UC San Francisco Electronic Theses and Dissertations
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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. -
Review Article Molecular Functions of Thyroid Hormones and Their Clinical Significance in Liver-Related Diseases
Hindawi Publishing Corporation BioMed Research International Volume 2013, Article ID 601361, 16 pages http://dx.doi.org/10.1155/2013/601361 Review Article Molecular Functions of Thyroid Hormones and Their Clinical Significance in Liver-Related Diseases Hsiang Cheng Chi,1 Cheng-Yi Chen,1 Ming-Ming Tsai,2 Chung-Ying Tsai,1 and Kwang-Huei Lin1 1 Department of Biochemistry, School of Medicine, Chang-Gung University, Taoyuan 333, Taiwan 2 Department of Nursing, Chang-Gung University of Science and Technology, Taoyuan 333, Taiwan Correspondence should be addressed to Kwang-Huei Lin; [email protected] Received 4 February 2013; Revised 14 May 2013; Accepted 28 May 2013 Academic Editor: Elena Orlova Copyright © 2013 Hsiang Cheng Chi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Thyroid hormones (THs) are potent mediators of several physiological processes, including embryonic development, cellular differentiation, metabolism, and cell growth. Triiodothyronine3 (T ) is the most biologically active TH form. Thyroid hormone receptors (TRs) belong to the nuclear receptor superfamily and mediate the biological functions of T3 via transcriptional regulation. TRs generally form heterodimers with the retinoid X receptor (RXR) and regulate target genes upon T3 stimulation. Research over the past few decades has revealed that disruption of cellular TH signaling triggers chronic liver diseases, including alcoholic or nonalcoholic fatty liver disease and hepatocellular carcinoma (HCC). Animal model experiments and epidemiologic studies to date imply close associations between high TH levels and prevention of liver disease. -
Molecular Functions of Thyroid Hormones and Their Clinical Significance in Liver-Related Diseases
Hindawi Publishing Corporation BioMed Research International Volume 2013, Article ID 601361, 16 pages http://dx.doi.org/10.1155/2013/601361 Review Article Molecular Functions of Thyroid Hormones and Their Clinical Significance in Liver-Related Diseases Hsiang Cheng Chi,1 Cheng-Yi Chen,1 Ming-Ming Tsai,2 Chung-Ying Tsai,1 and Kwang-Huei Lin1 1 Department of Biochemistry, School of Medicine, Chang-Gung University, Taoyuan 333, Taiwan 2 Department of Nursing, Chang-Gung University of Science and Technology, Taoyuan 333, Taiwan Correspondence should be addressed to Kwang-Huei Lin; [email protected] Received 4 February 2013; Revised 14 May 2013; Accepted 28 May 2013 Academic Editor: Elena Orlova Copyright © 2013 Hsiang Cheng Chi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Thyroid hormones (THs) are potent mediators of several physiological processes, including embryonic development, cellular differentiation, metabolism, and cell growth. Triiodothyronine3 (T ) is the most biologically active TH form. Thyroid hormone receptors (TRs) belong to the nuclear receptor superfamily and mediate the biological functions of T3 via transcriptional regulation. TRs generally form heterodimers with the retinoid X receptor (RXR) and regulate target genes upon T3 stimulation. Research over the past few decades has revealed that disruption of cellular TH signaling triggers chronic liver diseases, including alcoholic or nonalcoholic fatty liver disease and hepatocellular carcinoma (HCC). Animal model experiments and epidemiologic studies to date imply close associations between high TH levels and prevention of liver disease. -
Development and Validation of a Protein-Based Risk Score for Cardiovascular Outcomes Among Patients with Stable Coronary Heart Disease
Supplementary Online Content Ganz P, Heidecker B, Hveem K, et al. Development and validation of a protein-based risk score for cardiovascular outcomes among patients with stable coronary heart disease. JAMA. doi: 10.1001/jama.2016.5951 eTable 1. List of 1130 Proteins Measured by Somalogic’s Modified Aptamer-Based Proteomic Assay eTable 2. Coefficients for Weibull Recalibration Model Applied to 9-Protein Model eFigure 1. Median Protein Levels in Derivation and Validation Cohort eTable 3. Coefficients for the Recalibration Model Applied to Refit Framingham eFigure 2. Calibration Plots for the Refit Framingham Model eTable 4. List of 200 Proteins Associated With the Risk of MI, Stroke, Heart Failure, and Death eFigure 3. Hazard Ratios of Lasso Selected Proteins for Primary End Point of MI, Stroke, Heart Failure, and Death eFigure 4. 9-Protein Prognostic Model Hazard Ratios Adjusted for Framingham Variables eFigure 5. 9-Protein Risk Scores by Event Type This supplementary material has been provided by the authors to give readers additional information about their work. Downloaded From: https://jamanetwork.com/ on 10/02/2021 Supplemental Material Table of Contents 1 Study Design and Data Processing ......................................................................................................... 3 2 Table of 1130 Proteins Measured .......................................................................................................... 4 3 Variable Selection and Statistical Modeling ........................................................................................ -
Human Tryptase Γ‑1/TPSG1 Antibody Antigen Affinity-Purified Polyclonal Goat Igg Catalog Number: AF1667
Human Tryptase γ‑1/TPSG1 Antibody Antigen Affinity-purified Polyclonal Goat IgG Catalog Number: AF1667 DESCRIPTION Species Reactivity Human Specificity Detects human Tryptase γ-1/TPSG1 in direct ELISAs and Western blots. Source Polyclonal Goat IgG Purification Antigen Affinity-purified Immunogen Mouse myeloma cell line NS0-derived recombinant human Tryptase γ‑1/TPSG1 Arg20-Arg281 Accession # Q9NRR2 Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. See Certificate of Analysis for details. *Small pack size (-SP) is supplied either lyophilized or as a 0.2 μm filtered solution in PBS. APPLICATIONS Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website. Recommended Sample Concentration Western Blot 0.1 µg/mL Recombinant Human Tryptase γ‑1/TPSG1 (Catalog # 1667-SE) Immunoprecipitation 25 µg/mL Conditioned cell culture medium spiked with Recombinant Human Tryptase γ‑1/TPSG1 (Catalog # 1667-SE), see our available Western blot detection antibodies PREPARATION AND STORAGE Reconstitution Reconstitute at 0.2 mg/mL in sterile PBS. Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (-SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 6 months, -20 to -70 °C under sterile conditions after reconstitution. -
Human Kallikrein 5 Quantikine
Quantikine® ELISA Human Kallikrein 5 Immunoassay Catalog Number DKK500 For the quantitative determination of human Kallikrein 5 (KLK5) concentrations in cell culture supernates, serum, plasma, saliva, and human milk. This package insert must be read in its entirety before using this product. For research use only. Not for use in diagnostic procedures. TABLE OF CONTENTS SECTION PAGE INTRODUCTION .....................................................................................................................................................................1 PRINCIPLE OF THE ASSAY ...................................................................................................................................................2 LIMITATIONS OF THE PROCEDURE .................................................................................................................................2 TECHNICAL HINTS .................................................................................................................................................................2 MATERIALS PROVIDED & STORAGE CONDITIONS ...................................................................................................3 OTHER SUPPLIES REQUIRED .............................................................................................................................................3 PRECAUTIONS .........................................................................................................................................................................4 -
The Emerging Role of Mast Cell Proteases in Asthma
REVIEW ASTHMA The emerging role of mast cell proteases in asthma Gunnar Pejler1,2 Affiliations: 1Dept of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden. 2Dept of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden. Correspondence: Gunnar Pejler, Dept of Medical Biochemistry and Microbiology, BMC, Uppsala University, Box 582, 75123 Uppsala, Sweden. E-mail: [email protected] @ERSpublications Mast cells express large amounts of proteases, including tryptase, chymase and carboxypeptidase A3. An extensive review of how these proteases impact on asthma shows that they can have both protective and detrimental functions. http://bit.ly/2Gu1Qp2 Cite this article as: Pejler G. The emerging role of mast cell proteases in asthma. Eur Respir J 2019; 54: 1900685 [https://doi.org/10.1183/13993003.00685-2019]. ABSTRACT It is now well established that mast cells (MCs) play a crucial role in asthma. This is supported by multiple lines of evidence, including both clinical studies and studies on MC-deficient mice. However, there is still only limited knowledge of the exact effector mechanism(s) by which MCs influence asthma pathology. MCs contain large amounts of secretory granules, which are filled with a variety of bioactive compounds including histamine, cytokines, lysosomal hydrolases, serglycin proteoglycans and a number of MC-restricted proteases. When MCs are activated, e.g. in response to IgE receptor cross- linking, the contents of their granules are released to the exterior and can cause a massive inflammatory reaction. The MC-restricted proteases include tryptases, chymases and carboxypeptidase A3, and these are expressed and stored at remarkably high levels. -
TPSG1 Polyclonal Antibody
PRODUCT DATA SHEET Bioworld Technology,Inc. TPSG1 polyclonal antibody Catalog: BS61326 Host: Rabbit Reactivity: Human,Mouse,Rat BackGround: by affinity-chromatography using epitope-specific im- Tryptases comprise a family of trypsin-like serine prote- munogen and the purity is > 95% (by SDS-PAGE). ases, the peptidase family S1. Tryptases are enzymatically Applications: active only as heparin-stabilized tetramers, and they are WB: 1:500~1:1000 resistant to all known endogenous proteinase inhibitors. Storage&Stability: Several tryptase genes are clustered on chromosome Store at 4°C short term. Aliquot and store at -25°C long 16p13.3. There is uncertainty regarding the number of term. Avoid freeze-thaw cycles. genes in this cluster. Currently four functional genes - al- Specificity: pha I, beta I, beta II and gamma I - have been identified. TPSG1 polyclonal antibody detects endogenous levels of And beta I has an allelic variant named alpha II, beta II TPSG1 protein. has an allelic variant beta III, also gamma I has an allelic DATA: variant gamma II. Beta tryptases appear to be the main isoenzymes expressed in mast cells; whereas in basophils, alpha-tryptases predominant. This gene differs from other members of the tryptase gene family in that it has C-terminal hydrophobic domain, which may serve as a membrane anchor. Tryptases have been implicated as me- diators in the pathogenesis of asthma and other allergic and inflammatory disorders. Western blot (WB) analysis of TPSG1 polyclonal antibody at 1:500 di- Product: lution Lane1:HEK293T whole cell lysate Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, Lane2:RAW264.7 whole cell lysate Lane3:PC12 whole cell lysate 50% glycerol, pH7.2 Note: Molecular Weight: For research use only, not for use in diagnostic procedure. -
The Study of TMPRSS-ERG Gene Fusion in Prostate Cancer in Pakistan
CAPITAL UNIVERSITY OF SCIENCE AND TECHNOLOGY, ISLAMABAD The Study of TMPRSS-ERG Gene Fusion in Prostate Cancer in Pakistan by Samra Manzoor A thesis submitted in partial fulfillment for the degree of Master of Science in the Faculty of Health and Life Sciences Department of Biosciences 2018 i Copyright c 2018 by Samra Manzoor All rights reserved. No part of this thesis may be reproduced, distributed, or transmitted in any form or by any means, including photocopying, recording, or other electronic or mechanical methods, by any information storage and retrieval system without the prior written permission of the author. ii This thesis is dedicated to my husband Atif Mansoor Khan and my brother Naeem Ahmad who's support, encouragement, and constant love have sustained me throughout my life. I would like to dedicate this thesis to my best friend, Anila Sajjad and my kids (Shanzay and Aniq). Thank you for always believing in me, even when I did not, and cheering me on until the end. Words cannot express how much I love you all and appreciate everything you all have done for me. CAPITAL UNIVERSITY OF SCIENCE & TECHNOLOGY ISLAMABAD CERTIFICATE OF APPROVAL The Study of TMPRSS-ERG Gene Fusion in Prostate Cancer in Pakistan by Samra Manzoor MBS 163004 THESIS EXAMINING COMMITTEE S. No. Examiner Name Organization (a) External Examiner Dr. Maria Shabbir NUST, Islamabad (b) Internal Examiner Dr. Shaukat Iqbal Malik CUST, Islamabad (c) Supervisor Dr. Sahar Fazal CUST, Islamabad Dr. Sahar Fazal Thesis Supervisor October, 2018 Dr. Sahar Fazal Dr. Muhammad Abdul Qadir Head Dean Dept. of Biosciences Faculty of Health and Life Sciences October, 2018 October, 2018 iv Author's Declaration I, Samra Manzoor hereby state that my MS thesis titled \The Study of TMPRSS-ERG Gene Fusion in Prostate Cancer in Pakistan" is my own work and has not been submitted previously by me for taking any degree from Capital University of Science and Technology, Islamabad or anywhere else in the country/abroad. -
A Genomic Analysis of Rat Proteases and Protease Inhibitors
A genomic analysis of rat proteases and protease inhibitors Xose S. Puente and Carlos López-Otín Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Instituto Universitario de Oncología, Universidad de Oviedo, 33006-Oviedo, Spain Send correspondence to: Carlos López-Otín Departamento de Bioquímica y Biología Molecular Facultad de Medicina, Universidad de Oviedo 33006 Oviedo-SPAIN Tel. 34-985-104201; Fax: 34-985-103564 E-mail: [email protected] Proteases perform fundamental roles in multiple biological processes and are associated with a growing number of pathological conditions that involve abnormal or deficient functions of these enzymes. The availability of the rat genome sequence has opened the possibility to perform a global analysis of the complete protease repertoire or degradome of this model organism. The rat degradome consists of at least 626 proteases and homologs, which are distributed into five catalytic classes: 24 aspartic, 160 cysteine, 192 metallo, 221 serine, and 29 threonine proteases. Overall, this distribution is similar to that of the mouse degradome, but significatively more complex than that corresponding to the human degradome composed of 561 proteases and homologs. This increased complexity of the rat protease complement mainly derives from the expansion of several gene families including placental cathepsins, testases, kallikreins and hematopoietic serine proteases, involved in reproductive or immunological functions. These protease families have also evolved differently in the rat and mouse genomes and may contribute to explain some functional differences between these two closely related species. Likewise, genomic analysis of rat protease inhibitors has shown some differences with the mouse protease inhibitor complement and the marked expansion of families of cysteine and serine protease inhibitors in rat and mouse with respect to human. -
TPSG1 Mouse Monoclonal Antibody [Clone ID: OTI2A10] Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for CF504128 TPSG1 Mouse Monoclonal Antibody [Clone ID: OTI2A10] Product data: Product Type: Primary Antibodies Clone Name: OTI2A10 Applications: FC, IF, WB Recommended Dilution: WB 1:2000, IF 1:100, FLOW 1:100 Reactivity: Human Host: Mouse Isotype: IgG1 Clonality: Monoclonal Immunogen: Human recombinant protein fragment corresponding to amino acids 20-283 of human TPSG1(NP_036599) produced in E.coli. Formulation: Lyophilized powder (original buffer 1X PBS, pH 7.3, 8% trehalose) Reconstitution Method: For reconstitution, we recommend adding 100uL distilled water to a final antibody concentration of about 1 mg/mL. To use this carrier-free antibody for conjugation experiment, we strongly recommend performing another round of desalting process. (OriGene recommends Zeba Spin Desalting Columns, 7KMWCO from Thermo Scientific) Purification: Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G) Conjugation: Unconjugated Storage: Store at -20°C as received. Stability: Stable for 12 months from date of receipt. Predicted Protein Size: 32 kDa Gene Name: Homo sapiens tryptase gamma 1 (TPSG1), mRNA. Database Link: NP_036599 Entrez Gene 25823 Human Q9NRR2 This product is to be used for laboratory only. Not for diagnostic or therapeutic use. View online » ©2021 OriGene Technologies, Inc., 9620 Medical Center Drive, Ste 200, Rockville, MD 20850, US 1 / 3 TPSG1 Mouse Monoclonal Antibody [Clone ID: OTI2A10] – CF504128 Background: Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1. -
Hereditary Alpha Tryptasemia, Mastocytosis and Beyond
International Journal of Molecular Sciences Review Genetic Regulation of Tryptase Production and Clinical Impact: Hereditary Alpha Tryptasemia, Mastocytosis and Beyond Bettina Sprinzl 1,2, Georg Greiner 3,4,5 , Goekhan Uyanik 1,2,6, Michel Arock 7,8 , Torsten Haferlach 9, Wolfgang R. Sperr 4,10, Peter Valent 4,10 and Gregor Hoermann 4,9,* 1 Ludwig Boltzmann Institute for Hematology and Oncology at the Hanusch Hospital, Center for Medical Genetics, Hanusch Hospital, 1140 Vienna, Austria; [email protected] (B.S.); [email protected] (G.U.) 2 Center for Medical Genetics, Hanusch Hospital, 1140 Vienna, Austria 3 Department of Laboratory Medicine, Medical University of Vienna, 1090 Vienna, Austria; [email protected] 4 Ludwig Boltzmann Institute for Hematology and Oncology, Medical University of Vienna, 1090 Vienna, Austria; [email protected] (W.R.S.); [email protected] (P.V.) 5 Ihr Labor, Medical Diagnostic Laboratories, 1220 Vienna, Austria 6 Medical School, Sigmund Freud Private University, 1020 Vienna, Austria 7 Department of Hematology, APHP, Pitié-Salpêtrière-Charles Foix University Hospital and Sorbonne University, 75013 Paris, France; [email protected] 8 Centre de Recherche des Cordeliers, INSERM, Sorbonne University, Cell Death and Drug Resistance in Hematological Disorders Team, 75006 Paris, France 9 MLL Munich Leukemia Laboratory, 81377 Munich, Germany; [email protected] 10 Department of Internal Medicine I, Division of Hematology and Hemostaseology, Medical University of Vienna, 1090 Vienna, Austria * Correspondence: [email protected]; Tel.: +49-89-99017-315 Citation: Sprinzl, B.; Greiner, G.; Uyanik, G.; Arock, M.; Haferlach, T.; Abstract: Tryptase is a serine protease that is predominantly produced by tissue mast cells (MCs) and Sperr, W.R.; Valent, P.; Hoermann, G.