute for Evolutionary Anthropology, Deutscher Platz 6, 04103 Leipzig, Germany § Institute for Biochemistry, University of Leipzig, Medical Faculty, Johannisallee 30, 04103 Leipzig † Swedish University of Agricultural Sciences, Department of Clinical Sciences, Division of Computational Genetics, Mailing address: Box 7078 SE-75007 Uppsala Sweden ‡ Section of Population Genetics and Ecology, Institute of Marine Research, Bergen, Norway, Havforskningsinstituttet, Postboks 1870, Nordnes 5817, Bergen Norway ** MRC Clinical Sciences Centre, Faculty of Medicine, Imperial College London, Du Cane Road, London W12 0NN, UK §§ Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russia †† Department of Human Genetics, University of California, Los Angeles, Gonda Center, 695 Charles E. Young Drive South, Los Angeles, CA 90095, USA ‡‡ Department of Biological Chemistry, University of California, Los Angeles, Gonda Center, 695 Charles E. Young Drive South, Los Angeles, CA 90095, USA *** Howard Hughes Medical Institute, University of California, Los Angeles, Gonda Center, 695 Charles E. Young Drive South, Los Angeles, CA 90095, USA deceased: I.Z.P. Irina Z. Plyusnina . 1 ABSTRACT Inter-individual differences in many behaviors are partly due to genetic differences, but the identification of the genes and variants that influence behavior remains challenging. Here, we studied an F2 intercross of two outbred lines of rats selected for tame and aggressive behavior towards humans for more than 64 generations. -
The Putative Tumor Suppressor Gene GLTSCR2 Induces PTEN-Modulated Cell Death
Cell Death and Differentiation (2007) 14, 1872–1879 & 2007 Nature Publishing Group All rights reserved 1350-9047/07 $30.00 www.nature.com/cdd The putative tumor suppressor gene GLTSCR2 induces PTEN-modulated cell death J-H Yim1,2, Y-J Kim1,2, J-H Ko1,2, Y-E Cho1,2, S-M Kim1,2, J-Y Kim1,2, S Lee1,2 and J-H Park*,1,2 Glioma tumor suppressor candidate region gene 2 (GLTSCR2/PICT-1) is localized within the well-known 1.4-Mb tumor suppressive region of chromosome 19q, which is frequently altered in various human tumors, including diffuse gliomas. Aside from its localization on the chromosome, several lines of evidence, such as PTEN phosphorylation, support that GLTSCR2 partakes in the suppression of tumor growth and development. However, much remains unknown about the molecular mechanisms of the tumor suppressive activity of GLTSCR2. The purpose of this study was to investigate the molecular mechanisms of GLTSCR2 in cell death pathways in association with its binding partner PTEN. In this work, we show that GLTSCR2 is a nucleus-localized protein with a discrete globular expression pattern. In addition to phosphorylating PTEN, GLTSCR2 induces caspase-independent PTEN-modulated apoptotic cell death when overexpressed. However, the cytotoxic activity of GLTSCR2 is independent of its ability to phosphorylate PTEN, suggesting that the GLTSCR2-induced cell death pathway is divergent from PTEN-induced death pathways. Our results suggest that the induction of PTEN-modulated apoptosis is one of the putative mechanisms of tumor suppressive activity -
Thyroid and Parathyroid Glands
HISTOLOGY Endocrine Block – 432 Histology Team Lectures 2 and 3: Thyroid and Parathyroid Glands Done by: Lama Al Tawil Bayan Al Mugheerah Reviewed by: Ammar Alyamani Color Guide: Black: Slides. Red: Important. Green: Doctor’s notes (Female). Blue: Doctor’s notes (Male). Orange: Explanation. Objectives 1. Describe the histological structure of thyroid gland. 2. Identify and correlate between the different endocrine cells in thyroid gland and their functions. 3. Describe the microscopic structure of the parathyroid gland. 4. Describe the functional structure of the parathyroid cells. Mind Map THYROID GLAND STROMA PARENCHYMA Reticlular Follicular Parafollicular Capsule Septa cells cells (C cells) fibers Parathyroid Gland Stroma Parenchyma Reticlular Capsule Septa Chief Cells Oxyphil Cells C.T Thyroid Gland THYROID GLAND STROMA PARENCHYMA OF THYROID GLAND 1- Capsule: THYROID FOLLICLES: Dense irregular collagenous C.T. Are the structural and functional units of the 2- Septa (Interlobular septa): thyroid gland. (Variable in size and spherical in shape). Dense irregular collagenous C.T because L/M: it’s part of the capsule divides the thyroid 1- Simple cuboidal epithelium: into lobules. a- Follicular cells. 3- Reticular fibers: b- Parafollicular cells. (Adjacent to a). Thin C.T., composed mostly of reticular 2- Colloid: central colloid-filled lumen. (Acidophilic without any cells and rich in iodine and fibers with rich capillary plexus thyroglobulin, and so it has the stored hormone & (fenestrated blood capillary) surrounds it’s also the place of iodination). each thyroid follicle. N.B. Each follicle is surrounded by thin basal lamina. Each follicle is single layered. a) FOLLICULAR (PRINCIPAL) CELLS L/M: E/M: - Simple cuboidal cells. -
Produktinformation
Produktinformation Diagnostik & molekulare Diagnostik Laborgeräte & Service Zellkultur & Verbrauchsmaterial Forschungsprodukte & Biochemikalien Weitere Information auf den folgenden Seiten! See the following pages for more information! Lieferung & Zahlungsart Lieferung: frei Haus Bestellung auf Rechnung SZABO-SCANDIC Lieferung: € 10,- HandelsgmbH & Co KG Erstbestellung Vorauskassa Quellenstraße 110, A-1100 Wien T. +43(0)1 489 3961-0 Zuschläge F. +43(0)1 489 3961-7 [email protected] • Mindermengenzuschlag www.szabo-scandic.com • Trockeneiszuschlag • Gefahrgutzuschlag linkedin.com/company/szaboscandic • Expressversand facebook.com/szaboscandic TNKS2 Antibody, HRP conjugated Product Code CSB-PA867136LB01HU Abbreviation Tankyrase-2 Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze. Uniprot No. Q9H2K2 Immunogen Recombinant Human Tankyrase-2 protein (1-246AA) Raised In Rabbit Species Reactivity Human Tested Applications ELISA Relevance Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP- ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing -
ENDOCRINE SYSTEM the Nervous and Endocrine Systems Act Together to Coordinate Functions of All Body Systems
ENDOCRINE SYSTEM The nervous and endocrine systems act together to coordinate functions of all body systems. Recall that the nervous system acts through nerve impulses (action potentials) conducted along axons of neurons. At synapses, nerve impulses trigger the release\ of mediator (messenger) molecules called neurotransmitters The endocrine system also controls body activities by releasing mediators, called hormones, but the means of control of the two systems are very different A hormone (hormon _ to excite or get moving) is a mediator molecule that is released in one part of the body but regulates the activity of cells in other parts of the body. Most hormones enter interstitial fluid and then the bloodstream. The circulating blood delivers hormones to cells throughout the body. Both neurotransmitters and hormones exert their effects by binding to receptors on or in their ―target‖ cells. Several mediators act as both neurotransmitters and hormones. One familiar example is norepinephrine, which is released as a neurotransmitter by sympathetic postganglionic neurons and as a hormone by chromaffin cells of the adrenal medullae. The body contains two kinds of glands: exocrine glands and endocrine glands. Exocrine glands (exo- _ outside) secrete their products into ducts that carry the secretions into body cavities, into the lumen of an organ, or to the outer surface of the body. Exocrine glands include sudoriferous (sweat), sebaceous (oil), mucous, and digestive glands. Endocrine glands (endo- _ within) secrete their products (hormones) into the interstitial fluid surrounding the secretory cells rather than into ducts. From the interstitial fluid, hormones diffuse into blood capillaries and blood carries them to target cells throughout the body. -
The Intellectual Disability Gene PQBP1 Rescues Alzheimer’S Disease
Molecular Psychiatry (2018) 23:2090–2110 https://doi.org/10.1038/s41380-018-0253-8 ARTICLE The intellectual disability gene PQBP1 rescues Alzheimer’s disease pathology 1 1 1 1 1 2 Hikari Tanaka ● Kanoh Kondo ● Xigui Chen ● Hidenori Homma ● Kazuhiko Tagawa ● Aurelian Kerever ● 2 3 3 4 1 1,5 Shigeki Aoki ● Takashi Saito ● Takaomi Saido ● Shin-ichi Muramatsu ● Kyota Fujita ● Hitoshi Okazawa Received: 9 May 2018 / Revised: 9 August 2018 / Accepted: 6 September 2018 / Published online: 3 October 2018 © The Author(s) 2018. This article is published with open access Abstract Early-phase pathologies of Alzheimer’s disease (AD) are attracting much attention after clinical trials of drugs designed to remove beta-amyloid (Aβ) aggregates failed to recover memory and cognitive function in symptomatic AD patients. Here, we show that phosphorylation of serine/arginine repetitive matrix 2 (SRRM2) at Ser1068, which is observed in the brains of early phase AD mouse models and postmortem end-stage AD patients, prevents its nuclear translocation by inhibiting interaction with T-complex protein subunit α. SRRM2 deficiency in neurons destabilized polyglutamine binding protein 1 (PQBP1), a causative gene for intellectual disability (ID), greatly affecting the splicing patterns of synapse-related genes, as 1234567890();,: 1234567890();,: demonstrated in a newly generated PQBP1-conditional knockout model. PQBP1 and SRRM2 were downregulated in cortical neurons of human AD patients and mouse AD models, and the AAV-PQBP1 vector recovered RNA splicing, the synapse phenotype, and the cognitive decline in the two mouse models. Finally, the kinases responsible for the phosphorylation of SRRM2 at Ser1068 were identified as ERK1/2 (MAPK3/1). -
Rat Anti-TERF1 Monoclonal Antibody, Clone 683D (CABT-RM172) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Rat Anti-TERF1 monoclonal antibody, clone 683D (CABT-RM172) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Specificity Specifically detects murine Telomeric repeat-binding factor 1 (TRF1). Target TERF1 Immunogen His-tagged full-length recombinant mouse Telomeric repeat-binding factor 1 (TRF1). Isotype IgG1, κ Source/Host Rat Species Reactivity Mouse Clone 683D Purification Protein G purified Conjugate unconjugated Applications FC, ICC, IF, WB Molecular Weight ~51 kDa observed; 48.22 kDa calculated. Uncharacterized bands may be observed in some lysate(s). Format Liquid Size 100 μg, 25 μg Buffer 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl Preservative 0.05% sodium azide Storage Stable for 1 year at 2-8°C from date of receipt. Warnings Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals. 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 BACKGROUND Introduction Telomeric repeat-binding factor 1 is encoded by the Terf1 gene in murine species. TRF1 is a component of the shelterin complex that is involved in the regulation of telomere length and protection. It binds to telomeric DNA as a homodimer and protects telomeres. -
Structural Genomics Approach to Investigate Deleterious Impact Of
www.nature.com/scientificreports OPEN Structural genomics approach to investigate deleterious impact of nsSNPs in conserved telomere maintenance component 1 Arunabh Choudhury1,5, Taj Mohammad2,5, Nikhil Samarth3, Afzal Hussain4, Md. Tabish Rehman4, Asimul Islam2, Mohamed F. Alajmi4, Shailza Singh3 & Md. Imtaiyaz Hassan2* Conserved telomere maintenance component 1 (CTC1) is an important component of the CST (CTC1-STN1-TEN1) complex, involved in maintaining the stability of telomeric DNA. Several non- synonymous single-nucleotide polymorphisms (nsSNPs) in CTC1 have been reported to cause Coats plus syndrome and Dyskeratosis congenital diseases. Here, we have performed sequence and structure analyses of nsSNPs of CTC1 using state-of-the-art computational methods. The structure- based study focuses on the C-terminal OB-fold region of CTC1. There are 11 pathogenic mutations identifed, and detailed structural analyses were performed. These mutations cause a signifcant disruption of noncovalent interactions, which may be a possible reason for CTC1 instability and consequent diseases. To see the impact of such mutations on the protein conformation, all-atom molecular dynamics (MD) simulations of CTC1-wild-type (WT) and two of the selected mutations, R806C and R806L for 200 ns, were carried out. A signifcant conformational change in the structure of the R806C mutant was observed. This study provides a valuable direction to understand the molecular basis of CTC1 dysfunction in disease progression, including Coats plus syndrome. Unlike prokaryotic chromosomes, eukaryotic chromosomes are linear and are much larger in size. Te ends of the eukaryotic chromosome are composed of a specialized protein-DNA complex called telomeres which maintains the stability of the chromosome ends1. -
The MKKK62-MKK3-MAPK7/14 Module Negatively Regulates Seed
Mao et al. Rice (2019) 12:2 https://doi.org/10.1186/s12284-018-0260-z ORIGINAL ARTICLE Open Access The MKKK62-MKK3-MAPK7/14 module negatively regulates seed dormancy in rice Xingxue Mao1,2†, Jianjun Zhang3†, Wuge Liu1,2†, Shijuan Yan4, Qing Liu1,2, Hua Fu1,2, Junliang Zhao1,2, Wenjie Huang4, Jingfang Dong1,2, Shaohong Zhang1,2, Tifeng Yang1,2, Wu Yang1,2, Bin Liu1,2* and Feng Wang1,2* Abstract Background: Seed dormancy directly affects the phenotype of pre-harvest sprouting, and ultimately affects the quality and yield of rice seeds. Although many genes controlling seed dormancy have been cloned from cereals, the regulatory mechanisms controlling this process are complex, and much remains unknown. The MAPK cascade is involved in many signal transduction pathways. Recently, MKK3 has been reported to be involved in the regulation of seed dormancy, but its mechanism of action is unclear. Results: We found that MKKK62-overexpressing rice lines (OE) lost seed dormancy. Further analyses showed that the abscisic acid (ABA) sensitivity of OE lines was decreased. In yeast two-hybrid experiments, MKKK62 interacted with MKK3, and MKK3 interacted with MAPK7 and MAPK14. Knock-out experiments confirmed that MKK3, MAPK7, and MAPK14 were involved in the regulation of seed dormancy. The OE lines showed decreased transcript levels of OsMFT, a homolog of a gene that controls seed dormancy in wheat. The up-regulation of OsMFT in MKK3-knockout lines (OE/mkk3) and MAPK7/14-knockout lines (OE/mapk7/mapk14) indicated that the MKKK62-MKK3-MAPK7/ MAPK14 system controlled seed dormancy by regulating the transcription of OsMFT.