Curriculum Vitae Kathleen A. Trychta Program in Toxicology University Of

Total Page:16

File Type:pdf, Size:1020Kb

Curriculum Vitae Kathleen A. Trychta Program in Toxicology University Of Depletion of endoplasmic reticulum calcium triggers the loss of ER resident proteins Item Type dissertation Authors Trychta, Kathleen Anne Publication Date 2019 Abstract The endoplasmic reticulum (ER) contains proteins that carry out the diverse functions of the ER including calcium storage, protein folding, modification, and trafficking, lipid metabolism, and drug detoxification. When soluble ER resident proteins wi... Keywords Cellular biology; Molecular biology; Neurosciences; ER retention sequence; KDEL receptor; oxygen-glucose deprivation; Calcium; Endoplasmic Reticulum; Ischemia Download date 10/10/2021 05:06:38 Link to Item http://hdl.handle.net/10713/11613 Curriculum Vitae Kathleen A. Trychta Program in Toxicology University of Maryland, Baltimore Date: July 2019 Contact Information: [email protected] EDUCATION University of Maryland, Baltimore, MD August 2016-Present • Graduate Program • Molecular and Mechanistic Toxicology Colgate University, Hamilton, NY May 2013 • Bachelor of Arts (with honors) • Major: Cellular Neuroscience • Minor: Biology RESEARCH EXPERIENCE National Institutes of Health, Baltimore, MD August 2016-Present National Institute on Drug Abuse Pre-Doctoral Fellow (Dr. Brandon Harvey) • Study the departure of endoplasmic reticulum (ER) resident proteins from the ER in response to pathological conditions and propose a novel pathophysiological phenomenon defined as “ER exodosis” • Develop an assay to longitudinally monitor ER calcium depletion in vitro and in vivo using the specificity of an endogenous esterase for a fluorescein diester substrate • Examine the role of KDEL receptors and ligands in the ER protein retrieval pathway National Institutes of Health, Baltimore, MD 2013-2016 National Institute on Drug Abuse Post-Baccalaureate Fellow (Dr. Brandon Harvey, Dr. Mark Henderson) • Studied ER stress-induced protein secretion and approaches to monitor and manipulate the ER environment • Developed a library of ninety-nine different Gaussia luciferase luminescent-based reporters based off of ER resident proteins that can be used to monitor the dynamic nature of the endoplasmic reticulum proteome • Examined the differential stability of three KDEL receptor isoforms in cell lines • Performed in vivo studies focusing on ER calcium alterations in the hepatocytes of rats in a high fat diet model of obesity and ethanol vapor model of alcohol addiction Colgate University Neuroscience Department, Hamilton, NY 2012-2013 Student Researcher (Dr. Deborah Kreiss) • Investigated the suitability of two potential rat models of obsessive-compulsive disorder (OCD), one involving acute drug administration and the other examining chronic neonatal drug exposure • Assessed the predictive validity of established behavioral tests and examined a less thoroughly researched behavioral test for OCD • Prepared and coded drug solutions for researcher blind injections Massachusetts General Hospital, Boston, MA Summer 2011, 2012 Research Assistant, Partners Orthopaedic Trauma • Assembled data regarding the treatment of geriatric hip fractures over a one-year period to serve as a baseline of comparison for the newly established Geriatric Inpatient Fracture Service (GiFTS) program • Presented to a cross-hospital research team on a proposed new classification system for open bone fractures • Analyzed radiology reports, patient charts, and operative notes for retrospective research studies and identified patients for prospective studies TEACHING EXPERIENCE High School Student Mentor, Baltimore, MD 2014-2016 National Institute on Drug Abuse • Design and guide the research experiments of high school students working on their senior projects • Attend the Aberdeen Science and Math Academy's presentation of senior capstone project proposals as a panel expert to provide constructive feedback and assist students in refining their projects and developing an impactful research plan PROFESSIONAL ACTIVITIES • Co ad-hoc reviewer for PLOS One • Society for Neuroscience Member • American Society of Neural Therapy and Repair Member • American Society for Cell Biology Member HONORS AND AWARDS • American-Scandinavian Foundation Grant, 2018 • National Institute on Drug Abuse Graduate Student Incentive Program Award, 2017-2019 • Pre-Doctoral Intramural Research Training Award (IRTA), 2016-2018 • Outstanding Poster Award, NIH Post-Baccalaureate Poster Day 2014 • Post-Baccalaureate Intramural Research Training Award (IRTA), 2013-2015 • Beta Beta Beta, National Biological Honor Society • Colgate University Dean’s Award for Academic Excellence • Spring 2010-2013 Recipient of Michael S. '73 and Linda A. Walsh Endowed Scholarship for Physical Sciences PUBLICATIONS Trychta KA*, Bäck S*, Henderson MJ, Harvey BK. “KDEL receptors are differentially regulated to maintain the ER proteome under calcium deficiency.” Cell Reports 25(7): P1829-1840. 2018 Nov. 13. Trychta KA, Heathward EJ, Sulima A, Bäck S, Farokhnia M, Richie CT, Leggio L, Rice KC, Harvey BK. “Extracellular esterase activity as an indicator of endoplasmic reticulum calcium depletion.” Biomarkers DOI 10.1080/1254705X.2018.1490968. 2018 Aug. 10. Wires ES*, Trychta KA*, Bäck S, Sulima A, Rice KC, Harvey BK. “High fat diet disrupts ER calcium homeostasis in rat liver based on SERCaMP reporter assay.” Journal of Hepatology 67(5): 1009-1017. 2017 July 17. Wires ES, Henderson MJ, Yan X, Back S, Trychta KA, Lutrey MH, Harvey BK. “Longitudinal monitoring of Gaussia and Nano luciferase activities to concurrently assess ER calcium homeostasis and ER stress in vivo.” PLOS ONE 12(4): e0175481. 2017 April 12. Henderson MJ, Simons Wires EM, Trychta KA, Yan X, Harvey BK. “Monitoring endoplasmic reticulum calcium homeostasis using a Gaussia luciferase SERCaMP.” Journal of Visualized Experiments 103 (e53199). 2015 Sept. 6. Henderson MJ, Simons Wires EM, Trychta KA, Richie CT, Harvey BK. “SERCaMP: a carboxy-terminal protein modification that enables monitoring of ER calcium homeostasis.” Molecular Biology of the Cell 25(18): 2828-2839. 2014 Sept. 15. POSTERS Kathleen Trychta, Lowella Fortuno, Brandon Harvey (2019). “Hyperthermia promotes secretion of ER luminal proteins.” Gordon Research Conference: Stress Proteins in Growth, Development, and Disease, Lucca, Italy. Kathleen Trychta, Susanne Bäck, Mark Henderson, Brandon Harvey (2018). “Loss of ER resident proteins in response to calcium depletion is counteracted by KDEL receptor upregulation.” The American Society for Cell Biology, San Diego, CA. Kathleen Trychta, Xiaokang Yan, Jenni Anttila, Mikko Airavaara, Kou-Jen Wu, Yun Wang, Mark Henderson, Brandon Harvey (2018). “Monitoring ER calcium and ER proteostasis under hypoxic conditions.” International Symposium on Neuroprotection and Neurorepair, Dresden, Germany. Kathleen Trychta, Emily Heathward, Agnieszka Sulima, Susanne Bäck, Medhi Farokhnia, Christopher Richie, Lorenzo Leggio, Kenner Rice, Brandon Harvey (2018). “Extracellular esterase activity as an indicator of endoplasmic reticulum calcium depletion.” Gordon Research Conference: Protein Processing, Trafficking, and Secretion, New London, NH. Kathleen Trychta, Jenni Anttila, Mikko Airavaara, Kou-Jen Wu, Yun Wang, Mark Henderson, Brandon Harvey (2017). “Monitoring ER calcium and ER proteostasis under hypoxic conditions.” Gordon Research Conference: Stress Proteins in Growth, Development, and Disease, Newry, ME. Kathleen Trychta, Xiaokang Yan, Jenni Anttila, Mikko Airavaara, Kou-Jen Wu, Yun Wang, Mark Henderson, Brandon Harvey (2017). “Monitoring ER calcium and ER proteostasis under hypoxic conditions.” The American Society for Neural Therapy and Repair, Clearwater Beach, FL. Kathleen Trychta, Emily Simons Wires, Christopher Richie, Brandon Harvey, Mark Henderson (2014). “SERCaMP: A reporter to monitor endoplasmic reticulum calcium homeostasis in neurons.” Society for Neuroscience, Washington, DC. Kathleen Trychta, Rayshard Rogers, Mark Henderson, Brandon Harvey (2014). “Examining differences between the KDEL receptor isoforms and their roles in the ER retrieval process.” NIH Post-Baccalaureate Poster Day, Bethesda, MD. ABSTRACT Title of Dissertation: Depletion of endoplasmic reticulum calcium triggers the loss of ER resident proteins Kathleen A. Trychta, Doctor of Philosophy, 2019 Dissertation Directed by: Dr. Brandon Harvey, Ph.D. Unit Chief, Molecular Mechanisms of Cellular Stress and Inflammation, National Institute on Drug Abuse The endoplasmic reticulum (ER) contains proteins that carry out the diverse functions of the ER including calcium storage, protein folding, modification, and trafficking, lipid metabolism, and drug detoxification. When soluble ER resident proteins with an ER retention sequence (ERS) depart from the ER they interact with KDEL receptors in the Golgi membrane and are retrogradely transported to the ER lumen via the KDEL receptor retrieval pathway. ER calcium depletion disrupts this process resulting in the mass departure of ERS-containing proteins into the extracellular space. Such a loss of ER resident proteins has two potential consequences to an affected cell. First, there is a loss of proteins involved in the aforementioned critical ER functions. Second, the relocation of such proteins and their associated functions outside of the cell may cause changes in the extracellular environment. This dissertation describes the identification and characterization of a phenomenon whereby ER resident protein secretion is triggered by pathophysiological ER calcium depletion. By exploiting the enzymatic activity of one of the identified
Recommended publications
  • Product Name: C9orf78 Polyclonal Antibody, ALEXA FLUOR® 647 Conjugated Catalog No
    Product Name: C9orf78 Polyclonal Antibody, ALEXA FLUOR® 647 Conjugated Catalog No. : TAP01-84658R-A647 Intended Use: For Research Use Only. Not for used in diagnostic procedures. Size 100ul Concentration 1ug/ul Gene ID 51759 ISO Type Rabbit IgG Clone N/A Immunogen Range Conjugation ALEXA FLUOR® 647 Subcellular Locations Applications IF(IHC-P) Cross Reactive Species Human, Mouse, Rat Source KLH conjugated synthetic peptide derived from human C9orf78 Applications with IF(IHC-P)(1:50-200) Dilutions Purification Purified by Protein A. Background Chromosome 9 consists of about 145 million bases and 4% of the human genome and encodes nearly 900 genes. Considered to play a role in gender determination, deletion of the distal portion of 9p can lead to development of male to female sex reversal, the phenotype of a female with a male X,Y genotype. Hereditary hemorrhagic telangiectasia, which is characterized by harmful vascular defects, is associated with the chromosome 9 gene encoding endoglin protein, ENG. Familial dysautonomia is also associated with chromosome 9 though through the gene IKBKAP. Notably, chromosome 9 encompasses the largest interferon family gene cluster. Chromosome 9 is partnered with chromosome 22 in the translocation leading to the aberrant production of BCR-ABL fusion protein often found in leukemias. The C9orf78 gene product has been provisionally designated C9orf78 pending further characterization. Synonyms bA409K20.3; C9orf78; Chromosome 9 open reading frame 78; CI078_HUMAN; HCA59; Hepatocellular carcinoma associated antigen 59; Hepatocellular carcinoma-associated antigen 59; HSPC220; Uncharacterized protein C9orf78. Storage Aqueous buffered solution containing 1% BSA, 50% glycerol and 0.09% sodium azide. Store at 4°C for 12 months.
    [Show full text]
  • 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.
    [Show full text]
  • Epigenome-Wide Exploratory Study of Monozygotic Twins Suggests Differentially Methylated Regions to Associate with Hand Grip Strength
    Biogerontology (2019) 20:627–647 https://doi.org/10.1007/s10522-019-09818-1 (0123456789().,-volV)( 0123456789().,-volV) RESEARCH ARTICLE Epigenome-wide exploratory study of monozygotic twins suggests differentially methylated regions to associate with hand grip strength Mette Soerensen . Weilong Li . Birgit Debrabant . Marianne Nygaard . Jonas Mengel-From . Morten Frost . Kaare Christensen . Lene Christiansen . Qihua Tan Received: 15 April 2019 / Accepted: 24 June 2019 / Published online: 28 June 2019 Ó The Author(s) 2019 Abstract Hand grip strength is a measure of mus- significant CpG sites or pathways were found, how- cular strength and is used to study age-related loss of ever two of the suggestive top CpG sites were mapped physical capacity. In order to explore the biological to the COL6A1 and CACNA1B genes, known to be mechanisms that influence hand grip strength varia- related to muscular dysfunction. By investigating tion, an epigenome-wide association study (EWAS) of genomic regions using the comb-p algorithm, several hand grip strength in 672 middle-aged and elderly differentially methylated regions in regulatory monozygotic twins (age 55–90 years) was performed, domains were identified as significantly associated to using both individual and twin pair level analyses, the hand grip strength, and pathway analyses of these latter controlling the influence of genetic variation. regions revealed significant pathways related to the Moreover, as measurements of hand grip strength immune system, autoimmune disorders, including performed over 8 years were available in the elderly diabetes type 1 and viral myocarditis, as well as twins (age 73–90 at intake), a longitudinal EWAS was negative regulation of cell differentiation.
    [Show full text]
  • Supplementary Table 1: Adhesion Genes Data Set
    Supplementary Table 1: Adhesion genes data set PROBE Entrez Gene ID Celera Gene ID Gene_Symbol Gene_Name 160832 1 hCG201364.3 A1BG alpha-1-B glycoprotein 223658 1 hCG201364.3 A1BG alpha-1-B glycoprotein 212988 102 hCG40040.3 ADAM10 ADAM metallopeptidase domain 10 133411 4185 hCG28232.2 ADAM11 ADAM metallopeptidase domain 11 110695 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 195222 8038 hCG40937.4 ADAM12 ADAM metallopeptidase domain 12 (meltrin alpha) 165344 8751 hCG20021.3 ADAM15 ADAM metallopeptidase domain 15 (metargidin) 189065 6868 null ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme) 108119 8728 hCG15398.4 ADAM19 ADAM metallopeptidase domain 19 (meltrin beta) 117763 8748 hCG20675.3 ADAM20 ADAM metallopeptidase domain 20 126448 8747 hCG1785634.2 ADAM21 ADAM metallopeptidase domain 21 208981 8747 hCG1785634.2|hCG2042897 ADAM21 ADAM metallopeptidase domain 21 180903 53616 hCG17212.4 ADAM22 ADAM metallopeptidase domain 22 177272 8745 hCG1811623.1 ADAM23 ADAM metallopeptidase domain 23 102384 10863 hCG1818505.1 ADAM28 ADAM metallopeptidase domain 28 119968 11086 hCG1786734.2 ADAM29 ADAM metallopeptidase domain 29 205542 11085 hCG1997196.1 ADAM30 ADAM metallopeptidase domain 30 148417 80332 hCG39255.4 ADAM33 ADAM metallopeptidase domain 33 140492 8756 hCG1789002.2 ADAM7 ADAM metallopeptidase domain 7 122603 101 hCG1816947.1 ADAM8 ADAM metallopeptidase domain 8 183965 8754 hCG1996391 ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma) 129974 27299 hCG15447.3 ADAMDEC1 ADAM-like,
    [Show full text]
  • Uptake and Processing of the Cytolethal Distending Toxin by Mammalian Cells
    Toxins 2014, 6, 3098-3116; doi:10.3390/toxins6113098 OPEN ACCESS toxins ISSN 2072-6651 www.mdpi.com/journal/toxins Review Uptake and Processing of the Cytolethal Distending Toxin by Mammalian Cells Joseph M. DiRienzo Department of Microbiology, School of Dental Medicine, University of Pennsylvania, 240 South 40th Street, Philadelphia, PA 19104, USA; E-Mail: [email protected]; Tel.: +1-215-898-8238; Fax: +1-215-898-8385 External Editor: Holger Barth Received: 19 September 2014; in revised form: 10 October 2014 / Accepted: 10 October 2014 / Published: 31 October 2014 Abstract: The cytolethal distending toxin (Cdt) is a heterotrimeric holotoxin produced by a diverse group of Gram-negative pathogenic bacteria. The Cdts expressed by the members of this group comprise a subclass of the AB toxin superfamily. Some AB toxins have hijacked the retrograde transport pathway, carried out by the Golgi apparatus and endoplasmic reticulum (ER), to translocate to cytosolic targets. Those toxins have been used as tools to decipher the roles of the Golgi and ER in intracellular transport and to develop medically useful delivery reagents. In comparison to the other AB toxins, the Cdt exhibits unique properties, such as translocation to the nucleus, that present specific challenges in understanding the precise molecular details of the trafficking pathway in mammalian cells. The purpose of this review is to present current information about the mechanisms of uptake and translocation of the Cdt in relation to standard concepts of endocytosis and retrograde transport. Studies of the Cdt intoxication process to date have led to the discovery of new translocation pathways and components and most likely will continue to reveal unknown features about the mechanisms by which bacterial proteins target the mammalian cell nucleus.
    [Show full text]
  • ALG12 Gene Pair Kentaro Oh-Hashi1*, Hisashi Koga2, Shun Ikeda2, Kiyo Shimada2, Yoko Hirata1, Kazutoshi Kiuchi1
    Oh-hashi et al. BMC Genomics 2010, 11:664 http://www.biomedcentral.com/1471-2164/11/664 RESEARCH ARTICLE Open Access Role of an ER stress response element in regulating the bidirectional promoter of the mouse CRELD2 - ALG12 gene pair Kentaro Oh-hashi1*, Hisashi Koga2, Shun Ikeda2, Kiyo Shimada2, Yoko Hirata1, Kazutoshi Kiuchi1 Abstract Background: Recently, we identified cysteine-rich with EGF-like domains 2 (CRELD2) as a novel endoplasmic reticulum (ER) stress-inducible gene and characterized its transcriptional regulation by ATF6 under ER stress conditions. Interestingly, the CRELD2 and asparagine-linked glycosylation 12 homolog (ALG12) genes are arranged as a bidirectional (head-to-head) gene pair and are separated by less than 400 bp. In this study, we characterized the transcriptional regulation of the mouse CRELD2 and ALG12 genes that is mediated by a common bidirectional promoter. Results: This short intergenic region contains an ER stress response element (ERSE) sequence and is well conserved among the human, rat and mouse genomes. Microarray analysis revealed that CRELD2 and ALG12 mRNAs were induced in Neuro2a cells by treatment with thapsigargin (Tg), an ER stress inducer, in a time- dependent manner. Other ER stress inducers, tunicamycin and brefeldin A, also increased the expression of these two mRNAs in Neuro2a cells. We then tested for the possible involvement of the ERSE motif and other regulatory sites of the intergenic region in the transcriptional regulation of the mouse CRELD2 and ALG12 genes by using variants of the bidirectional reporter construct. With regards to the promoter activities of the CRELD2-ALG12 gene pair, the entire intergenic region hardly responded to Tg, whereas the CRELD2 promoter constructs of the proximal region containing the ERSE motif showed a marked responsiveness to Tg.
    [Show full text]
  • Noelia Díaz Blanco
    Effects of environmental factors on the gonadal transcriptome of European sea bass (Dicentrarchus labrax), juvenile growth and sex ratios Noelia Díaz Blanco Ph.D. thesis 2014 Submitted in partial fulfillment of the requirements for the Ph.D. degree from the Universitat Pompeu Fabra (UPF). This work has been carried out at the Group of Biology of Reproduction (GBR), at the Department of Renewable Marine Resources of the Institute of Marine Sciences (ICM-CSIC). Thesis supervisor: Dr. Francesc Piferrer Professor d’Investigació Institut de Ciències del Mar (ICM-CSIC) i ii A mis padres A Xavi iii iv Acknowledgements This thesis has been made possible by the support of many people who in one way or another, many times unknowingly, gave me the strength to overcome this "long and winding road". First of all, I would like to thank my supervisor, Dr. Francesc Piferrer, for his patience, guidance and wise advice throughout all this Ph.D. experience. But above all, for the trust he placed on me almost seven years ago when he offered me the opportunity to be part of his team. Thanks also for teaching me how to question always everything, for sharing with me your enthusiasm for science and for giving me the opportunity of learning from you by participating in many projects, collaborations and scientific meetings. I am also thankful to my colleagues (former and present Group of Biology of Reproduction members) for your support and encouragement throughout this journey. To the “exGBRs”, thanks for helping me with my first steps into this world. Working as an undergrad with you Dr.
    [Show full text]
  • Molecular Effects of Isoflavone Supplementation Human Intervention Studies and Quantitative Models for Risk Assessment
    Molecular effects of isoflavone supplementation Human intervention studies and quantitative models for risk assessment Vera van der Velpen Thesis committee Promotors Prof. Dr Pieter van ‘t Veer Professor of Nutritional Epidemiology Wageningen University Prof. Dr Evert G. Schouten Emeritus Professor of Epidemiology and Prevention Wageningen University Co-promotors Dr Anouk Geelen Assistant professor, Division of Human Nutrition Wageningen University Dr Lydia A. Afman Assistant professor, Division of Human Nutrition Wageningen University Other members Prof. Dr Jaap Keijer, Wageningen University Dr Hubert P.J.M. Noteborn, Netherlands Food en Consumer Product Safety Authority Prof. Dr Yvonne T. van der Schouw, UMC Utrecht Dr Wendy L. Hall, King’s College London This research was conducted under the auspices of the Graduate School VLAG (Advanced studies in Food Technology, Agrobiotechnology, Nutrition and Health Sciences). Molecular effects of isoflavone supplementation Human intervention studies and quantitative models for risk assessment Vera van der Velpen Thesis submitted in fulfilment of the requirements for the degree of doctor at Wageningen University by the authority of the Rector Magnificus Prof. Dr M.J. Kropff, in the presence of the Thesis Committee appointed by the Academic Board to be defended in public on Friday 20 June 2014 at 13.30 p.m. in the Aula. Vera van der Velpen Molecular effects of isoflavone supplementation: Human intervention studies and quantitative models for risk assessment 154 pages PhD thesis, Wageningen University, Wageningen, NL (2014) With references, with summaries in Dutch and English ISBN: 978-94-6173-952-0 ABSTRact Background: Risk assessment can potentially be improved by closely linked experiments in the disciplines of epidemiology and toxicology.
    [Show full text]
  • KDELR3 Dnaxpab a C-Terminal Tetrapeptide Signal, Usually Lys-Asp-Glu-Leu (KDEL) in Animal Cells, and His-Asp-Glu-Leu (HDEL) in S
    KDELR3 DNAxPab a C-terminal tetrapeptide signal, usually lys-asp-glu-leu (KDEL) in animal cells, and his-asp-glu-leu (HDEL) in S. Catalog Number: H00011015-W01P cerevisiae. This process is mediated by a receptor that recognizes, and binds the tetrapeptide-containing Regulation Status: For research use only (RUO) protein, and returns it to the ER. In yeast, the sorting receptor encoded by a single gene, ERD2, is a Product Description: Rabbit polyclonal antibody raised seven-transmembrane protein. Unlike yeast, several against a full-length human KDELR3 DNA using DNAx™ human homologs of the ERD2 gene, constituting the Immune technology. KDEL receptor gene family, have been described. KDELR3 was the third member of the family to be Immunogen: Full-length human DNA identified, and it encodes a protein highly homologous to KDELR1 and KDELR2 proteins. Two transcript variants Sequence: of KDELR3 that arise by alternative splicing, and encode MNVFRILGDLSHLLAMILLLGKIWRSKCCKGISGKSQIL different isoforms of KDELR3 receptor, have been FALVFTTRYLDLFTNFISIYNTVMKVVFLLCAYVTVYMIY described. [provided by RefSeq] GKFRKTFDSENDTFRLEFLLVPVIGLSFLENYSFTLLEIL WTFSIYLESVAILPQLFMISKTGEAETITTHYLFFLGLYR ALYLANWIRRYQTENFYDQIAVVSGVVQTIFYCDFFYL YVTKVLKGKKLSLPMPI Host: Rabbit Reactivity: Human Applications: Flow Cyt-Tr, IF-Ex, IF-Tr, WB-Tr (See our web site product page for detailed applications information) Protocols: See our web site at http://www.abnova.com/support/protocols.asp or product page for detailed protocols Purification: Protein A Storage Buffer: In 1x PBS, pH 7.4 Storage Instruction: Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. Entrez GeneID: 11015 Gene Symbol: KDELR3 Gene Alias: ERD2L3 Gene Summary: Retention of resident soluble proteins in the lumen of the endoplasmic reticulum (ER) is achieved in both yeast and animal cells by their continual retrieval from the cis-Golgi, or a pre-Golgi compartment.
    [Show full text]
  • TITLE PAGE Oxidative Stress and Response to Thymidylate Synthase
    Downloaded from molpharm.aspetjournals.org at ASPET Journals on October 2, 2021 -Targeted -Targeted 1 , University of of , University SC K.W.B., South Columbia, (U.O., Carolina, This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted. The final version may differ from this version. This article has not been copyedited and formatted.
    [Show full text]
  • Duplications at 19Q13.33 in Patients with Neurodevelopmental Disorders
    bioRxiv preprint doi: https://doi.org/10.1101/130377; this version posted April 25, 2017. 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. Duplications at 19q13.33 in patients with neurodevelopmental disorders. Eduardo Pérez-Palma, PhD; Elmo Saarentaus; Joris Andrieux, MD, PhD; Marie Ravoet, PhD; Giancarlo V. De Ferrari, PhD; Peter Nuernberg, PhD; Bertrand Isidor, MD, PhD; Bernd A. Neubauer, MD, ; Dennis Lal, PhD. Eduardo Pérez.Palma, Center for Biomedical Research, Faculty of Biological Sciences and Faculty of Medicine, Universidad Andres Bello, Santiago, Chile; and the Cologne Center for Genomics, University of Cologne, Cologne, Germany. Elmo Saarentaus, Stanley Center for Psychiatric Genetics, Broad Institute of MIT and Harvard, Cambridge, Massachusetts, USA; and the Analytic and Translational Genetics Unit, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA, USA. Joris Andrieux,Institut de Génétique Médicale Hopital Jeanne de Flandre CHRU de Lille, France. Marie Ravoet, Molecular Immunology Unit, Institut Jules Bordet, Université Libre de Bruxelles, Brussels, Belgium. Giancarlo V. De Ferrari, Center for Biomedical Research, Faculty of Biological Sciences and Faculty of Medicine, Universidad Andres Bello, Santiago, Chile. Peter Nürnberg, Cologne Center for Genomics, University of Cologne, Cologne, Germany. Bertrand Isidor, Service de Génétique Médicale, CHU Hôtel Dieu, France. Bernd A. Neubauer, Department of Neuropediatrics, University Medical Clinic Giessen, Giessen, Germany. Dennis Lal, Stanley Center for Psychiatric Genetics, Broad Institute of MIT and Harvard, Cambridge, Massachusetts, USA; the Analytic and Translational Genetics Unit, Department of Medicine, Massachusetts General Hospital and Harvard Medical School, Boston, MA, USA; and the Cologne Center for Genomics, University of Cologne, Cologne, Germany.
    [Show full text]
  • Placenta-Derived Exosomes Continuously Increase in Maternal
    Sarker et al. Journal of Translational Medicine 2014, 12:204 http://www.translational-medicine.com/content/12/1/204 RESEARCH Open Access Placenta-derived exosomes continuously increase in maternal circulation over the first trimester of pregnancy Suchismita Sarker1, Katherin Scholz-Romero1, Alejandra Perez2, Sebastian E Illanes1,2,3, Murray D Mitchell1, Gregory E Rice1,2 and Carlos Salomon1,2* Abstract Background: Human placenta releases specific nanovesicles (i.e. exosomes) into the maternal circulation during pregnancy, however, the presence of placenta-derived exosomes in maternal blood during early pregnancy remains to be established. The aim of this study was to characterise gestational age related changes in the concentration of placenta-derived exosomes during the first trimester of pregnancy (i.e. from 6 to 12 weeks) in plasma from women with normal pregnancies. Methods: A time-series experimental design was used to establish pregnancy-associated changes in maternal plasma exosome concentrations during the first trimester. A series of plasma were collected from normal healthy women (10 patients) at 6, 7, 8, 9, 10, 11 and 12 weeks of gestation (n = 70). We measured the stability of these vesicles by quantifying and observing their protein and miRNA contents after the freeze/thawing processes. Exosomes were isolated by differential and buoyant density centrifugation using a sucrose continuous gradient and characterised by their size distribution and morphology using the nanoparticles tracking analysis (NTA; Nanosight™) and electron microscopy (EM), respectively. The total number of exosomes and placenta-derived exosomes were determined by quantifying the immunoreactive exosomal marker, CD63 and a placenta-specific marker (Placental Alkaline Phosphatase PLAP).
    [Show full text]