GPR56 Regulates VEGF Production and Angiogenesis During Melanoma Progression
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Killer-Like Receptors and GPR56 Progressive Expression Defines Cytokine Production of Human CD4+ Memory T Cells
ARTICLE https://doi.org/10.1038/s41467-019-10018-1 OPEN Killer-like receptors and GPR56 progressive expression defines cytokine production of human CD4+ memory T cells Kim-Long Truong1,7, Stephan Schlickeiser1,2,7, Katrin Vogt1, David Boës1, Katarina Stanko1, Christine Appelt1, Mathias Streitz1, Gerald Grütz1,2, Nadja Stobutzki1, Christian Meisel1, Christina Iwert1, Stefan Tomiuk3, Julia K. Polansky2,4, Andreas Pascher5, Nina Babel2,6, Ulrik Stervbo 6, Igor Sauer 5, Undine Gerlach5 & Birgit Sawitzki1,2 1234567890():,; All memory T cells mount an accelerated response on antigen reencounter, but significant functional heterogeneity is present within the respective memory T-cell subsets as defined by CCR7 and CD45RA expression, thereby warranting further stratification. Here we show that several surface markers, including KLRB1, KLRG1, GPR56, and KLRF1, help define low, high, or exhausted cytokine producers within human peripheral and intrahepatic CD4+ memory T-cell populations. Highest simultaneous production of TNF and IFN-γ is observed in KLRB1+KLRG1+GPR56+ CD4 T cells. By contrast, KLRF1 expression is associated with T-cell exhaustion and reduced TNF/IFN-γ production. Lastly, TCRβ repertoire analysis and in vitro differentiation support a regulated, progressive expression for these markers during CD4+ memory T-cell differentiation. Our results thus help refine the classification of human memory T cells to provide insights on inflammatory disease progression and immunotherapy development. 1 Institute of Medical Immunology, Charité – Universitätsmedizin Berlin, Freie Universität Berlin, Humboldt-Universität zu Berlin and Berlin Institute of Health, 13353 Berlin, Germany. 2 Berlin-Brandenburg Center for Regenerative Therapies (BCRT), Charité – Universitätsmedizin Berlin, 13353 Berlin, Germany. 3 Milteny Biotec GmbH, 51429 Bergisch Gladbach, Germany. -
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, -
Progastrin Production Transitions from Bmi1+/Prox1+ to Lgr5high Cells During Early Intestinal Tumorigenesis Julie Giraud, M
Progastrin production transitions from Bmi1+/Prox1+ to Lgr5high cells during early intestinal tumorigenesis Julie Giraud, M. Foroutan, Jihane Boubaker-Vitre, Fanny Grillet, Z. Homayed, U. Jadhav, Philippe Crespy, Cyril Breuker, J-F. Bourgaux, J. Hazerbroucq, et al. To cite this version: Julie Giraud, M. Foroutan, Jihane Boubaker-Vitre, Fanny Grillet, Z. Homayed, et al.. Progastrin production transitions from Bmi1+/Prox1+ to Lgr5high cells during early intestinal tumorigene- sis. Translational Oncology, Elsevier, 2020, 14 (2), pp.101001. 10.1016/j.tranon.2020.101001. hal- 03090781 HAL Id: hal-03090781 https://hal.archives-ouvertes.fr/hal-03090781 Submitted on 12 Jan 2021 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Distributed under a Creative Commons Attribution - NonCommercial - NoDerivatives| 4.0 International License Translational Oncology 14 (2021) 101001 Contents lists available at ScienceDirect Translational Oncology journal homepage: www.elsevier.com/locate/tranon Original Research + + high Progastrin production transitions from Bmi1 /Prox1 to Lgr5 cells during early intestinal tumorigenesis J. Giraud a, M. Foroutan b,c,1, J. Boubaker-Vitre a,1, F. Grillet a, Z. Homayed a, U. Jadhav d, P. Crespy a, C. Breuker a, J-F. -
Pancancer Progression Human Vjune2017
Gene Symbol Accession Alias/Prev Symbol Official Full Name AAMP NM_001087.3 - angio-associated, migratory cell protein ABI3BP NM_015429.3 NESHBP|TARSH ABI family, member 3 (NESH) binding protein ACHE NM_000665.3 ACEE|ARACHE|N-ACHE|YT acetylcholinesterase ACTG2 NM_001615.3 ACT|ACTA3|ACTE|ACTL3|ACTSG actin, gamma 2, smooth muscle, enteric ACVR1 NM_001105.2 ACTRI|ACVR1A|ACVRLK2|ALK2|FOP|SKR1|TSRI activin A receptor, type I ACVR1C NM_145259.2 ACVRLK7|ALK7 activin A receptor, type IC ACVRL1 NM_000020.1 ACVRLK1|ALK-1|ALK1|HHT|HHT2|ORW2|SKR3|TSR-I activin A receptor type II-like 1 ADAM15 NM_207195.1 MDC15 ADAM metallopeptidase domain 15 ADAM17 NM_003183.4 ADAM18|CD156B|CSVP|NISBD|TACE ADAM metallopeptidase domain 17 ADAM28 NM_014265.4 ADAM 28|ADAM23|MDC-L|MDC-Lm|MDC-Ls|MDCL|eMDC II|eMDCII ADAM metallopeptidase domain 28 ADAM8 NM_001109.4 CD156|MS2 ADAM metallopeptidase domain 8 ADAM9 NM_001005845.1 CORD9|MCMP|MDC9|Mltng ADAM metallopeptidase domain 9 ADAMTS1 NM_006988.3 C3-C5|METH1 ADAM metallopeptidase with thrombospondin type 1 motif, 1 ADAMTS12 NM_030955.2 PRO4389 ADAM metallopeptidase with thrombospondin type 1 motif, 12 ADAMTS8 NM_007037.4 ADAM-TS8|METH2 ADAM metallopeptidase with thrombospondin type 1 motif, 8 ADAP1 NM_006869.2 CENTA1|GCS1L|p42IP4 ArfGAP with dual PH domains 1 ADD1 NM_001119.4 ADDA adducin 1 (alpha) ADM2 NM_001253845.1 AM2|dJ579N16.4 adrenomedullin 2 ADRA2B NM_000682.4 ADRA2L1|ADRA2RL1|ADRARL1|ALPHA2BAR|alpha-2BAR adrenoceptor alpha 2B AEBP1 NM_001129.3 ACLP AE binding protein 1 AGGF1 NM_018046.3 GPATC7|GPATCH7|HSU84971|HUS84971|VG5Q -
The N-Terminus of the Saccharomyces Cerevisiae G Protein-Coupled Receptor Ste2p: Formation of Dimer Interfaces and Negative Regulation
University of Tennessee, Knoxville TRACE: Tennessee Research and Creative Exchange Doctoral Dissertations Graduate School 8-2013 The N-terminus of the Saccharomyces cerevisiae G protein- coupled receptor Ste2p: formation of dimer interfaces and negative regulation Mohammad Seraj Uddin [email protected] Follow this and additional works at: https://trace.tennessee.edu/utk_graddiss Part of the Biochemistry Commons, Molecular Biology Commons, and the Structural Biology Commons Recommended Citation Uddin, Mohammad Seraj, "The N-terminus of the Saccharomyces cerevisiae G protein-coupled receptor Ste2p: formation of dimer interfaces and negative regulation. " PhD diss., University of Tennessee, 2013. https://trace.tennessee.edu/utk_graddiss/2490 This Dissertation is brought to you for free and open access by the Graduate School at TRACE: Tennessee Research and Creative Exchange. It has been accepted for inclusion in Doctoral Dissertations by an authorized administrator of TRACE: Tennessee Research and Creative Exchange. For more information, please contact [email protected]. To the Graduate Council: I am submitting herewith a dissertation written by Mohammad Seraj Uddin entitled "The N- terminus of the Saccharomyces cerevisiae G protein-coupled receptor Ste2p: formation of dimer interfaces and negative regulation." I have examined the final electronic copy of this dissertation for form and content and recommend that it be accepted in partial fulfillment of the requirements for the degree of Doctor of Philosophy, with a major in Microbiology. Jeffrey -
An Overview on G Protein-Coupled Receptor-Induced Signal Transduction in Acute Myeloid Leukemia
An overview on G protein-coupled receptor-induced signal transduction in Acute Myeloid Leukemia 1* 1,3 4,5,6 2* Frode Selheim , Elise Aasebø , Catalina Ribas and Anna M. Aragay 1The Proteomics Unit at the University of Bergen, Department of Biomedicine, University of Bergen, Jonas Lies vei 91, 5020 Bergen, Norway; 3 Department of Clinical Science, University of Bergen, Jonas Lies vei 87, 5021 Bergen, Norway; [email protected]. 2Departamento de Biologia Celular. Instituto de Biología Molecular de Barcelona (IBMB-CSIC), Spanish National Research Council (CSIC), Baldiri i Reixac, 15, 08028 Barcelona, Spain; [email protected]. 4Departamento de Biología Molecular and Centro de Biología Molecular “Severo Ochoa” (UAM-CSIC), 28049 Madrid, Spain; 5Instituto de Investigación Sanitaria La Princesa, 28006 Madrid, Spain; 6CIBER de Enfermedades Cardiovasculares, ISCIII (CIBERCV), 28029 Madrid, Spain, [email protected] * Corresponding authors: Frode Selheim Adr: Jonas Lies vei 91, 5020 Bergen, Norway Email: [email protected], Tel:+4755586091 Anna M. Aragay Adr: Baldiri i Reixac, 15, 08028 Barcelona. Spain. E-mail: [email protected]; Tel.: +934098671 1 Abstract Background: Acute myeloid leukemia (AML) is a genetically heterogeneous disease characterized by uncontrolled proliferation of precursor myeloid-lineage cells in the bone marrow. AML is also characterized with patients with poor long-term survival outcomes due to relapse. Many efforts have been made to understand the biological heterogeneity of AML and the challenges to develop new therapies are therefore enormous. G protein-coupled receptors (GPCRs) are a large attractive drug targeted family of transmembrane proteins, and aberrant GPCR expression and GPCR-mediated signaling have been implicated in leukemogenesis of AML. -
The Adhesion G Protein-Coupled Receptor GPR56 Is a Cell-Autonomous Regulator of Oligodendrocyte Development
ARTICLE Received 27 May 2014 | Accepted 14 Dec 2014 | Published 21 Jan 2015 DOI: 10.1038/ncomms7121 OPEN The adhesion G protein-coupled receptor GPR56 is a cell-autonomous regulator of oligodendrocyte development Stefanie Giera1,*, Yiyu Deng1,*,w, Rong Luo1,*, Sarah D. Ackerman2, Amit Mogha2, Kelly R. Monk2,3, Yanqin Ying1, Sung-Jin Jeong1,w, Manabu Makinodan4,5, Allison R. Bialas4,5, Bernard S. Chang6, Beth Stevens4,5, Gabriel Corfas4,5,w & Xianhua Piao1 Mutations in GPR56, a member of the adhesion G protein-coupled receptor family, cause a human brain malformation called bilateral frontoparietal polymicrogyria (BFPP). Magnetic resonance imaging (MRI) of BFPP brains reveals myelination defects in addition to brain malformation. However, the cellular role of GPR56 in oligodendrocyte development remains unknown. Here, we demonstrate that loss of Gpr56 leads to hypomyelination of the central nervous system in mice. GPR56 levels are abundant throughout early stages of oligodendrocyte development, but are downregulated in myelinating oligodendrocytes. Gpr56-knockout mice manifest with decreased oligodendrocyte precursor cell (OPC) proliferation and diminished levels of active RhoA, leading to fewer mature oligodendrocytes and a reduced number of myelinated axons in the corpus callosum and optic nerves. Conditional ablation of Gpr56 in OPCs leads to a reduced number of mature oligodendrocytes as seen in constitutive knockout of Gpr56. Together, our data define GPR56 as a cell-autonomous regulator of oligodendrocyte development. 1 Division of Newborn Medicine, Department of Medicine, Boston Children’s Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA. 2 Department of Developmental Biology, Washington University School of Medicine, St Louis, Missouri 63110, USA. -
Multi-Functionality of Proteins Involved in GPCR and G Protein Signaling: Making Sense of Structure–Function Continuum with In
Cellular and Molecular Life Sciences (2019) 76:4461–4492 https://doi.org/10.1007/s00018-019-03276-1 Cellular andMolecular Life Sciences REVIEW Multi‑functionality of proteins involved in GPCR and G protein signaling: making sense of structure–function continuum with intrinsic disorder‑based proteoforms Alexander V. Fonin1 · April L. Darling2 · Irina M. Kuznetsova1 · Konstantin K. Turoverov1,3 · Vladimir N. Uversky2,4 Received: 5 August 2019 / Revised: 5 August 2019 / Accepted: 12 August 2019 / Published online: 19 August 2019 © Springer Nature Switzerland AG 2019 Abstract GPCR–G protein signaling system recognizes a multitude of extracellular ligands and triggers a variety of intracellular signal- ing cascades in response. In humans, this system includes more than 800 various GPCRs and a large set of heterotrimeric G proteins. Complexity of this system goes far beyond a multitude of pair-wise ligand–GPCR and GPCR–G protein interactions. In fact, one GPCR can recognize more than one extracellular signal and interact with more than one G protein. Furthermore, one ligand can activate more than one GPCR, and multiple GPCRs can couple to the same G protein. This defnes an intricate multifunctionality of this important signaling system. Here, we show that the multifunctionality of GPCR–G protein system represents an illustrative example of the protein structure–function continuum, where structures of the involved proteins represent a complex mosaic of diferently folded regions (foldons, non-foldons, unfoldons, semi-foldons, and inducible foldons). The functionality of resulting highly dynamic conformational ensembles is fne-tuned by various post-translational modifcations and alternative splicing, and such ensembles can undergo dramatic changes at interaction with their specifc partners. -
The Functional Roles of Ph-Sensing G Protein
The Functional Roles of pH-sensing G protein-coupled receptors in Intestinal Inflammation by Edward Joseph Sanderlin November, 2018 Director of Dissertation: Li Yang, PhD Department: Internal Medicine The inflammatory microenvironment in inflammatory bowel disease (IBD) is complex, replete with microbial byproducts, complement, leukocytes, and resulting inflammatory cytokines. Parallel to these microenvironmental factors are protons, which are produced in excess due to altered metabolism of infiltrated leukocytes and local ischemia. Immune cells and intestinal microvasculature exist in the acidic, inflamed microenvironment and in turn alter their function in response to the acidic pH. Currently, only little is known how cells sense extracellular acidity and subsequently alter the inflammatory response. Recently, a class of proton-sensing G protein- coupled receptors (GPCRs) have emerged as functional pH-sensors, expressed in either leukocytes or vasculature, and are capable of altering immune cell inflammatory programs in response to acidic pH. These family members include GPR4, OGR1 (GPR68), TDAG8 (GPR65), and G2A (GPR132). Our group has uncovered a novel role for GPR4 in mediating endothelial cell (EC) inflammation in response to acidic pH. GPR4 activation in ECs have resulted in increased vascular adhesion molecule expression and functionally mediates leukocyte-EC interactions which are essential for the leukocyte extravasation process. Proton-sensors GPR65 and GPR68, however, are not expressed in ECs but are highly expressed in myeloid and lymphoid cells. GPR65 and GPR68, therefore, has been shown to mediate both pro- and anti-inflammatory responses in leukocytes in response to acidic pH. GPR132, however, has been described as a promiscuous GPCR, capable of responding to protons, bioactive lipids, and oxidized free fatty acids. -
Adhesion G Protein-Coupled Receptors
1521-0111/88/3/617–623$25.00 http://dx.doi.org/10.1124/mol.115.098749 MOLECULAR PHARMACOLOGY Mol Pharmacol 88:617–623, September 2015 Copyright ª 2015 by The American Society for Pharmacology and Experimental Therapeutics MINIREVIEW—EXPLORING THE BIOLOGY OF GPCRS: FROM IN VITRO TO IN VIVO Adhesion G Protein–Coupled Receptors: From In Vitro Pharmacology to In Vivo Mechanisms Kelly R. Monk, Jörg Hamann, Tobias Langenhan, Saskia Nijmeijer, Torsten Schöneberg, and Ines Liebscher Downloaded from Department of Developmental Biology, Washington University School of Medicine, St. Louis, Missouri (K.R.M.); Department of Experimental Immunology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands (J.H.); Department of Neurophysiology, Institute of Physiology, University of Würzburg, Würzburg, Germany (T.L.); Department of Medicinal Chemistry/Amsterdam Institute for Molecules, Medicines and Systems, VU University, Amsterdam, The Netherlands (S.N.); and Institute of Biochemistry, Molecular Biochemistry, Medical Faculty, University of Leipzig, Leipzig, Germany (T.S., I.L.) Received February 27, 2015; accepted May 8, 2015 molpharm.aspetjournals.org ABSTRACT The adhesion family of G protein–coupled receptors (aGPCRs) we present an overview of our current knowledge on aGPCR comprises 33 members in humans. aGPCRs are characterized activation and signal transduction with a focus on the latest by their enormous size and complex modular structures. While findings regarding the interplay between ligand binding, me- the physiologic importance of many aGPCRs has been clearly chanical force, and the tethered agonistic Stachel sequence, as demonstrated in recent years, the underlying molecular func- well as implications on translational approaches that may derive tions have only recently begun to be elucidated. -
Anti-GPR56 Monoclonal Antibody Potentiates GPR56-Mediated Src-Fak Signaling to Modulate Cell Adhesion
bioRxiv preprint doi: https://doi.org/10.1101/2020.05.11.089177; this version posted May 13, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Anti-GPR56 monoclonal antibody potentiates GPR56-mediated Src-Fak signaling to modulate cell adhesion Treena Chatterjee1, Sheng Zhang1, Tressie A. Posey1, Ling Wu1, Wangsheng Yu1, Qingyun J. Liu1, and Kendra S. Carmon1* 1The Brown Foundation Institute of Molecular Medicine and Center for Translational Cancer Research, University of Texas Health Science Center at Houston, Houston, TX *Corresponding Author: Kendra S. Carmon, Brown Foundation Institute of Molecular Medicine, University of Texas Health Science Center at Houston, 1825 Pressler St., Houston, TX 77030 Email: [email protected] ORCID: 0000-0002-3244-6096 Running Title: GPR56 activates Src-Fak adhesion signaling Keywords: GPR56, ADGRG1, G protein‐coupled receptor (GPCR), monoclonal antibody, Src, focal adhesion kinase (Fak), paxillin, cell adhesion, colorectal cancer (CRC) 1 bioRxiv preprint doi: https://doi.org/10.1101/2020.05.11.089177; this version posted May 13, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Abstract immune function (2), maintenance of hematopoietic stem cells (3), and oligodendrocyte GPR56, also known as ADGRG1, is a member of and cortex development (4-7). Mutations in GPR56 the adhesion G protein-coupled receptor (aGPCR) have been associated with bilateral frontoparietal family shown to play important roles in cell polymicogyria (BFPP), a disorder characterized by adhesion, brain development, immune system a disruption in the organization of the frontal cortex function, and tumorigenesis. -
Adenylyl Cyclase 2 Selectively Regulates IL-6 Expression in Human Bronchial Smooth Muscle Cells Amy Sue Bogard University of Tennessee Health Science Center
University of Tennessee Health Science Center UTHSC Digital Commons Theses and Dissertations (ETD) College of Graduate Health Sciences 12-2013 Adenylyl Cyclase 2 Selectively Regulates IL-6 Expression in Human Bronchial Smooth Muscle Cells Amy Sue Bogard University of Tennessee Health Science Center Follow this and additional works at: https://dc.uthsc.edu/dissertations Part of the Medical Cell Biology Commons, and the Medical Molecular Biology Commons Recommended Citation Bogard, Amy Sue , "Adenylyl Cyclase 2 Selectively Regulates IL-6 Expression in Human Bronchial Smooth Muscle Cells" (2013). Theses and Dissertations (ETD). Paper 330. http://dx.doi.org/10.21007/etd.cghs.2013.0029. This Dissertation is brought to you for free and open access by the College of Graduate Health Sciences at UTHSC Digital Commons. It has been accepted for inclusion in Theses and Dissertations (ETD) by an authorized administrator of UTHSC Digital Commons. For more information, please contact [email protected]. Adenylyl Cyclase 2 Selectively Regulates IL-6 Expression in Human Bronchial Smooth Muscle Cells Document Type Dissertation Degree Name Doctor of Philosophy (PhD) Program Biomedical Sciences Track Molecular Therapeutics and Cell Signaling Research Advisor Rennolds Ostrom, Ph.D. Committee Elizabeth Fitzpatrick, Ph.D. Edwards Park, Ph.D. Steven Tavalin, Ph.D. Christopher Waters, Ph.D. DOI 10.21007/etd.cghs.2013.0029 Comments Six month embargo expired June 2014 This dissertation is available at UTHSC Digital Commons: https://dc.uthsc.edu/dissertations/330 Adenylyl Cyclase 2 Selectively Regulates IL-6 Expression in Human Bronchial Smooth Muscle Cells A Dissertation Presented for The Graduate Studies Council The University of Tennessee Health Science Center In Partial Fulfillment Of the Requirements for the Degree Doctor of Philosophy From The University of Tennessee By Amy Sue Bogard December 2013 Copyright © 2013 by Amy Sue Bogard.