Differential Expression of Hydroxyurea Transporters in Normal and Polycythemia Vera Hematopoietic Stem and Progenitor Cell Subpopulations
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New Advances in Urea Transporter UT-A1 Membrane Trafficking
Int. J. Mol. Sci. 2013, 14, 10674-10682; doi:10.3390/ijms140510674 OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 www.mdpi.com/journal/ijms Review New Advances in Urea Transporter UT-A1 Membrane Trafficking Guangping Chen Department of Physiology, Emory University School of Medicine, Atlanta, GA 30322, USA; E-Mail: [email protected]; Tel.: +1-404-727-7494; Fax: +1-404-727-2648. Received: 22 April 2013; in revised form: 9 May 2013 / Accepted: 9 May 2013 / Published: 21 May 2013 Abstract: The vasopressin-regulated urea transporter UT-A1, expressed in kidney inner medullary collecting duct (IMCD) epithelial cells, plays a critical role in the urinary concentrating mechanisms. As a membrane protein, the function of UT-A1 transport activity relies on its presence in the plasma membrane. Therefore, UT-A1 successfully trafficking to the apical membrane of the polarized epithelial cells is crucial for the regulation of urea transport. This review summarizes the research progress of UT-A1 regulation over the past few years, specifically on the regulation of UT-A1 membrane trafficking by lipid rafts, N-linked glycosylation and a group of accessory proteins. Keywords: lipid rafts; glycosylation; accessory proteins; SNARE protein; cytoskeleton protein 1. Introduction Urea is the major end product of amino acid metabolism. It is generated from the ornithine cycle in liver, and is ultimately excreted by the kidney representing 90% of total nitrogen in urine. The physiological significance of urea in the production of concentrated urine was recognized by Gamble in the 1930s [1,2]. Urea reabsorbed in the kidney inner medullary collecting duct (IMCD) contributes to the development of the osmolality in the medullary interstitium. -
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. -
Protein Identities in Evs Isolated from U87-MG GBM Cells As Determined by NG LC-MS/MS
Protein identities in EVs isolated from U87-MG GBM cells as determined by NG LC-MS/MS. No. Accession Description Σ Coverage Σ# Proteins Σ# Unique Peptides Σ# Peptides Σ# PSMs # AAs MW [kDa] calc. pI 1 A8MS94 Putative golgin subfamily A member 2-like protein 5 OS=Homo sapiens PE=5 SV=2 - [GG2L5_HUMAN] 100 1 1 7 88 110 12,03704523 5,681152344 2 P60660 Myosin light polypeptide 6 OS=Homo sapiens GN=MYL6 PE=1 SV=2 - [MYL6_HUMAN] 100 3 5 17 173 151 16,91913397 4,652832031 3 Q6ZYL4 General transcription factor IIH subunit 5 OS=Homo sapiens GN=GTF2H5 PE=1 SV=1 - [TF2H5_HUMAN] 98,59 1 1 4 13 71 8,048185945 4,652832031 4 P60709 Actin, cytoplasmic 1 OS=Homo sapiens GN=ACTB PE=1 SV=1 - [ACTB_HUMAN] 97,6 5 5 35 917 375 41,70973209 5,478027344 5 P13489 Ribonuclease inhibitor OS=Homo sapiens GN=RNH1 PE=1 SV=2 - [RINI_HUMAN] 96,75 1 12 37 173 461 49,94108966 4,817871094 6 P09382 Galectin-1 OS=Homo sapiens GN=LGALS1 PE=1 SV=2 - [LEG1_HUMAN] 96,3 1 7 14 283 135 14,70620005 5,503417969 7 P60174 Triosephosphate isomerase OS=Homo sapiens GN=TPI1 PE=1 SV=3 - [TPIS_HUMAN] 95,1 3 16 25 375 286 30,77169764 5,922363281 8 P04406 Glyceraldehyde-3-phosphate dehydrogenase OS=Homo sapiens GN=GAPDH PE=1 SV=3 - [G3P_HUMAN] 94,63 2 13 31 509 335 36,03039959 8,455566406 9 Q15185 Prostaglandin E synthase 3 OS=Homo sapiens GN=PTGES3 PE=1 SV=1 - [TEBP_HUMAN] 93,13 1 5 12 74 160 18,68541938 4,538574219 10 P09417 Dihydropteridine reductase OS=Homo sapiens GN=QDPR PE=1 SV=2 - [DHPR_HUMAN] 93,03 1 1 17 69 244 25,77302971 7,371582031 11 P01911 HLA class II histocompatibility antigen, -
Anti-SLC22A13 (Aa 38-139) Polyclonal Antibody (DPAB-DC3801) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-SLC22A13 (aa 38-139) polyclonal antibody (DPAB-DC3801) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Antigen Description This gene encodes a member of the organic-cation transporter family. It is located in a gene cluster with another member of the family, organic cation transporter like 4. The encoded protein is a transmembrane protein involved in the transport of small molecules. This protein can function to mediate urate uptake and is a high affinity nicotinate exchanger in the kidneys and the intestine. Immunogen SLC22A13 (NP_004247, 38 a.a. ~ 139 a.a) partial recombinant protein with GST tag. The sequence is AHVFMVLDEPHHCAVAWVKNHTFNLSAAEQLVLSVPLDTAGHPEPCLMFRPPPANASLQDILSH RFNETQPCDMGWEYPENRLPSLKNEFNLVCDRKHLKDT Source/Host Mouse Species Reactivity Human Conjugate Unconjugated Applications WB (Recombinant protein), ELISA, Size 50 μl Buffer 50 % glycerol Preservative None Storage Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. GENE INFORMATION Gene Name SLC22A13 solute carrier family 22 (organic anion/urate transporter), member 13 [ Homo sapiens (human) ] Official Symbol SLC22A13 Synonyms SLC22A13; solute carrier family 22 (organic anion/urate transporter), member 13; OAT10; 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 OCTL1; OCTL3; ORCTL3; ORCTL-3; solute carrier family 22 member 13; organic cation transporter-like 3; organic-cation transporter like 3; organic cationic transporter-like 3; solute carrier family 22, member 13; solute carrier family 22 (organic anion transporter), member 13; Entrez Gene ID 9390 Protein Refseq NP_004247 UniProt ID Q9Y226 Chromosome Location 3p21.3 Function nicotinate transporter activity; organic cation transmembrane transporter activity; 45-1 Ramsey Road, Shirley, NY 11967, USA Email: [email protected] Tel: 1-631-624-4882 Fax: 1-631-938-8221 2 © Creative Diagnostics All Rights Reserved. -
Cellular and Molecular Signatures in the Disease Tissue of Early
Cellular and Molecular Signatures in the Disease Tissue of Early Rheumatoid Arthritis Stratify Clinical Response to csDMARD-Therapy and Predict Radiographic Progression Frances Humby1,* Myles Lewis1,* Nandhini Ramamoorthi2, Jason Hackney3, Michael Barnes1, Michele Bombardieri1, Francesca Setiadi2, Stephen Kelly1, Fabiola Bene1, Maria di Cicco1, Sudeh Riahi1, Vidalba Rocher-Ros1, Nora Ng1, Ilias Lazorou1, Rebecca E. Hands1, Desiree van der Heijde4, Robert Landewé5, Annette van der Helm-van Mil4, Alberto Cauli6, Iain B. McInnes7, Christopher D. Buckley8, Ernest Choy9, Peter Taylor10, Michael J. Townsend2 & Costantino Pitzalis1 1Centre for Experimental Medicine and Rheumatology, William Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK. Departments of 2Biomarker Discovery OMNI, 3Bioinformatics and Computational Biology, Genentech Research and Early Development, South San Francisco, California 94080 USA 4Department of Rheumatology, Leiden University Medical Center, The Netherlands 5Department of Clinical Immunology & Rheumatology, Amsterdam Rheumatology & Immunology Center, Amsterdam, The Netherlands 6Rheumatology Unit, Department of Medical Sciences, Policlinico of the University of Cagliari, Cagliari, Italy 7Institute of Infection, Immunity and Inflammation, University of Glasgow, Glasgow G12 8TA, UK 8Rheumatology Research Group, Institute of Inflammation and Ageing (IIA), University of Birmingham, Birmingham B15 2WB, UK 9Institute of -
Dur3 Is the Major Urea Transporter in Candida Albicans and Is Co-Regulated with the Urea Amidolyase Dur1,2 Dhammika H
University of Nebraska - Lincoln DigitalCommons@University of Nebraska - Lincoln Kenneth Nickerson Papers Papers in the Biological Sciences 2011 Dur3 is the major urea transporter in Candida albicans and is co-regulated with the urea amidolyase Dur1,2 Dhammika H. M. L. P Navarathna National Cancer Institute Aditi Das Universitat Wurzburg Joachim Morschhauser Universitat Wurzburg Kenneth W. Nickerson University of Nebraska - Lincoln, [email protected] David D. Roberts National Cancer Institute, [email protected] Follow this and additional works at: http://digitalcommons.unl.edu/bioscinickerson Part of the Environmental Microbiology and Microbial Ecology Commons, Other Life Sciences Commons, and the Pathogenic Microbiology Commons Navarathna, Dhammika H. M. L. P; Das, Aditi; Morschhauser, Joachim; Nickerson, Kenneth W.; and Roberts, David D., "Dur3 is the major urea transporter in Candida albicans and is co-regulated with the urea amidolyase Dur1,2" (2011). Kenneth Nickerson Papers. 11. http://digitalcommons.unl.edu/bioscinickerson/11 This Article is brought to you for free and open access by the Papers in the Biological Sciences at DigitalCommons@University of Nebraska - Lincoln. It has been accepted for inclusion in Kenneth Nickerson Papers by an authorized administrator of DigitalCommons@University of Nebraska - Lincoln. Microbiology (2011), 157, 270–279 DOI 10.1099/mic.0.045005-0 Dur3 is the major urea transporter in Candida albicans and is co-regulated with the urea amidolyase Dur1,2 Dhammika H. M. L. P. Navarathna,1 Aditi Das,2 Joachim Morschha¨user,2 Kenneth W. Nickerson3 and David D. Roberts1 Correspondence 1Laboratory of Pathology, Center for Cancer Research, National Cancer Institute, National Institutes David D. -
Serum Albumin OS=Homo Sapiens
Protein Name Cluster of Glial fibrillary acidic protein OS=Homo sapiens GN=GFAP PE=1 SV=1 (P14136) Serum albumin OS=Homo sapiens GN=ALB PE=1 SV=2 Cluster of Isoform 3 of Plectin OS=Homo sapiens GN=PLEC (Q15149-3) Cluster of Hemoglobin subunit beta OS=Homo sapiens GN=HBB PE=1 SV=2 (P68871) Vimentin OS=Homo sapiens GN=VIM PE=1 SV=4 Cluster of Tubulin beta-3 chain OS=Homo sapiens GN=TUBB3 PE=1 SV=2 (Q13509) Cluster of Actin, cytoplasmic 1 OS=Homo sapiens GN=ACTB PE=1 SV=1 (P60709) Cluster of Tubulin alpha-1B chain OS=Homo sapiens GN=TUBA1B PE=1 SV=1 (P68363) Cluster of Isoform 2 of Spectrin alpha chain, non-erythrocytic 1 OS=Homo sapiens GN=SPTAN1 (Q13813-2) Hemoglobin subunit alpha OS=Homo sapiens GN=HBA1 PE=1 SV=2 Cluster of Spectrin beta chain, non-erythrocytic 1 OS=Homo sapiens GN=SPTBN1 PE=1 SV=2 (Q01082) Cluster of Pyruvate kinase isozymes M1/M2 OS=Homo sapiens GN=PKM PE=1 SV=4 (P14618) Glyceraldehyde-3-phosphate dehydrogenase OS=Homo sapiens GN=GAPDH PE=1 SV=3 Clathrin heavy chain 1 OS=Homo sapiens GN=CLTC PE=1 SV=5 Filamin-A OS=Homo sapiens GN=FLNA PE=1 SV=4 Cytoplasmic dynein 1 heavy chain 1 OS=Homo sapiens GN=DYNC1H1 PE=1 SV=5 Cluster of ATPase, Na+/K+ transporting, alpha 2 (+) polypeptide OS=Homo sapiens GN=ATP1A2 PE=3 SV=1 (B1AKY9) Fibrinogen beta chain OS=Homo sapiens GN=FGB PE=1 SV=2 Fibrinogen alpha chain OS=Homo sapiens GN=FGA PE=1 SV=2 Dihydropyrimidinase-related protein 2 OS=Homo sapiens GN=DPYSL2 PE=1 SV=1 Cluster of Alpha-actinin-1 OS=Homo sapiens GN=ACTN1 PE=1 SV=2 (P12814) 60 kDa heat shock protein, mitochondrial OS=Homo -
Abrothrix Olivacea)
Received: 13 June 2017 | Revised: 30 May 2018 | Accepted: 31 May 2018 DOI: 10.1111/mec.14778 ORIGINAL ARTICLE An association between differential expression and genetic divergence in the Patagonian olive mouse (Abrothrix olivacea) Facundo M. Giorello1,2 | Matias Feijoo1 | Guillermo D'Elía3 | Daniel E. Naya1 | Lourdes Valdez3 | Juan C. Opazo3 | Enrique P. Lessa1 1Departamento de Ecología y Evolución, Facultad de Ciencias, Universidad de la Abstract República, Montevideo, Uruguay Recent molecular studies have found striking differences between desert‐adapted 2Espacio de Biología Vegetal del Noreste, species and model mammals regarding water conservation. In particular, aquaporin Centro Universitario de Tacuarembó, Universidad de la República, Tacuarembó, 4, a classical gene involved in water regulation of model species, is absent or not Uruguay expressed in the kidneys of desert‐adapted species. To further understand the 3Instituto de Ciencias Ambientales y Evolutivas, Universidad Austral de Chile, molecular response to water availability, we studied the Patagonian olive mouse Valdivia, Chile Abrothrix olivacea, a species with an unusually broad ecological tolerance that exhi- Correspondence bits a great urine concentration capability. The species is able to occupy both the Facundo M. Giorello, Departamento de arid Patagonian steppe and the Valdivian and Magellanic forests. We sampled 95 Ecología y Evolución, Facultad de Ciencias, Universidad de la República, Iguá 4225, olive mouse specimens from four localities (two in the steppe and two in the for- Montevideo 11400, Uruguay. ests) and analysed both phenotypic variables and transcriptomic data to investigate Email: [email protected] the response of this species to the contrasting environmental conditions. The rela- Funding information tive size of the kidney and the ratio of urine to plasma concentrations were, as Fondo Nacional de Desarrollo Científico y Tecnológico, Grant/Award Number: expected, negatively correlated with annual rainfall. -
Structure and Permeation Mechanism of a Mammalian Urea Transporter
Structure and permeation mechanism of a mammalian urea transporter Elena J. Levina,1, Yu Caoa,1, Giray Enkavib, Matthias Quickc, Yaping Pana, Emad Tajkhorshidb,2, and Ming Zhoua,2 aDepartment of Physiology and Cellular Biophysics, College of Physicians and Surgeons, Columbia University, 630 West 168th Street, New York, NY 10032; bCenter for Biophysics and Computational Biology, Department of Biochemistry, College of Medicine, and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801; and cDepartment of Psychiatry and Center for Molecular Recognition, Columbia University, 650 West 168th Street, New York, NY 10032 Edited by Christopher Miller, HHMI, Brandeis University, Waltham, MA, and approved June 1, 2012 (received for review May 3, 2012) As an adaptation to infrequent access to water, terrestrial mam- homolog (21), dvUT, which forms a trimer with a continuous mals produce urine that is hyperosmotic to plasma. To prevent membrane-spanning pore at the center of each protomer. How- osmotic diuresis by the large quantity of urea generated by protein ever, it remained unclear how similar this structure was to that catabolism, the kidney epithelia contain facilitative urea transpor- of the mammalian UTs, and the details of the permeation me- ters (UTs) that allow rapid equilibration between the urinary space chanism were unknown. To answer these questions, we solved and the hyperosmotic interstitium. Here we report the first X-ray the structure of a mammalian UT-B and investigated the permea- crystal structure of a mammalian UT, UT-B, at a resolution of 2.36 Å. tion mechanism with molecular dynamics simulations and func- UT-B is a homotrimer and each protomer contains a urea con- tional studies of UT-B mutants. -
Supplementary Table S4. FGA Co-Expressed Gene List in LUAD
Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase -
Daphnia Pulex Lineages in Response to Acute Copper Exposure Sneha Suresh1,2, Teresa J
Suresh et al. BMC Genomics (2020) 21:433 https://doi.org/10.1186/s12864-020-06831-4 RESEARCH ARTICLE Open Access Alternative splicing is highly variable among Daphnia pulex lineages in response to acute copper exposure Sneha Suresh1,2, Teresa J. Crease3, Melania E. Cristescu4 and Frédéric J. J. Chain1* Abstract Background: Despite being one of the primary mechanisms of gene expression regulation in eukaryotes, alternative splicing is often overlooked in ecotoxicogenomic studies. The process of alternative splicing facilitates the production of multiple mRNA isoforms from a single gene thereby greatly increasing the diversity of the transcriptome and proteome. This process can be important in enabling the organism to cope with stressful conditions. Accurate identification of splice sites using RNA sequencing requires alignment to independent exonic positions within the genome, presenting bioinformatic challenges, particularly when using short read data. Although technological advances allow for the detection of splicing patterns on a genome-wide scale, very little is known about the extent of intraspecies variation in splicing patterns, particularly in response to environmental stressors. In this study, we used RNA-sequencing to study the molecular responses to acute copper exposure in three lineages of Daphnia pulex by focusing on the contribution of alternative splicing in addition to gene expression responses. Results: By comparing the overall gene expression and splicing patterns among all 15 copper-exposed samples and 6 controls, we identified 588 differentially expressed (DE) genes and 16 differentially spliced (DS) genes. Most of the DS genes (13) were not found to be DE, suggesting unique transcriptional regulation in response to copper that went unnoticed with conventional DE analysis. -
Analysis of OAT, OCT, OCTN, and Other Family Members Reveals 8
bioRxiv preprint doi: https://doi.org/10.1101/2019.12.23.887299; this version posted December 26, 2019. 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. Reclassification of SLC22 Transporters: Analysis of OAT, OCT, OCTN, and other Family Members Reveals 8 Functional Subgroups Darcy Engelhart1, Jeffry C. Granados2, Da Shi3, Milton Saier Jr.4, Michael Baker6, Ruben Abagyan3, Sanjay K. Nigam5,6 1Department of Biology, University of California San Diego, La Jolla 92093 2Department of Bioengineering, University of California San Diego, La Jolla 92093 3School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla 92093 4Department of Molecular Biology, Division of Biological Sciences, University of California at San Diego, San Diego, CA, USA 5Department of Pediatrics, University of California San Diego, La Jolla 92093 6Department of Medicine, University of California San Diego, La Jolla 92093 *To whom correspondence should be addressed: [email protected] Running title: Functional subgroups for SLC22 1 bioRxiv preprint doi: https://doi.org/10.1101/2019.12.23.887299; this version posted December 26, 2019. 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. Abstract Among transporters, the SLC22 family is emerging as a central hub of endogenous physiology.