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G Protein-Coupled Receptors
G PROTEIN-COUPLED RECEPTORS Overview:- The completion of the Human Genome Project allowed the identification of a large family of proteins with a common motif of seven groups of 20-24 hydrophobic amino acids arranged as α-helices. Approximately 800 of these seven transmembrane (7TM) receptors have been identified of which over 300 are non-olfactory receptors (see Frederikson et al., 2003; Lagerstrom and Schioth, 2008). Subdivision on the basis of sequence homology allows the definition of rhodopsin, secretin, adhesion, glutamate and Frizzled receptor families. NC-IUPHAR recognizes Classes A, B, and C, which equate to the rhodopsin, secretin, and glutamate receptor families. The nomenclature of 7TM receptors is commonly used interchangeably with G protein-coupled receptors (GPCR), although the former nomenclature recognises signalling of 7TM receptors through pathways not involving G proteins. For example, adiponectin and membrane progestin receptors have some sequence homology to 7TM receptors but signal independently of G-proteins and appear to reside in membranes in an inverted fashion compared to conventional GPCR. Additionally, the NPR-C natriuretic peptide receptor has a single transmembrane domain structure, but appears to couple to G proteins to generate cellular responses. The 300+ non-olfactory GPCR are the targets for the majority of drugs in clinical usage (Overington et al., 2006), although only a minority of these receptors are exploited therapeutically. Signalling through GPCR is enacted by the activation of heterotrimeric GTP-binding proteins (G proteins), made up of α, β and γ subunits, where the α and βγ subunits are responsible for signalling. The α subunit (tabulated below) allows definition of one series of signalling cascades and allows grouping of GPCRs to suggest common cellular, tissue and behavioural responses. -
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. -
GNB2 Rabbit Polyclonal Antibody – TA590202 | Origene
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for TA590202 GNB2 Rabbit Polyclonal Antibody Product data: Product Type: Primary Antibodies Applications: ELISA, IHC, WB Recommended Dilution: WB 1:20000, IHC 1:150,ELISA 1:100-1:2000 Reactivity: Human Host: Rabbit Isotype: IgG Clonality: Polyclonal Immunogen: DNA immunization. This antibody is specific for the N Terminus Region of the target protein. Formulation: 20 mM Potassium Phosphate, 150 mM Sodium Chloride, pH 7.0 Concentration: 0.99197 mg/ml Purification: Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G) Conjugation: Unconjugated Storage: Store at -20°C as received. Stability: Stable for 12 months from date of receipt. Gene Name: G protein subunit beta 2 Database Link: NP_005264 Entrez Gene 2783 Human P62879 Background: Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors. This gene contains a trinucleotide (CCG) repeat length polymorphism in its 5' UTR. Synonyms: beta-2 subunit; G(S); G(T) beta subunit 2; G protein; guanine nucleotide-binding protein; guanine nucleotide-binding protein G(I); OTTHUMP00000174601; OTTHUMP00000174602; signal-transducing guanine nucleotide-binding regulatory protein beta This product is to be used for laboratory only. -
NIH Public Access Author Manuscript Alcohol
NIH Public Access Author Manuscript Alcohol. Author manuscript; available in PMC 2014 November 01. NIH-PA Author ManuscriptPublished NIH-PA Author Manuscript in final edited NIH-PA Author Manuscript form as: Alcohol. 2013 November ; 47(7): . doi:10.1016/j.alcohol.2013.07.002. Stress-response pathways are altered in the hippocampus of chronic alcoholics Jeanette N. McClinticka, Xiaoling Xueia, Jay A. Tischfieldb, Alison Goatec, Tatiana Foroudd, Leah Wetherilld,e, Marissa A. Ehringerf,g, and Howard J. Edenberga,d,* aDepartment of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202, USA bDepartment of Genetics, Rutgers University, Piscataway, NJ 08854, USA cDepartment of Psychiatry, School of Medicine, Washington University in St. Louis, St. Louis, MO 63110, USA dDepartment of Medical and Molecular Genetics, Indiana University School of Medicine, Indianapolis, IN 46202, USA eDepartment of Psychology, IUPUI School of Science, Indianapolis, IN 46202, USA fInstitute for Behavioral Genetics, University of Colorado, Boulder, CO 80309, USA gDepartment of Integrative Physiology, University of Colorado, Boulder, CO 80309, USA Abstract The chronic high-level alcohol consumption seen in alcoholism leads to dramatic effects on the hippocampus, including decreased white matter, loss of oligodendrocytes and other glial cells, and inhibition of neurogenesis. Examining gene expression in post mortem hippocampal tissue from 20 alcoholics and 19 controls allowed us to detect differentially expressed genes that may play a role in the risk for alcoholism or whose expression is modified by chronic consumption of alcohol. We identified 639 named genes whose expression significantly differed between alcoholics and controls at a False Discovery Rate (FDR) ≤ 0.20; 52% of these genes differed by at least 1.2-fold. -
Supplementary Table 1
Up-regulated accession # Development M93275 ADFP, adipose differentiation related protein D43694 MATH-1, homolog of atonal 1 M64068 Bmi-1, zinc finger protein AW124785 Midnolin, midbrain nucleolar protein AI843178 Cla3, Cerebellar ataxia 3 D10712 Nedd1, Neural precursor cell expressed, developmentally down-regulated gene 1 AB011678 Doublecortin, for neurogenesis M57683 mPDGF-alpha-R, PDGF alpha receptor U41626 DSS1, deleted in split hand/split foot 1 homolog (Dss1), for limb development AB010833 PTCH2, patched 2, Mouse homolog of yeast CDC46 NP_034226 Ebf3, early B-cell factor 3 AI846695 Qk, Quaking U63386 Edr1 Early development regulator 1 (homolog of polyhomeotic 1), Mph1 AI043016 Rnf2, Ring finger protein 2 X69942 Enhancer-trap-locus 1, for transcription regulation AF100694 Ruvbl1, Ruv-B like protein 1, DNA helicase AW123618 Fzd2, Frizzled homolog 2 U88566 Sfrp1, secreted frizzled related protein 1 AA681520 Geminin-pending, for embryogenesis and morphogenesis U88567 Sfrp2, secreted frizzled related protein 2 AB025922 Gli1, GLI-Kruppel family member 1 AF089721 Smo, Smoothened X99104 Gli2, GLI-Kruppel family member 2 AF009414 SOX11, SRY-box containing gene 11 U61362 Grg1, groucho-related gene 1, Tle1, transducin-like enhancer of split 1 U85614 SRG3, Smarcc1, SWI/SNF related, matrix associated, action dependent regulator of chromatin, subfamily, member 1 M97506 Hen1, helix-loop-helix protein AI837838 Tmeff1, Transmembrane protein with EGF-like and two follistatin-like domains 1 U79748 Madh4, MAD homolog 4, for transcription regulation -
Hypoxia Transcriptomic Modifications Induced by Proton Irradiation In
Journal of Personalized Medicine Article Hypoxia Transcriptomic Modifications Induced by Proton Irradiation in U87 Glioblastoma Multiforme Cell Line Valentina Bravatà 1,2,† , Walter Tinganelli 3,†, Francesco P. Cammarata 1,2,* , Luigi Minafra 1,2,* , Marco Calvaruso 1,2 , Olga Sokol 3 , Giada Petringa 2, Giuseppe A.P. Cirrone 2, Emanuele Scifoni 4 , Giusi I. Forte 1,2,‡ and Giorgio Russo 1,2,‡ 1 Institute of Molecular Bioimaging and Physiology–National Research Council (IBFM-CNR), 90015 Cefalù, Italy; [email protected] (V.B.); [email protected] (M.C.); [email protected] (G.I.F.); [email protected] (G.R.) 2 Laboratori Nazionali del SUD, Istituto Nazionale di Fisica Nucleare (LNS-INFN), 95100 Catania, Italy; [email protected] (G.P.); [email protected] (G.A.P.C.) 3 Biophysics Department, GSI Helmholtzzentrum für Schwerionenforschung GmbH, 64291 Darmstadt, Germany; [email protected] (W.T.); [email protected] (O.S.) 4 Trento Institute for Fundamental Physics and Applications (TIFPA), Istituto Nazionale Fisica Nucleare (INFN), 38123 Trento, Italy; [email protected] * Correspondence: [email protected] (F.P.C.); [email protected] (L.M.) † These authors contributed equally to this work. ‡ These authors contributed equally to this work. Abstract: In Glioblastoma Multiforme (GBM), hypoxia is associated with radioresistance and poor prognosis. Since standard GBM treatments are not always effective, new strategies are needed Citation: Bravatà, V.; Tinganelli, W.; to overcome resistance to therapeutic treatments, including radiotherapy (RT). Our study aims Cammarata, F.P.; Minafra, L.; to shed light on the biomarker network involved in a hypoxic (0.2% oxygen) GBM cell line that Calvaruso, M.; Sokol, O.; Petringa, G.; is radioresistant after proton therapy (PT). -
Large-Scale Proteomics and Phosphoproteomics of Urinary Exosomes
JASN Express. Published on December 3, 2008 as doi: 10.1681/ASN.2008040406 BASIC RESEARCH www.jasn.org Large-Scale Proteomics and Phosphoproteomics of Urinary Exosomes Patricia A. Gonzales,*† Trairak Pisitkun,* Jason D. Hoffert,* Dmitry Tchapyjnikov,* ʈ Robert A. Star,‡ Robert Kleta,§ ¶ Nam Sun Wang,† and Mark A. Knepper* *Laboratory of Kidney and Electrolyte Metabolism, National Heart, Lung, and Blood Institute, ‡Renal Diagnostics and Therapeutics Unit, National Institute of Diabetes and Digestive and Kidney Diseases, §Section of Human ʈ Biochemical Genetics, Medical Genetics Branch, National Human Genome Research Institute, and Office of Rare Diseases, Office of the Director, National Institutes of Health, Bethesda, and †Department of Chemical and Biomolecular Engineering, University of Maryland, College Park, Maryland; and ¶London Epithelial Group, Centre for Nephrology, University College London, London, United Kingdom ABSTRACT Normal human urine contains large numbers of exosomes, which are 40- to 100-nm vesicles that originate as the internal vesicles in multivesicular bodies from every renal epithelial cell type facing the urinary space. Here, we used LC-MS/MS to profile the proteome of human urinary exosomes. Overall, the analysis identified 1132 proteins unambiguously, including 177 that are represented on the Online Mendelian Inheritance in Man database of disease-related genes, suggesting that exosome analysis is a potential approach to discover urinary biomarkers. We extended the proteomic analysis to phospho- proteomic profiling using neutral loss scanning, and this yielded multiple novel phosphorylation sites, including serine-811 in the thiazide-sensitive Na-Cl co-transporter, NCC. To demonstrate the potential use of exosome analysis to identify a genetic renal disease, we carried out immunoblotting of exosomes from urine samples of patients with a clinical diagnosis of Bartter syndrome type I, showing an absence of the sodium-potassium-chloride co-transporter 2, NKCC2. -
Mrna Expression and DNA Methylation Analysis of The
ONCOLOGY LETTERS 20: 288, 2020 mRNA expression and DNA methylation analysis of the inhibitory mechanism of H2O2 on the proliferation of A549 cells YEPENG LI1, ZHONGHENG WEI1, SHIQING HUANG1 and BO YANG2 1Department of Oncology, 2Key Laboratory of Guangxi College and Universities, Biomedical Research Center, The Affiliated Hospital of Youjiang Medical University for Nationalities, Baise, Guangxi Zhuang Autonomous Region 533000, P.R. China Received October 31, 2019; Accepted August 18, 2020 DOI: 10.3892/ol.2020.12151 Abstract. Reactive oxygen species, particularly hydrogen leading to cell death (2). Lung cancer is one of the most malignant peroxide (H2O2), can induce proliferation inhibition and death tumours in the respiratory tract, and 85% of lung cancer cases are of A549 cells via oxidative stress. Oxidative stress has effect non‑small cell lung cancer (NSCLC) (3). Previous reports have on DNA methylation. Oxidative stress and DNA methylation revealed that H2O2 may inhibit the proliferation of A549 lung feature a common denominator: The one carbon cycle. To cancer cells via oxidative stress (4,5). A recent study demonstrated explore the inhibitory mechanism of H2O2 on the proliferation of that in lung cancer cells treated with H2O2, MAPK inhibitors ‑ lung cancer cells, the present study analysed the mRNA expres‑ (mainly the JNK inhibitor) increased O2 and glutathione deple‑ sion and methylation profiles in A549 cells treated with H2O2 for tion, thus leading to cell death (6). Furthermore, oligomeric 24 h, as adenocarcinoma is the most common pathological type proanthocyanidins have been reported to protect A549 cells from of lung cancer. The DNA methylation profile was constructed oxidative stress induced by H2O2 through the Nrf2‑antioxidant using reduced representation bisulphite sequencing, which iden‑ responsive element signalling pathway (7). -
Supplementary Data
Supplementary Figure 1 Supplementary Figure 2 CCR-10-3244.R1 Supplementary Figure Legends Supplementary Figure 1. B-Myb is overexpressed in primary AML blasts and B-CLL cells. Baseline B-Myb mRNA levels were determined by quantitative RT-PCR, after normalization to the level of housekeeping gene, in primary B-CLL (n=10) and AML (n=5) patient samples, and in normal CD19+ (n=5) and CD34+ (n=4) cell preparations. Each sample was determined in triplicate. Horizontal bars are median, upper and lower edges of box are 75th and 25th percentiles, lines extending from box are 10th and 90th percentiles. Supplementary Figure 2. Cytotoxicity by Nutlin-3 and Chlorambucil used alone or in combination in leukemic cells. The p53wild-type EHEB and SKW6.4 cells lines, and the p53mutated BJAB cell line were exposed to Nutlin-3 or Chlorambucil used either alone or in combination. (Nutl.+Chlor.). In A, upon treatment with Nutlin-3 or Chlorambucil, used either alone (both at 10 μM) or in combination (Nutl.+Chlor.), induction of apoptosis was quantitatively evaluated by Annexin V/PI staining, while E2F1 and pRb protein levels were analyzed by Western blot. Tubulin staining is shown as loading control. The average combination index (CI) values (analyzed by the method of Chou and Talalay) for effects of Chlorambucil+Nutlin-3 on cell viability are shown. ED indicates effect dose. In B, levels of B-Myb and E2F1 mRNA were analyzed by quantitative RT- PCR. Results are expressed as fold of B-Myb and E2F1 modulation in cells treated for 24 hours as indicated, with respect to the control untreated cultures set to 1 (hatched line). -
List of Predicted Circfam120a Target Mrnas Gene in Pathway Species Gene Name
List of predicted circFAM120A target mRNAs Gene in pathway Species Gene name HRAS Homo sapiens HRas proto-oncogene, GTPase (HRAS) ADCY1 Homo sapiens Adenylate cyclase 1 (ADCY1) ADCY2 Homo sapiens Adenylate cyclase 2 (ADCY2) ADCY7 Homo sapiens Adenylate cyclase 7 (ADCY7) PTGS2 Homo sapiens Prostaglandin-endoperoxide synthase 2 (PTGS2) PGF Homo sapiens Placental growth factor (PGF) ADCY5 Homo sapiens Adenylate cyclase 5 (ADCY5) STAT5A Homo sapiens Signal transducer and activator of transcription 5A (STAT5A) ADCY6 Homo sapiens Adenylate cyclase 6 (ADCY6) STAT5B Homo sapiens Signal transducer and activator of transcription 5B (STAT5B) LPAR3 Homo sapiens Lysophosphatidic acid receptor 3 (LPAR3) LPAR2 Homo sapiens Lysophosphatidic acid receptor 2 (LPAR2) CTNNB1 Homo sapiens Catenin beta 1 (CTNNB1) CUL2 Homo sapiens Cullin 2 (CUL2) RARA Homo sapiens Retinoic acid receptor alpha (RARA) GNG2 Homo sapiens G protein subunit gamma 2 (GNG2) RARB Homo sapiens Retinoic acid receptor beta (RARB) GNG3 Homo sapiens G protein subunit gamma 3 (GNG3) FAS Homo sapiens Fas cell surface death receptor (FAS) GNG4 Homo sapiens G protein subunit gamma 4 (GNG4) GNG7 Homo sapiens G protein subunit gamma 7 (GNG7) PIK3CG Homo sapiens Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma (PIK3CG) WNT10B Homo sapiens Wnt family member 10B (WNT10B) BCR Homo sapiens BCR, RhoGEF and GTPase activating protein (BCR) BRAF Homo sapiens B-Raf proto-oncogene, serine/threonine kinase (BRAF) RXRB Homo sapiens Retinoid X receptor beta (RXRB) ROCK2 Homo sapiens Rho -
Supplementary Data
A Suppl. Figure 1 A 1.0 p = 0.0192 0.8 0.6 0.4 Proportion Surviving 0.2 Gain Normal 0.0 0122436486072 Months After Esophagectomy B p = 0.034 Below Median Proportion Surviving Above Median Months After Esophagectomy Suppl. Figure 2 Suppl. Figure 3 Suppl. Figure 4 Suppl. Figure 5 A Score 0 Score 1 Score 2 Score 3 N=25, (22.5% of patients) N=53, (47.7% of patients) N=23, (20.7% of patients) N=10, (9.0% of patients) B 60 50 40 30 % of Patients 20 10 0 1 23 Score SUPPLEMENTARY MATERIAL Supplementary methods: Real-time PCR analysis. Real-time PCR analysis for CDK4 expression was performed in 108 tumors using Assays-on-Demand (AOD, Life technologies Corp, Carlsbad, CA). 88ng of cDNA (RNA equivalents) template was used in each qPCR reaction and assays were performed in triplicate. Quantification of CDK4 expression was measured relative to the geometric mean of five endogenous control genes (HMBS, POLRA, TBP, PGK, UCBH). Network-based analysis. Genes that were differently expressed between CDK6-positive and CDK6- negative samples with a p-value < 0.05 and fold-change >0.5 were identified using limma package from bioconductor (1). Network-based analysis was performed using the functional interaction (FI) network (2). Briefly, this consists of 10956 proteins and more than 200,000 curated functional interactions. We calculated pairwise shortest paths among genes of interest in the FI network, hierarchically clustered them based on the average linkage method, and then selected a cluster containing more than 80% altered genes. -
Gene Profile of Myeloid-Derived Suppressive Cells from the Bone Marrow of Lysosomal Acid Lipase Knock-Out Mice
Gene Profile of Myeloid-Derived Suppressive Cells from the Bone Marrow of Lysosomal Acid Lipase Knock-Out Mice Cong Yan1,2,3, Xinchun Ding1,2,3, Nupur Dasgupta4, Lingyan Wu1,2,3, Hong Du2,3* 1 The Center for Immunobiology, Indiana University School of Medicine, Indianapolis, Indiana, United States of America, 2 IU Simon Cancer Center, Indiana University School of Medicine, Indianapolis, Indiana, United States of America, 3 Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, Indiana, United States of America, 4 Division of Human Genetics, Cincinnati Children’s Hospital Medical Center, Cincinnati, Ohio, United States of America Abstract Background: Lysosomal acid lipase (LAL) controls development and homeostasis of myeloid lineage cells. Loss of the lysosomal acid lipase (LAL) function leads to expansion of myeloid-derived suppressive cells (MDSCs) that cause myeloproliferative neoplasm. Methodology/Principal Findings: Affymetrix GeneChip microarray analysis identified detailed intrinsic defects in Ly6G+ myeloid lineage cells of LAL knock-out (lal2/2) mice. Ingenuity Pathway Analysis revealed activation of the mammalian target of rapamycin (mTOR) signaling, which functions as a nutrient/energy/redox sensor, and controls cell growth, cell cycle entry, cell survival, and cell motility. Loss of the LAL function led to major alteration of large GTPase and small GTPase signal transduction pathways. lal2/2 Ly6G+ myeloid cells in the bone marrow showed substantial increase of cell proliferation in association with up-regulation of cyclin and cyclin-dependent kinase (cdk) genes. The epigenetic microenvironment was significantly changed due to the increased expression of multiple histone cluster genes, centromere protein genes and chromosome modification genes.