List of Four Hundred and Twenty Variant Proteins Identified
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Faith and the Human Genome
Plenary Presenters Faith and the Human Genome Faith and the Human Genome Francis S. Collins Despite the best efforts of the American Scientific Affiliation to bridge the gap between science and faith, few gatherings of scientists involved in biology include any meaningful discussion about the spiritual significance of the current revolution in genetics and genomics. Most biologists and geneticists seem to have concluded that science and faith are incompatible, but few who embrace that conclusion seem to have seriously considered the evidence. From my perspective as director of the Human Genome Project, the scientific and religious world views are not only compatible but also inherently complementary. Hence the profound polarization of the scientific and religious perspectives, now glaringly apparent in the fields of biology and genetics, is a source of great distress. Hard-liners in either camp paint increasingly uncompromising pictures that force sincere seekers to choose one view over the other. How all of this must break God’s heart! The elegance and complexity of the human genome is a source of profound wonder. That wonder only strengthens my faith, as it provides glimpses of aspects of From my humanity, which God has known all along, but which we are just now beginning to discover. perspective as e are just on the edge of a whole You made him a little lower than the heav- director of the Whost of developments spurred on enly beings and crowned him with glory by genetics that are going to and honor. You made him ruler over the Human require careful and deliberative thought. -
Propranolol-Mediated Attenuation of MMP-9 Excretion in Infants with Hemangiomas
Supplementary Online Content Thaivalappil S, Bauman N, Saieg A, Movius E, Brown KJ, Preciado D. Propranolol-mediated attenuation of MMP-9 excretion in infants with hemangiomas. JAMA Otolaryngol Head Neck Surg. doi:10.1001/jamaoto.2013.4773 eTable. List of All of the Proteins Identified by Proteomics This supplementary material has been provided by the authors to give readers additional information about their work. © 2013 American Medical Association. All rights reserved. Downloaded From: https://jamanetwork.com/ on 10/01/2021 eTable. List of All of the Proteins Identified by Proteomics Protein Name Prop 12 mo/4 Pred 12 mo/4 Δ Prop to Pred mo mo Myeloperoxidase OS=Homo sapiens GN=MPO 26.00 143.00 ‐117.00 Lactotransferrin OS=Homo sapiens GN=LTF 114.00 205.50 ‐91.50 Matrix metalloproteinase‐9 OS=Homo sapiens GN=MMP9 5.00 36.00 ‐31.00 Neutrophil elastase OS=Homo sapiens GN=ELANE 24.00 48.00 ‐24.00 Bleomycin hydrolase OS=Homo sapiens GN=BLMH 3.00 25.00 ‐22.00 CAP7_HUMAN Azurocidin OS=Homo sapiens GN=AZU1 PE=1 SV=3 4.00 26.00 ‐22.00 S10A8_HUMAN Protein S100‐A8 OS=Homo sapiens GN=S100A8 PE=1 14.67 30.50 ‐15.83 SV=1 IL1F9_HUMAN Interleukin‐1 family member 9 OS=Homo sapiens 1.00 15.00 ‐14.00 GN=IL1F9 PE=1 SV=1 MUC5B_HUMAN Mucin‐5B OS=Homo sapiens GN=MUC5B PE=1 SV=3 2.00 14.00 ‐12.00 MUC4_HUMAN Mucin‐4 OS=Homo sapiens GN=MUC4 PE=1 SV=3 1.00 12.00 ‐11.00 HRG_HUMAN Histidine‐rich glycoprotein OS=Homo sapiens GN=HRG 1.00 12.00 ‐11.00 PE=1 SV=1 TKT_HUMAN Transketolase OS=Homo sapiens GN=TKT PE=1 SV=3 17.00 28.00 ‐11.00 CATG_HUMAN Cathepsin G OS=Homo -
Eradication of ENO1-Deleted Glioblastoma Through Collateral Lethality
bioRxiv preprint doi: https://doi.org/10.1101/331538; this version posted May 25, 2018. 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. Eradication of ENO1-deleted Glioblastoma through Collateral Lethality Yu-Hsi Lin1, Nikunj Satani1,2, Naima Hammoudi1, Jeffrey J. Ackroyd1, Sunada Khadka1, Victoria C. Yan1, Dimitra K. Georgiou1, Yuting Sun3, Rafal Zielinski4, Theresa Tran1, Susana Castro Pando1, Xiaobo Wang1, David Maxwell5, Zhenghong Peng6, Federica Pisaneschi1, Pijus Mandal7, Paul G. Leonard8, Quanyu Xu,9 Qi Wu9, Yongying Jiang9, Barbara Czako10, Zhijun Kang10, John M. Asara11, Waldemar Priebe4, William Bornmann12, Joseph R. Marszalek3, Ronald A. DePinho13 and Florian L. Muller#1 1) Department of Cancer Systems Imaging, The University of Texas MD Anderson Cancer Center, Houston, TX 77054 2) Institute of Stroke and Cerebrovascular Disease, The University of Texas Health Science Center at Houston, TX 77030 3) Center for Co-Clinical Trials, The University of Texas MD Anderson Cancer Center, Houston, TX 77054 4) Department of Experimental Therapeutics, The University of Texas MD Anderson Cancer Center, Houston, TX 77054 5) Institutional Analytics & Informatics, The University of Texas MD Anderson Cancer Center, Houston, TX 77030 6) Cardtronics, Inc., Houston, TX 77042 7) Department of Genomic Medicine, The University of Texas MD Anderson Cancer Center, Houston, TX 77054 bioRxiv preprint doi: https://doi.org/10.1101/331538; this version posted May 25, 2018. 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. -
DF6216-CSRP1 Antibody
Affinity Biosciences website:www.affbiotech.com order:[email protected] CSRP1 Antibody Cat.#: DF6216 Concn.: 1mg/ml Mol.Wt.: 21kDa Size: 50ul,100ul,200ul Source: Rabbit Clonality: Polyclonal Application: WB 1:500-1:2000, IHC 1:50-1:200, ELISA(peptide) 1:20000-1:40000 *The optimal dilutions should be determined by the end user. Reactivity: Human,Mouse,Rat Purification: The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific). Specificity: CSRP1 Antibody detects endogenous levels of total CSRP1. Immunogen: A synthesized peptide derived from human CSRP1, corresponding to a region within the internal amino acids. Uniprot: P21291 Description: This gene encodes a member of the cysteine-rich protein (CSRP) family. This gene family includes a group of LIM domain proteins, which may be involved in regulatory processes important for development and cellular differentiation. The LIM/double zinc-finger motif found in this gene product occurs in proteins with critical functions in gene regulation, cell growth, and somatic differentiation. Alternatively spliced transcript variants have been described. [provided by RefSeq, Aug 2010] Storage Condition and Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM Buffer: NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt. Western blot analysis of CSRP1 expression in Mouse lung lysate 1 / 2 Affinity Biosciences website:www.affbiotech.com order:[email protected] DF6216 at 1/100 staining Mouse brain tissue by IHC-P. The sample was formaldehyde fixed and a heat mediated antigen retrieval step in citrate buffer was performed. -
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, -
Plakophilin-2 Haploinsufficiency Causes Calcium Handling
International Journal of Molecular Sciences Article Plakophilin-2 Haploinsufficiency Causes Calcium Handling Deficits and Modulates the Cardiac Response Towards Stress Chantal J.M. van Opbergen 1 , Maartje Noorman 1, Anna Pfenniger 2, Jaël S. Copier 1, Sarah H. Vermij 2,3 , Zhen Li 2, Roel van der Nagel 1, Mingliang Zhang 2, Jacques M.T. de Bakker 1,4, Aaron M. Glass 5, Peter J. Mohler 6,7, Steven M. Taffet 5, Marc A. Vos 1, Harold V.M. van Rijen 1, Mario Delmar 2 and Toon A.B. van Veen 1,* 1 Department of Medical Physiology, Division of Heart & Lungs, University Medical Center Utrecht, Yalelaan 50, 3584CM Utrecht, The Netherlands 2 Division of Cardiology, NYU School of Medicine, New York, NY 10016, USA 3 Institute of Biochemistry and Molecular Medicine, University of Bern, 3012 Bern, Switzerland 4 Department of Medical Biology, Academic Medical Center Amsterdam, 1105AZ Amsterdam, The Netherlands 5 Department of Microbiology and Immunology, SUNY Upstate Medical University, Syracuse, NY 13210, USA 6 Dorothy M. Davis Heart and Lung Research Institute, The Ohio State University College of Medicine and Wexner Medical Center, Columbus, OH 43210, USA 7 Departments of Physiology & Cell Biology and Internal Medicine, Division of Cardiovascular Medicine, The Ohio State University College of Medicine Wexner Medical Center, Columbus, OH 43210, USA * Correspondence: [email protected] Received: 1 August 2019; Accepted: 19 August 2019; Published: 21 August 2019 Abstract: Human variants in plakophilin-2 (PKP2) associate with most cases of familial arrhythmogenic cardiomyopathy (ACM). Recent studies show that PKP2 not only maintains intercellular coupling, but also regulates transcription of genes involved in Ca2+ cycling and cardiac rhythm. -
Growth and Molecular Profile of Lung Cancer Cells Expressing Ectopic LKB1: Down-Regulation of the Phosphatidylinositol 3-Phosphate Kinase/PTEN Pathway1
[CANCER RESEARCH 63, 1382–1388, March 15, 2003] Growth and Molecular Profile of Lung Cancer Cells Expressing Ectopic LKB1: Down-Regulation of the Phosphatidylinositol 3-Phosphate Kinase/PTEN Pathway1 Ana I. Jimenez, Paloma Fernandez, Orlando Dominguez, Ana Dopazo, and Montserrat Sanchez-Cespedes2 Molecular Pathology Program [A. I. J., P. F., M. S-C.], Genomics Unit [O. D.], and Microarray Analysis Unit [A. D.], Spanish National Cancer Center, 28029 Madrid, Spain ABSTRACT the cell cycle in G1 (8, 9). However, the intrinsic mechanism by which LKB1 activity is regulated in cells and how it leads to the suppression Germ-line mutations in LKB1 gene cause the Peutz-Jeghers syndrome of cell growth is still unknown. It has been proposed that growth (PJS), a genetic disease with increased risk of malignancies. Recently, suppression by LKB1 is mediated through p21 in a p53-dependent LKB1-inactivating mutations have been identified in one-third of sporadic lung adenocarcinomas, indicating that LKB1 gene inactivation is critical in mechanism (7). In addition, it has been observed that LKB1 binds to tumors other than those of the PJS syndrome. However, the in vivo brahma-related gene 1 protein (BRG1) and this interaction is required substrates of LKB1 and its role in cancer development have not been for BRG1-induced growth arrest (10). Similar to what happens in the completely elucidated. Here we show that overexpression of wild-type PJS, Lkb1 heterozygous knockout mice show gastrointestinal hamar- LKB1 protein in A549 lung adenocarcinomas cells leads to cell-growth tomatous polyposis and frequent hepatocellular carcinomas (11, 12). suppression. To examine changes in gene expression profiles subsequent to Interestingly, the hamartomas, but not the malignant tumors, arising in exogenous wild-type LKB1 in A549 cells, we used cDNA microarrays. -
Macropinocytosis Requires Gal-3 in a Subset of Patient-Derived Glioblastoma Stem Cells
ARTICLE https://doi.org/10.1038/s42003-021-02258-z OPEN Macropinocytosis requires Gal-3 in a subset of patient-derived glioblastoma stem cells Laetitia Seguin1,8, Soline Odouard2,8, Francesca Corlazzoli 2,8, Sarah Al Haddad2, Laurine Moindrot2, Marta Calvo Tardón3, Mayra Yebra4, Alexey Koval5, Eliana Marinari2, Viviane Bes3, Alexandre Guérin 6, Mathilde Allard2, Sten Ilmjärv6, Vladimir L. Katanaev 5, Paul R. Walker3, Karl-Heinz Krause6, Valérie Dutoit2, ✉ Jann N. Sarkaria 7, Pierre-Yves Dietrich2 & Érika Cosset 2 Recently, we involved the carbohydrate-binding protein Galectin-3 (Gal-3) as a druggable target for KRAS-mutant-addicted lung and pancreatic cancers. Here, using glioblastoma patient-derived stem cells (GSCs), we identify and characterize a subset of Gal-3high glio- 1234567890():,; blastoma (GBM) tumors mainly within the mesenchymal subtype that are addicted to Gal-3- mediated macropinocytosis. Using both genetic and pharmacologic inhibition of Gal-3, we showed a significant decrease of GSC macropinocytosis activity, cell survival and invasion, in vitro and in vivo. Mechanistically, we demonstrate that Gal-3 binds to RAB10, a member of the RAS superfamily of small GTPases, and β1 integrin, which are both required for macro- pinocytosis activity and cell survival. Finally, by defining a Gal-3/macropinocytosis molecular signature, we could predict sensitivity to this dependency pathway and provide proof-of- principle for innovative therapeutic strategies to exploit this Achilles’ heel for a significant and unique subset of GBM patients. 1 University Côte d’Azur, CNRS UMR7284, INSERM U1081, Institute for Research on Cancer and Aging (IRCAN), Nice, France. 2 Laboratory of Tumor Immunology, Department of Oncology, Center for Translational Research in Onco-Hematology, Swiss Cancer Center Léman (SCCL), Geneva University Hospitals, University of Geneva, Geneva, Switzerland. -
Screening and Identification of Hub Genes in Bladder Cancer by Bioinformatics Analysis and KIF11 Is a Potential Prognostic Biomarker
ONCOLOGY LETTERS 21: 205, 2021 Screening and identification of hub genes in bladder cancer by bioinformatics analysis and KIF11 is a potential prognostic biomarker XIAO‑CONG MO1,2*, ZI‑TONG ZHANG1,3*, MENG‑JIA SONG1,2, ZI‑QI ZHOU1,2, JIAN‑XIONG ZENG1,2, YU‑FEI DU1,2, FENG‑ZE SUN1,2, JIE‑YING YANG1,2, JUN‑YI HE1,2, YUE HUANG1,2, JIAN‑CHUAN XIA1,2 and DE‑SHENG WENG1,2 1State Key Laboratory of Oncology in South China, Collaborative Innovation Centre for Cancer Medicine; 2Department of Biotherapy, Sun Yat‑Sen University Cancer Center; 3Department of Radiation Oncology, Sun Yat‑Sen University Cancer Center, Guangzhou, Guangdong 510060, P.R. China Received July 31, 2020; Accepted December 18, 2020 DOI: 10.3892/ol.2021.12466 Abstract. Bladder cancer (BC) is the ninth most common immunohistochemistry and western blotting. In summary, lethal malignancy worldwide. Great efforts have been devoted KIF11 was significantly upregulated in BC and might act as to clarify the pathogenesis of BC, but the underlying molecular a potential prognostic biomarker. The present identification mechanisms remain unclear. To screen for the genes associated of DEGs and hub genes in BC may provide novel insight for with the progression and carcinogenesis of BC, three datasets investigating the molecular mechanisms of BC. were obtained from the Gene Expression Omnibus. A total of 37 tumor and 16 non‑cancerous samples were analyzed to Introduction identify differentially expressed genes (DEGs). Subsequently, 141 genes were identified, including 55 upregulated and Bladder cancer (BC) is the ninth most common malignancy 86 downregulated genes. The protein‑protein interaction worldwide with substantial morbidity and mortality. -
A Spontaneous Mutation in Contactin 1 in the Mouse
A Spontaneous Mutation in Contactin 1 in the Mouse Muriel T. Davisson1*, Roderick T. Bronson1, Abigail L. D. Tadenev1, William W. Motley1, Arjun Krishnaswamy2, Kevin L. Seburn1, Robert W. Burgess1 1 The Jackson Laboratory, Bar Harbor, Maine, United States of America, 2 Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts, United States of America Abstract Mutations in the gene encoding the immunoglobulin-superfamily member cell adhesion molecule contactin1 (CNTN1) cause lethal congenital myopathy in human patients and neurodevelopmental phenotypes in knockout mice. Whether the mutant mice provide an accurate model of the human disease is unclear; resolving this will require additional functional tests of the neuromuscular system and examination of Cntn1 mutations on different genetic backgrounds that may influence the phenotype. Toward these ends, we have analyzed a new, spontaneous mutation in the mouse Cntn1 gene that arose in a BALB/c genetic background. The overt phenotype is very similar to the knockout of Cntn1, with affected animals having reduced body weight, a failure to thrive, locomotor abnormalities, and a lifespan of 2–3 weeks. Mice homozygous for the new allele have CNTN1 protein undetectable by western blotting, suggesting that it is a null or very severe hypomorph. In an analysis of neuromuscular function, neuromuscular junctions had normal morphology, consistent with previous studies in knockout mice, and the muscles were able to generate appropriate force when normalized for their reduced size in late stage animals. Therefore, the Cntn1 mutant mice do not show evidence for a myopathy, but instead the phenotype is likely to be caused by dysfunction in the nervous system. -
Ryanodine Binding to Ryr1. Final Report Edward M
Evaluation of GSK2487213A on [3H]Ryanodine Binding to RyR1. Final Report Edward M. Balog, PhD School of Applied Physiology Georgia Institute of Technology December 17, 2010 1 Summary The effects of GSK2487213A (213A) on RyR1 function was assessed via skeletal muscle heavy sarcoplasmic reticulum (HSR) [3H]ryanodine binding. 213A did not affect HSR ryanodine binding when Ca2+ was the sole RyR1 regulator. Stripping HSR of FKBP12.0, via treatment with FK506, increased Ca2+-activated ryanodine binding. Exogenous FKBP12.0 alone or in combination with 213A and or reducing agents failed to reverse the effects prior exposure to FK506. Including FK506 in the HSR [3H]ryanodine binding buffer dose-dependently increased ryanodine binding. 213A did not alter the FK506 dose response. Treating HSR with the nitric oxide donor, NOR-3, did not substantially reduce the FKBP12.0 content of the HSR. Prior exposure to NOR-3 enhanced Ca2+ stimulated HSR ryanodine binding. 213A reversed the NOR-3 activation of RyR1. These results suggest that 213A reverses nitrosylation-induced activation of RyR1 and the inhibition does not occur via stabilizing the interaction between RyR1 and FKBP12.0. Introduction Ryanodine receptors (RyR) are endo/sarcoplamic reticulum (SR) resident Ca2+ selective channels that form the efflux pathway for the release of Ca2+ from the SR to initiate muscle contraction. Isoform 1 (RyR1) is the predominate form in skeletal muscle, RyR2 is the predominate form in the heart while RyR3 has a widespread distribution. The channels are regulated by numerous endogenous effectors including ions primarily Ca2+ and Mg2+, metabolites such as the adenine nucleotides and accessory proteins including calmodulin and the FK506-binding proteins (FKBP). -
Anti-HABP2 Monoclonal Antibody, Clone FQS25662 (DCABH-7346) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
Anti-HABP2 monoclonal antibody, clone FQS25662 (DCABH-7346) This product is for research use only and is not intended for diagnostic use. PRODUCT INFORMATION Product Overview Rabbit monoclonal to HABP2 Antigen Description Cleaves the alpha-chain at multiple sites and the beta-chain between Lys-53 and Lys-54 but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII. Immunogen Synthetic peptide (the amino acid sequence is considered to be commercially sensitive) within Human HABP2 aa 350-450. The exact sequence is proprietary.Database link: Q14520 Isotype IgG Source/Host Rabbit Species Reactivity Mouse, Rat, Human Clone FQS25662 Purity Tissue culture supernatant Conjugate Unconjugated Applications WB, IHC-P, ICC/IF Positive Control Human fetal liver, HepG2, MCF-7 and A549 lysate. Rat liver tissue. HepG2 cells. Format Liquid Size 100 μl Buffer Preservative: 0.01% Sodium azide; Constituents: 40% Glycerol, 59% PBS, 0.05% BSA Preservative 0.01% Sodium Azide Storage Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle. Ship Shipped at 4°C. 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