Axxam Cell-Based Assay List
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Cells Δγ Lineage Choice and Shapes Peripheral Purinergic P2X7
Purinergic P2X7 Receptor Drives T Cell Lineage Choice and Shapes Peripheral δγ Cells This information is current as Michela Frascoli, Jessica Marcandalli, Ursula Schenk and of October 2, 2021. Fabio Grassi J Immunol 2012; 189:174-180; Prepublished online 30 May 2012; doi: 10.4049/jimmunol.1101582 http://www.jimmunol.org/content/189/1/174 Downloaded from Supplementary http://www.jimmunol.org/content/suppl/2012/05/30/jimmunol.110158 Material 2.DC1 http://www.jimmunol.org/ References This article cites 31 articles, 15 of which you can access for free at: http://www.jimmunol.org/content/189/1/174.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists by guest on October 2, 2021 • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2012 by The American Association of Immunologists, Inc. All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Purinergic P2X7 Receptor Drives T Cell Lineage Choice and Shapes Peripheral gd Cells Michela Frascoli,* Jessica Marcandalli,* Ursula Schenk,*,1 and Fabio Grassi*,† TCR signal strength instructs ab versus gd lineage decision in immature T cells. -
Sara Catarina Timóteo Dos Santos Domingues Identificação De
Universidade de Aveiro Secção Autónoma de Ciências da Saúde 201 2 Sara Catarina Timóteo Identificação de Complexos Proteicos na Doença de dos Santos Domingues Alzheimer Identification of Protein Complexes in Alzheimer’s Disease Universida de de Aveiro Secção Autónoma de Ciências da Saúde 20 12 Sara Catarina Timóteo Identificação de Complexos Proteicos na Doença de dos Santos Domingues Alzheimer Identification of Protein Complexes in Alzheimer’s Disease Tese apresentada à Universidade de Aveiro para cumprimento dos requisitos necessários à obtenção do grau de Doutor em Ciências Biomédicas, realizada sob a orientação científica da Prof. Doutora Odete Abreu Beirão da Cruz e Silva, Professora Auxiliar com Agregação da Secção Autónoma de Ciências da Saúde da Universidade de Aveiro. Apoio financeiro da FCT e do FSE no âmbito do III Quadro Comunitário de Apoio (Bolsa de Doutoramento SFRH/ BD/ 21559/ 2005 ). o júri presidente Doutor Artur da Rosa Pires Professor Catedrático da Universidade de Aveiro Doutor Uwe Konietzko Investigador Sénior da Universidade de Zurique Doutor José António Henriques de Conde Belo Professor Associado com Agregação da Universidade do Algarve Doutora Patrícia Espinheira de Sá Maciel Professora Associada da Escola de Ciências da Saúde da Universidade do Minho Doutora Odete Abreu Beirão da Cruz e Silva Professora Auxiliar com Agregação da Universidade de Aveiro Doutora Margarida Sâncio da Cruz Fardilha Professora Auxiliar Convidada da Universidade de Aveiro agradecimentos I would like to express my gratitude to FCT, for the financial support. To the Centre for Cell Biology and to the Biology and Health Sciences Departments from the University of Aveiro, for providing the necessary conditions. -
FTY720P Upregulates the Na+/K+ Atpase in Hepg2 Cells by Activating S1PR3 and Inducing PGE2 Release
Cellular Physiology Cell Physiol Biochem 2019;53:518-531 DOI: 10.33594/00000015510.33594/000000155 © 2019 The Author(s).© 2019 Published The Author(s) by and Biochemistry Published online: 11 SeptemberSeptember 20192019 Cell Physiol BiochemPublished Press GmbH&Co. by Cell Physiol KG Biochem 518 + + Press GmbH&Co. KG, Duesseldorf ChakkourAccepted: 5et September al.: FTY720-P 2019 Upregulates Na /K Atpase www.cellphysiolbiochem.com This article is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 Interna- tional License (CC BY-NC-ND). Usage and distribution for commercial purposes as well as any distribution of modified material requires written permission. Original Paper FTY720P Upregulates the Na+/K+ ATPase in HepG2 Cells by Activating S1PR3 and Inducing PGE2 Release Mohamed Chakkour Sawsan Kreydiyyeh Department of Biology, Faculty of Arts & Sciences, American University of Beirut, Beirut, Lebanon Key Words FTY720-P • Na+/K+ATPase • HepG2 • PKC • ERK • PGE2 Abstract Background/Aims: Liver regeneration is induced by S1P and accompanied with an increase in hepatic Na+/K+ ATPase activity, suggesting a potential modulatory role of the sphingolipid on the ATPase activity. The ability of S1P to alter the ATPase activity was confirmed in a previous work which showed a time dependent effect, with an inhibition appearing at 15min and a stimulation at two hours. The aim of this work was to investigate if FTY720-P, an analogue of S1P used in the treatment of multiple sclerosis, exerts a similar effect at 2 hours. Methods: HepG2 cells were treated with FTY720-P for two hours and the activity of the Na+/K+ ATPase was assayed by measuring the amount of inorganic phosphate liberated in presence and absence of ouabain. -
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. -
Bradykinin Receptor Deficiency Or Antagonism Do Not Impact the Host
Ding et al. Intensive Care Medicine Experimental (2019) 7:14 Intensive Care Medicine https://doi.org/10.1186/s40635-019-0228-3 Experimental RESEARCH Open Access Bradykinin receptor deficiency or antagonism do not impact the host response during gram-negative pneumonia-derived sepsis Chao Ding1,2, Jack Yang2, Cornelis van’t Veer2 and Tom van der Poll2,3* * Correspondence: t.vanderpoll@ amc.uva.nl Abstract 2Center of Experimental and Molecular Medicine, Academic Background: Kinins are short peptides with a wide range of proinflammatory Medical Center, University of properties that are generated from kininogens in the so-called kallikrein-kinin system. Amsterdam, Meibergdreef 9, Room Kinins exert their biological activities through stimulation of two distinct receptor G2-130, 1105 AZ Amsterdam, the Netherlands subtypes, the kinin or bradykinin B1 and B2 receptors (B1R, B2R). Acute challenge 3Division of Infectious Diseases, models have implicated B1R and B2R in the pathogenesis of sepsis. However, their Academic Medical Center, role in the host response during sepsis originating from the lung is not known. University of Amsterdam, Amsterdam, the Netherlands Results: To determine the role of B1R and B2R in pneumonia-derived sepsis, B1R/ Full list of author information is B2R-deficient mice and wild-type mice treated with the B1R antagonist R-715 or the available at the end of the article B2R antagonist HOE-140 were studied after infection with the common gram- negative pathogen Klebsiella pneumoniae via the airways. Neither B1R/B2R deficiency nor B1R or B2R inhibition influenced bacterial growth at the primary site of infection or dissemination to distant body sites. -
An Explanation of G-Protein Coupled Receptor Structure
Journal of Stem Cell Research & Therapeutics Review Article Open Access Role of GPCRS towards cell: an explanation of g-protein coupled receptor structure Abstract Volume 2 Issue 3 - 2017 G- protein coupled receptors are the heptahelical, serpentine receptor and are Nidhi Sharma,1 Anil Kumar Sahdev,2 Vinit Raj2 multifunctional receptors having modulatory activity of a wide variety of biological 1Dr. K. N. Modi Institute of Pharmacy & Research centre, process including: Neurotransmission, Chemoattraction, Cardiac function, Olfaction Modinagar, India. and Vision etc. At largest level they are involved in signal transduction across cell 2Department of Pharmaceutical Sciences, Babasaheb Bhimrao membranes therefore they represent major targets in the development of novel drug Ambedkar University, India candidates in all clinical areas. Particularly membrane cholesterol has been reported to have a great role in the functioning of a number of GPCRs. Apart from this it also Correspondence: Vinit Raj, Department of Pharmaceutical have some drawbacks. Mutations that occur are associated with a broad spectrum of Sciences, Babasaheb Bhimrao Ambedkar University, VidyaVihar, diseases of diverse etiology. As a mutations result, there is a change in receptor activity Rae Bareli Road, Lucknow-226025, Email [email protected] (GPCR become inactive, overactive, or constitutively active), in the process of ligand binding and signal transduction. Changes in the GPCRs functioning can cause diseases Received: January 31, 2017 | Published: March 27, 2017 such as retinitis pigmentosa (rhodopsin mutations), nephrogenic diabetes insipidus (vasopressin receptor mutations), and obesity (melanocortin receptor mutations). Keywords: gpcrs, serpentine receptor, neurotransmission, retinitis pigmentosa, nephrogenic diabetes insipidus, bardet-biedl syndrome, hypogonadism Introduction deliver a message and appropriate cellular and physiological response1,2 (Figure 1). -
Investigation of Candidate Genes and Mechanisms Underlying Obesity
Prashanth et al. BMC Endocrine Disorders (2021) 21:80 https://doi.org/10.1186/s12902-021-00718-5 RESEARCH ARTICLE Open Access Investigation of candidate genes and mechanisms underlying obesity associated type 2 diabetes mellitus using bioinformatics analysis and screening of small drug molecules G. Prashanth1 , Basavaraj Vastrad2 , Anandkumar Tengli3 , Chanabasayya Vastrad4* and Iranna Kotturshetti5 Abstract Background: Obesity associated type 2 diabetes mellitus is a metabolic disorder ; however, the etiology of obesity associated type 2 diabetes mellitus remains largely unknown. There is an urgent need to further broaden the understanding of the molecular mechanism associated in obesity associated type 2 diabetes mellitus. Methods: To screen the differentially expressed genes (DEGs) that might play essential roles in obesity associated type 2 diabetes mellitus, the publicly available expression profiling by high throughput sequencing data (GSE143319) was downloaded and screened for DEGs. Then, Gene Ontology (GO) and REACTOME pathway enrichment analysis were performed. The protein - protein interaction network, miRNA - target genes regulatory network and TF-target gene regulatory network were constructed and analyzed for identification of hub and target genes. The hub genes were validated by receiver operating characteristic (ROC) curve analysis and RT- PCR analysis. Finally, a molecular docking study was performed on over expressed proteins to predict the target small drug molecules. Results: A total of 820 DEGs were identified between -
Integrated Triple Gut Hormone Action Broadens the Therapeutic Potential of Endocrine Biologics for Metabolic Diseases
Integrated triple gut hormone action broadens the therapeutic potential of endocrine biologics for metabolic diseases Brian Finan1–3*#, Bin Yang3,4*, Nickki Ottaway5, David L. Smiley3, Tao Ma3,6, Christoffer Clemmensen1,2, Joe Chabenne3,7, Lianshan Zhang4, Kirk M. Habegger8, Katrin Fischer1,2, Jonathan E. Campbell9, Darleen Sandoval5, Randy J. Seeley5, Konrad Bleicher10, Sabine Uhles10, William Riboulet10, Jürgen Funk10, Cornelia Hertel10, Sara Belli10, Elena Sebokova10, Karin Conde-Knape10, Anish Konkar10, Daniel J. Drucker9, Vasily Gelfanov3, Paul T. Pfluger1,2,5, Timo D. Müller1,2, Diego Perez-Tilve5, Richard D. DiMarchi3# & Matthias H. Tschöp1,2,5# Nature Medicine: doi:10.1038/nm.3761 Supplemental Results Chemical evolution from co-agonism to tri-agonism The structural and sequence similarities amongst the three hormones (Fig. 1e), coupled with prior structure-function studies1,2, informed the design of sequence hybridized peptides of high potency and balanced mixed agonism. The native hormones share nine conserved amino acids at positions 4, 5, 6, 8, 9, 11, 22, 25, and 26. These residues can be broadly grouped into two regions constituted by amino acids 4-11 and 22-26. The remaining central residues (amino acids 12-21) and the proximal terminal amino acids (1-3 and 27-30) exhibit more diversity that imparts the specificity of receptor interaction with each respective native hormone. Consequently, the challenge here is to maintain the individual affinity of each ligand for its receptor while eliminating the structural elements that convey selective preference for each individual receptor. Or stated differently, the objective here was the identification of a high affinity, promiscuous peptide for these three receptors. -
Protein-Protein Interaction Analysis of Bradykinin Receptor B2 with Bradykinin and Kallidin
J. Chosun Natural Sci. Vol. 10, No. 2 (2017) pp. 74 − 77 https://doi.org/10.13160/ricns.2017.10.2.74 Protein-protein Interaction Analysis of Bradykinin Receptor B2 with Bradykinin and Kallidin Santhosh Kumar Nagarajan1,2 and Thirumurthy Madhavan2† Abstract Bradykinin receptor B2 (B2R) is a GPCR protein which binds with the inflammatory mediator hormone bradkynin. Kallidin, a decapeptide, also signals through this receptor. B2R is crucial in the cross-talk between renin-angiotensin system (RAS) and the kinin-kallikrein system (KKS) and in many processes including vasodilation, edema, smooth muscle spasm and pain fiber stimulation. Thus the structural study of the receptor becomes important. We have predicted the peptide structures of Bradykinin and Kallidin from their amino acid sequences and the structures were docked with the receptor structure. The results obtained from protein-protein docking could be helpful in studying the B2R structural features and in the pathophysiology in various diseases related to it. Keywords: Bradykinin B2 Receptor, GPCR, Bradykinin, Kallidin, Peptide Modeling, Protein-Protein Docking 1. Introduction and Gi helps in inhibiting the adenylate cyclase. Also, the receptor stimulates the mitogen-activated protein Bradykinin is an inflammatory peptide, consisting of kinase pathways[4,5]. B2 receptor involves in the slow nine amino acids. It involves in the contraction of the contraction of various smooth muscles including veins, venous smooth muscle, activation of sensory fibers, intestine, uterus, trachea, and lung. It induces the endo- release of cytokines, proliferation of connective tissue thelium-dependent relaxation of arteries and arterioles. and in the endothelium-dependent vasodilation[1,2]. Kalli- B2R also activates the natriuresis/diuresis in the kid- din, a bioactive kinin, is a decapeptide, having ten ney[6]. -
Supplementary Table 1. Pain and PTSS Associated Genes (N = 604
Supplementary Table 1. Pain and PTSS associated genes (n = 604) compiled from three established pain gene databases (PainNetworks,[61] Algynomics,[52] and PainGenes[42]) and one PTSS gene database (PTSDgene[88]). These genes were used in in silico analyses aimed at identifying miRNA that are predicted to preferentially target this list genes vs. a random set of genes (of the same length). ABCC4 ACE2 ACHE ACPP ACSL1 ADAM11 ADAMTS5 ADCY5 ADCYAP1 ADCYAP1R1 ADM ADORA2A ADORA2B ADRA1A ADRA1B ADRA1D ADRA2A ADRA2C ADRB1 ADRB2 ADRB3 ADRBK1 ADRBK2 AGTR2 ALOX12 ANO1 ANO3 APOE APP AQP1 AQP4 ARL5B ARRB1 ARRB2 ASIC1 ASIC2 ATF1 ATF3 ATF6B ATP1A1 ATP1B3 ATP2B1 ATP6V1A ATP6V1B2 ATP6V1G2 AVPR1A AVPR2 BACE1 BAMBI BDKRB2 BDNF BHLHE22 BTG2 CA8 CACNA1A CACNA1B CACNA1C CACNA1E CACNA1G CACNA1H CACNA2D1 CACNA2D2 CACNA2D3 CACNB3 CACNG2 CALB1 CALCRL CALM2 CAMK2A CAMK2B CAMK4 CAT CCK CCKAR CCKBR CCL2 CCL3 CCL4 CCR1 CCR7 CD274 CD38 CD4 CD40 CDH11 CDK5 CDK5R1 CDKN1A CHRM1 CHRM2 CHRM3 CHRM5 CHRNA5 CHRNA7 CHRNB2 CHRNB4 CHUK CLCN6 CLOCK CNGA3 CNR1 COL11A2 COL9A1 COMT COQ10A CPN1 CPS1 CREB1 CRH CRHBP CRHR1 CRHR2 CRIP2 CRYAA CSF2 CSF2RB CSK CSMD1 CSNK1A1 CSNK1E CTSB CTSS CX3CL1 CXCL5 CXCR3 CXCR4 CYBB CYP19A1 CYP2D6 CYP3A4 DAB1 DAO DBH DBI DICER1 DISC1 DLG2 DLG4 DPCR1 DPP4 DRD1 DRD2 DRD3 DRD4 DRGX DTNBP1 DUSP6 ECE2 EDN1 EDNRA EDNRB EFNB1 EFNB2 EGF EGFR EGR1 EGR3 ENPP2 EPB41L2 EPHB1 EPHB2 EPHB3 EPHB4 EPHB6 EPHX2 ERBB2 ERBB4 EREG ESR1 ESR2 ETV1 EZR F2R F2RL1 F2RL2 FAAH FAM19A4 FGF2 FKBP5 FLOT1 FMR1 FOS FOSB FOSL2 FOXN1 FRMPD4 FSTL1 FYN GABARAPL1 GABBR1 GABBR2 GABRA2 GABRA4 -
Reproductionresearch
REPRODUCTIONRESEARCH Bovine germinal vesicle oocyte and cumulus cell proteomics E Memili1,2, D Peddinti3,4, L A Shack3,4, B Nanduri3,4, F McCarthy3,4, H Sagirkaya1,5 and S C Burgess2,3,4 1Department of Animal and Dairy Sciences, Mississippi State University, Starkville, Mississippi 39762-6100, USA, 2Mississippi Agricultural and Forestry Experiment Station, Starkville, Mississippi 39762, USA, 3College of Veterinary Medicine and 4Institute for Digital Biology, Mississippi State University, Starkville, Mississippi 39762, USA and 5Department of Reproduction and Artificial Insemination, Uludag University Veterinary Faculty, Gorukle-Bursa 16059, Turkey Correspondence should be addressed to E Memili; Email: [email protected] Abstract Germinal vesicle (GV) breakdown is fundamental for maturation of fully grown, developmentally competent, mammalian oocytes. Bidirectional communication between oocytes and surrounding cumulus cells (CC) is essential for maturation of a competent oocyte. However, neither the factors involved in this communication nor the mechanisms of their actions are well defined. Here, we define the proteomes of GV oocytes and their surrounding CC, including membrane proteins, using proteomics in a bovine model. We found that 4395 proteins were expressed in the CC and 1092 proteins were expressed in oocytes. Further, 858 proteins were common to both the CC and the oocytes. This first comprehensive proteome analysis of bovine oocytes and CC not only provides a foundation for signaling and cell physiology at the GV stage of oocyte development, but are also valuable for comparative studies of other stages of oocyte development at the molecular level. Furthermore, some of these proteins may represent molecular biomarkers for developmental potential of oocytes. Reproduction (2007) 133 1107–1120 Introduction periods of protein synthesis; namely, synthesis required for GVBD, MI, MII, and maintenance of MII (Khatir et al. -
Transcriptomes and Neurotransmitter Profiles of Classes of Gustatory And
ARTICLE DOI: 10.1038/s41467-017-01095-1 OPEN Transcriptomes and neurotransmitter profiles of classes of gustatory and somatosensory neurons in the geniculate ganglion Gennady Dvoryanchikov 1, Damian Hernandez1, Jennifer K. Roebber 2, David L. Hill3, Stephen D. Roper 1,2,4 & Nirupa Chaudhari 1,2,4 Taste buds are innervated by neurons whose cell bodies reside in cranial sensory ganglia. Studies on the functional properties and connectivity of these neurons are hindered by the lack of markers to define their molecular identities and classes. The mouse geniculate ganglion contains chemosensory neurons innervating lingual and palatal taste buds and somatosensory neurons innervating the pinna. Here, we report single cell RNA sequencing of geniculate ganglion neurons. Using unbiased transcriptome analyses, we show a pronounced separation between two major clusters which, by anterograde labeling, correspond to gus- tatory and somatosensory neurons. Among the gustatory neurons, three subclusters are present, each with its own complement of transcription factors and neurotransmitter response profiles. The smallest subcluster expresses both gustatory- and mechanosensory- related genes, suggesting a novel type of sensory neuron. We identify several markers to help dissect the functional distinctions among gustatory neurons and address questions regarding target interactions and taste coding. 1 Department of Physiology & Biophysics, University of Miami Miller School of Medicine, Miami, FL 33136, USA. 2 Graduate Program in Neurosciences, University of Miami Miller School of Medicine, Miami, FL 33136, USA. 3 Department of Psychology, University of Virginia, Charlottesville, VA 22904, USA. 4 Department of Otolaryngology, University of Miami Miller School of Medicine, Miami, FL 33136, USA. Gennady Dvoryanchikov and Damian Hernandez contributed equally to the work.