DOCSLIB.ORG

Figure S1. Quality Control Validation of MS Data. (A‑C) Mass Error Distribution of All Peptides Identified in the Acetylome

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

Figure S1. Quality control validation of MS data. (A‑C) Mass error distribution of all peptides identified in the acetylome, succi- nylome and quantitative proteome, respectively. (D‑F) Length distribution of peptides identified in the acetylome, succinylome and quantitative proteome, respectively. Figure S2. Comparison of modification level between breast cancer tissue and normal tissue. Comparison of acetylation level (A) and succinylation level (B) between breast cancer tissue and normal tissue. Data are medians and were analyzed using Wilcoxon Signed Rank Test. **P<0.01. Table SI. Protein sites whose acetylation and succinylation levels were both significantly upregulated in breast cancer tissues (fold change ≥1.5 compared with normal tissues). Protein ID Protein name Modification site P54868 HMCS2 310K Q15063 POSTN 549K Q99715 COCA1 1601K P51572 BAP31 72K P07237 PDLA1 328K Q06830 PRDX1 192K P48735 IDHP 180K P30101 PDIA3 417K P0DMV9 HS71B 526K Q01995 TAGL 21K P06748 NPM1 27K Q00325 MPCP 209K P00488 F13A 69K P02545 LMNA 260K P08133 ANXA6 478K P02452 CO1A1 751K Table SII. Protein sites whose acetylation and succinylation levels were both significantly downregulated in breast cancer tissues (fold change ≥1.5 compared with normal tissues). Protein ID Protein name Modification site RET4 P02753 30K PSG2 P07585 142K HBA P69905 12K IGKC P01834 80K HBA P69905 8K Table SIII. All proteins whose expression level were significantly upregulated in breast cancer tissues (fold change ≥1.5 compared with normal tissues). Protein ID Protein description Ratio (cancer vs. normal) P‑value P29762 Cellular retinoic acid‑binding protein 1 OS=Homo sapiens GN=CRABP1 PE=2 SV=2 4.5485 0.005237 P05787 Keratin, type II cytoskeletal 8 OS=Homo sapiens GN=KRT8 PE=1 SV=7 3.3785 3.49E‑13 Q01105 Protein SET OS=Homo sapiens GN=SET PE=1 SV=3 2.846 0.000294 Q9NZJ9 Diphosphoinositol polyphosphate phosphohydrolase 2 OS=Homo sapiens GN=NUDT4 PE=1 SV=2 2.814 0.002214 P40121 Macrophage-capping protein OS=Homo sapiens GN=CAPG PE=1 SV=2 2.808 0.0001 Q8WX93 Palladin OS=Homo sapiens GN=PALLD PE=1 SV=3 2.7565 5.55E-06 Q9UQP3 Tenascin-N OS=Homo sapiens GN=TNN PE=1 SV=2 2.724 0.00859 P15924 Desmoplakin OS=Homo sapiens GN=DSP PE=1 SV=3 2.7135 3.49E-14 Q13153 Serine/threonine‑protein kinase PAK 1 OS=Homo sapiens GN=PAK1 PE=1 SV=2 2.713 0.003549 P23528 Cofilin‑1 OS=Homo sapiens GN=CFL1 PE=1 SV=3 2.702 1.4E‑08 Q12874 Splicing factor 3A subunit 3 OS=Homo sapiens GN=SF3A3 PE=1 SV=1 2.699 0.009968 Q15063 Periostin OS=Homo sapiens GN=POSTN PE=1 SV=2 2.6945 1.37E‑12 Q13185 Chromobox protein homolog 3 OS=Homo sapiens GN=CBX3 PE=1 SV=4 2.6695 0.00138 Q8TF66 Leucine‑rich repeat‑containing protein 15 OS=Homo sapiens GN=LRRC15 PE=1 SV=2 2.661 0.002947 Q6P996 Pyridoxal‑dependent decarboxylase domain‑containing protein 1 OS=Homo sapiens GN=PDXDC1 PE=1 SV=2 2.635 1.09E‑05 P35442 Thrombospondin‑2 OS=Homo sapiens GN=THBS2 PE=1 SV=2 2.621 7.37E‑05 P13611 Versican core protein OS=Homo sapiens GN=VCAN PE=1 SV=3 2.617 4.99E‑06 Q00688 Peptidyl‑prolyl cis‑trans isomerase FKBP3 OS=Homo sapiens GN=FKBP3 PE=1 SV=1 2.529 0.006514 P08727 Keratin, type I cytoskeletal 19 OS=Homo sapiens GN=KRT19 PE=1 SV=4 2.493 1.01E‑10 Q02790 Peptidyl‑prolyl cis‑trans isomerase FKBP4 OS=Homo sapiens GN=FKBP4 PE=1 SV=3 2.465 8.29E‑05 P22626 Heterogeneous nuclear ribonucleoproteins A2/B1 OS=Homo sapiens GN=HNRNPA2B1 PE=1 SV=2 2.459 2.66E‑07 Q05682 Caldesmon OS=Homo sapiens GN=CALD1 PE=1 SV=3 2.4345 2.5E‑06 Q9P258 Protein RCC2 OS=Homo sapiens GN=RCC2 PE=1 SV=2 2.4015 0.009156 P30520 Adenylosuccinate synthetase isozyme 2 OS=Homo sapiens GN=ADSS PE=1 SV=3 2.391 0.003515 Q5SSJ5 Heterochromatin protein 1‑binding protein 3 OS=Homo sapiens GN=HP1BP3 PE=1 SV=1 2.375 0.001099 P05783 Keratin, type I cytoskeletal 18 OS=Homo sapiens GN=KRT18 PE=1 SV=2 2.3525 1.38E‑08 P21266 Glutathione S‑transferase Mu 3 OS=Homo sapiens GN=GSTM3 PE=1 SV=3 2.348 2.27E‑05 Q6EEV6 Small ubiquitin‑related modifier 4 OS=Homo sapiens GN=SUMO4 PE=1 SV=2 2.311 0.008154 P10253 Lysosomal alpha‑glucosidase OS=Homo sapiens GN=GAA PE=1 SV=4 2.2855 0.001327 P17844 Probable ATP‑dependent RNA helicase DDX5 OS=Homo sapiens GN=DDX5 PE=1 SV=1 2.249 0.000284 P50454 Serpin H1 OS=Homo sapiens GN=SERPINH1 PE=1 SV=2 2.211 6.02E‑06 P23193 Transcription elongation factor A protein 1 OS=Homo sapiens GN=TCEA1 PE=1 SV=2 2.203 0.004442 P39748 Flap endonuclease 1 OS=Homo sapiens GN=FEN1 PE=1 SV=1 2.197 0.005466 Q8TE77 Protein phosphatase Slingshot homolog 3 OS=Homo sapiens GN=SSH3 PE=1 SV=2 2.185 0.0028 P0CW22 40S ribosomal protein S17‑like OS=Homo sapiens GN=RPS17L PE=1 SV=1 2.171 0.007463 Q92544 Transmembrane 9 superfamily member 4 OS=Homo sapiens GN=TM9SF4 PE=1 SV=2 2.17 0.003809 P10155 60 kDa SS‑A/Ro ribonucleoprotein OS=Homo sapiens GN=TROVE2 PE=1 SV=2 2.168 0.000968 P63208 S‑phase kinase‑associated protein 1 OS=Homo sapiens GN=SKP1 PE=1 SV=2 2.165 0.000695 Table SIII. Continued. Protein ID Protein description Ratio (cancer vs. normal) P‑value Q8IV36 Protein HID1 OS=Homo sapiens GN=HID1 PE=1 SV=1 2.1405 0.002398 Q9Y266 Nuclear migration protein nudC OS=Homo sapiens GN=NUDC PE=1 SV=1 2.124 3.41E‑06 P62753 40S ribosomal protein S6 OS=Homo sapiens GN=RPS6 PE=1 SV=1 2.113 0.004002 P15170 Eukaryotic peptide chain release factor GTP‑binding subunit ERF3A OS=Homo sapiens GN=GSPT1 PE=1 SV=1 2.109 0.006605 Q13148 TAR DNA‑binding protein 43 OS=Homo sapiens GN=TARDBP PE=1 SV=1 2.092 5.22E‑05 Q9Y2X3 Nucleolar protein 58 OS=Homo sapiens GN=NOP58 PE=1 SV=1 2.087 0.005814 Q99715 Collagen alpha‑1(XII) chain OS=Homo sapiens GN=COL12A1 PE=1 SV=2 2.084 1.36E‑11 Q9UGI8 Testin OS=Homo sapiens GN=TES PE=1 SV=1 2.08 0.001602 O43390 Heterogeneous nuclear ribonucleoprotein R OS=Homo sapiens GN=HNRNPR PE=1 SV=1 2.069 5.72E‑05 P52272 Heterogeneous nuclear ribonucleoprotein M OS=Homo sapiens GN=HNRNPM PE=1 SV=3 2.066 8.9E‑08 P12830 Cadherin‑1 OS=Homo sapiens GN=CDH1 PE=1 SV=3 2.0585 1.43E‑05 P26373 60S ribosomal protein L13 OS=Homo sapiens GN=RPL13 PE=1 SV=4 2.047 0.006719 P08621 U1 small nuclear ribonucleoprotein 70 kDa OS=Homo sapiens GN=SNRNP70 PE=1 SV=2 2.045 0.000827 Q9UNE7 E3 ubiquitin‑protein ligase CHIP OS=Homo sapiens GN=STUB1 PE=1 SV=2 2.043 0.000282 P22234 Multifunctional protein ADE2 OS=Homo sapiens GN=PAICS PE=1 SV=3 2.04 0.005675 Q15233 Non‑POU domain‑containing octamer‑binding protein OS=Homo sapiens GN=NONO PE=1 SV=4 2.0385 1.4E‑08 P50851 Lipopolysaccharide‑responsive and beige‑like anchor protein OS=Homo sapiens GN=LRBA PE=1 SV=4 2.0365 0.000609 Q13765 Nascent polypeptide‑associated complex subunit alpha OS=Homo sapiens GN=NACA PE=1 SV=1 2.029 0.001067 Q08J23 tRNA (cytosine(34)‑C(5))‑methyltransferase OS=Homo sapiens GN=NSUN2 PE=1 SV=2 2.0205 0.008385 O75223 Gamma‑glutamylcyclotransferase OS=Homo sapiens GN=GGCT PE=1 SV=1 2.006 0.003327 P20700 Lamin‑B1 OS=Homo sapiens GN=LMNB1 PE=1 SV=2 1.982 6.8E‑05 P43487 Ran‑specific GTPase‑activating protein OS=Homo sapiens GN=RANBP1 PE=1 SV=1 1.9695 0.007456 P30050 60S ribosomal protein L12 OS=Homo sapiens GN=RPL12 PE=1 SV=1 1.961 0.000103 P08729 Keratin, type II cytoskeletal 7 OS=Homo sapiens GN=KRT7 PE=1 SV=5 1.96 3.5E‑08 P49585 Choline‑phosphate cytidylyltransferase A OS=Homo sapiens GN=PCYT1A PE=1 SV=2 1.949 0.009506 P15311 Ezrin OS=Homo sapiens GN=EZR PE=1 SV=4 1.937 0.000112 P19338 Nucleolin OS=Homo sapiens GN=NCL PE=1 SV=3 1.9285 4.89E‑05 Q9NR99 Matrix‑remodeling‑associated protein 5 OS=Homo sapiens GN=MXRA5 PE=2 SV=3 1.9275 0.004449 Q8IUX7 Adipocyte enhancer‑binding protein 1 OS=Homo sapiens GN=AEBP1 PE=1 SV=1 1.912 0.004188 Q15459 Splicing factor 3A subunit 1 OS=Homo sapiens GN=SF3A1 PE=1 SV=1 1.911 0.002117 P38919 Eukaryotic initiation factor 4A‑III OS=Homo sapiens GN=EIF4A3 PE=1 SV=4 1.91 0.008213 Q9UHB6 LIM domain and actin‑binding protein 1 OS=Homo sapiens GN=LIMA1 PE=1 SV=1 1.9085 0.001674 P47813 Eukaryotic translation initiation factor 1A, X‑chromosomal OS=Homo sapiens GN=EIF1AX PE=1 SV=2 1.9045 0.008956 Q9NR45 Sialic acid synthase OS=Homo sapiens GN=NANS PE=1 SV=2 1.9025 5.07E‑05 Q14103 Heterogeneous nuclear ribonucleoprotein D0 OS=Homo sapiens GN=HNRNPD PE=1 SV=1 1.893 0.002203 P49207 60S ribosomal protein L34 OS=Homo sapiens GN=RPL34 PE=1 SV=3 1.887 0.005138 Q32P51 Heterogeneous nuclear ribonucleoprotein A1‑like 2 OS=Homo sapiens GN=HNRNPA1L2 PE=2 SV=2 1.885 0.000146 P24821 Tenascin OS=Homo sapiens GN=TNC PE=1 SV=3 1.874 4.26E‑06 Table SIII.
Recommended publications
  • Reprogramming of Trna Modifications Controls the Oxidative Stress Response by Codon-Biased Translation of Proteins

    Reprogramming of Trna Modifications Controls the Oxidative Stress Response by Codon-Biased Translation of Proteins

    Reprogramming of tRNA modifications controls the oxidative stress response by codon-biased translation of proteins The MIT Faculty has made this article openly available. Please share how this access benefits you. Your story matters. Citation Chan, Clement T.Y. et al. “Reprogramming of tRNA Modifications Controls the Oxidative Stress Response by Codon-biased Translation of Proteins.” Nature Communications 3 (2012): 937. As Published http://dx.doi.org/10.1038/ncomms1938 Publisher Nature Publishing Group Version Author's final manuscript Citable link http://hdl.handle.net/1721.1/76775 Terms of Use Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. Reprogramming of tRNA modifications controls the oxidative stress response by codon-biased translation of proteins Clement T.Y. Chan,1,2 Yan Ling Joy Pang,1 Wenjun Deng,1 I. Ramesh Babu,1 Madhu Dyavaiah,3 Thomas J. Begley3 and Peter C. Dedon1,4* 1Department of Biological Engineering, 2Department of Chemistry and 4Center for Environmental Health Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139; 3College of Nanoscale Science and Engineering, University at Albany, SUNY, Albany, NY 12203 * Corresponding author: PCD, Department of Biological Engineering, NE47-277, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139; tel 617-253-8017; fax 617-324-7554; email [email protected] 2 ABSTRACT Selective translation of survival proteins is an important facet of cellular stress response. We recently demonstrated that this translational control involves a stress-specific reprogramming of modified ribonucleosides in tRNA.
  • Allele-Specific Expression of Ribosomal Protein Genes in Interspecific Hybrid Catfish

    Allele-Specific Expression of Ribosomal Protein Genes in Interspecific Hybrid Catfish

    Allele-specific Expression of Ribosomal Protein Genes in Interspecific Hybrid Catfish by Ailu Chen A dissertation submitted to the Graduate Faculty of Auburn University in partial fulfillment of the requirements for the Degree of Doctor of Philosophy Auburn, Alabama August 1, 2015 Keywords: catfish, interspecific hybrids, allele-specific expression, ribosomal protein Copyright 2015 by Ailu Chen Approved by Zhanjiang Liu, Chair, Professor, School of Fisheries, Aquaculture and Aquatic Sciences Nannan Liu, Professor, Entomology and Plant Pathology Eric Peatman, Associate Professor, School of Fisheries, Aquaculture and Aquatic Sciences Aaron M. Rashotte, Associate Professor, Biological Sciences Abstract Interspecific hybridization results in a vast reservoir of allelic variations, which may potentially contribute to phenotypical enhancement in the hybrids. Whether the allelic variations are related to the downstream phenotypic differences of interspecific hybrid is still an open question. The recently developed genome-wide allele-specific approaches that harness high- throughput sequencing technology allow direct quantification of allelic variations and gene expression patterns. In this work, I investigated allele-specific expression (ASE) pattern using RNA-Seq datasets generated from interspecific catfish hybrids. The objective of the study is to determine the ASE genes and pathways in which they are involved. Specifically, my study investigated ASE-SNPs, ASE-genes, parent-of-origins of ASE allele and how ASE would possibly contribute to heterosis. My data showed that ASE was operating in the interspecific catfish system. Of the 66,251 and 177,841 SNPs identified from the datasets of the liver and gill, 5,420 (8.2%) and 13,390 (7.5%) SNPs were identified as significant ASE-SNPs, respectively.
  • Supplemental Data

    Supplemental Data

    SUPPLEMENTAL INFORMATION Glomerular cell crosstalk influences composition and assembly of extracellular matrix Adam Byron,1,*,† Michael J. Randles,1,2,† Jonathan D. Humphries,1 Aleksandr Mironov,1 Hellyeh Hamidi,1 Shelley Harris,2 Peter W. Mathieson,3 Moin A. Saleem,3 Simon S. Satchell,3 Roy Zent,4,5 Martin J. Humphries,1 and Rachel Lennon.1,2 1Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, UK; 2Faculty of Medical and Human Sciences, University of Manchester, Manchester, UK; 3Academic Renal Unit, Faculty of Medicine and Dentistry, University of Bristol, Bristol, UK; 4Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA; and 5Veterans Affairs Hospital, Nashville, TN, USA. *Present address: Edinburgh Cancer Research UK Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, UK. †These authors contributed equally to this work. Corresponding author: Dr Rachel Lennon, Wellcome Trust Centre for Cell-Matrix Research, Michael Smith Building, University of Manchester, Manchester M13 9PT, UK. Phone: 0044 (0) 161 2755498. Fax: 0044 (0) 161 2755082. Email: [email protected] Supplementary methods Non-glomerular cell culture HEK 293T and human foreskin fibroblasts were cultured until confluent in Dulbecco's Modified Eagle Medium supplemented with 10% foetal calf serum. Lentiviral production and transduction Podocytes stably expressing GFP were produced by lentiviral transduction. Briefly, HEK 293T cells were transfected with three plasmids obtained from Addgene (psPAX2 Addgene ID 12260, pMD2.G Addgene ID 12259 and pWPXL Addgene ID 12257) using polyethyleneimine (Sigma-Aldrich). Conditioned medium containing viruses was collected after 5 days following several media changes including an 8 hr incubation with sodium butyrate- containing media to promote virus production.
  • Aldolase C (C-Terminus Specific) Data Sheet

    Aldolase C (C-Terminus Specific) Data Sheet

    Aldolase C (C-terminus Specific) Data Sheet Catalog Number: MO22157 Host: Mouse Product Type: Monoclonal IgG1 Species Human, horse, cow, pig, Affinity Purified Antibody Reactivity: chicken, rat, mouse Immunogen Sequence: C-terminal sequence Format: Liquid, 100 ul aliquot KYEGSGEDGGAAAQSLYIANHAY Concentration: 1 mg/ml HGNC name for this protein is ALDOC Applications: Immunofluorescence/Immunocytochemistry: 1:500-1:1,000 Immunohistochemistry: 1: 500-1:1,000 Western Blot: 1:1,000 Dilutions listed as a recommendation. Optimal dilution should be determined by investigator. Storage: Antibody can also be aliquoted and stored frozen at -20° C to -70° C in a manual defrost freezer for six months without detectable loss of activity. The antibody can be stored at 2° - 8° C for 1 month without detectable loss of activity. Avoid repeated freeze-thaw cycles. Application Notes Description/Data: Aldolase A is generally considered to be a muscle enzyme. Northern analysis of cultured cells suggests that it is present in both neurons and glia. Aldolase C shares 81% amino acid identity with aldolase A and 70% identity with aldolase B. Earlier studies using isozyme-specific antibodies report its location in gray matter astrocytes and cells of the pia mater. In situ hybridization of mouse central nervous system using isozyme-specific probes revealed that aldolase A and C are expressed in complementary cell types: aldolase A mRNA is found in neurons; aldolase C message is detected in astrocytes, some cells of the pia mater, and Purkinje cells. Aldolase C can in some situations be used as an astrocyte marker. However Purkinje cells of the cerebellum contain high levels of the enzyme, so the enzyme is not totally astrocyte specific.
  • Datasheet: VPA00226

    Datasheet: VPA00226

    Datasheet: VPA00226 Description: RABBIT ANTI ALDOA Specificity: ALDOA Format: Purified Product Type: PrecisionAb™ Polyclonal Isotype: Polyclonal IgG Quantity: 100 µl Product Details Applications This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit www.bio-rad-antibodies.com/protocols. Yes No Not Determined Suggested Dilution Western Blotting 1/1000 PrecisionAb antibodies have been extensively validated for the western blot application. The antibody has been validated at the suggested dilution. Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Further optimization may be required dependant on sample type. Target Species Human Species Cross Reacts with: Mouse, Rat Reactivity N.B. Antibody reactivity and working conditions may vary between species. Product Form Purified IgG - liquid Preparation Rabbit Ig fraction prepared by ammonium sulphate precipitation Buffer Solution Phosphate buffered saline Preservative 0.09% Sodium Azide (NaN3) Stabilisers Immunogen KLH conjugated synthetic peptide between 66-95 amino acids from the N-terminal region of human ALDOA External Database UniProt: Links P04075 Related reagents Entrez Gene: 226 ALDOA Related reagents Page 1 of 2 Synonyms ALDA Specificity Rabbit anti Human ALDOA antibody recognizes fructose-bisphosphate aldolase A, also known as epididymis secretory sperm binding protein Li 87p, fructose-1,6-bisphosphate triosephosphate-lyase, lung cancer antigen NY-LU-1 and muscle-type aldolase. Encoded by the ALDOA gene, fructose-bisphosphate aldolase A is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate.
  • Curcumin Alters Gene Expression-Associated DNA Damage, Cell Cycle, Cell Survival and Cell Migration and Invasion in NCI-H460 Human Lung Cancer Cells in Vitro

    Curcumin Alters Gene Expression-Associated DNA Damage, Cell Cycle, Cell Survival and Cell Migration and Invasion in NCI-H460 Human Lung Cancer Cells in Vitro

    ONCOLOGY REPORTS 34: 1853-1874, 2015 Curcumin alters gene expression-associated DNA damage, cell cycle, cell survival and cell migration and invasion in NCI-H460 human lung cancer cells in vitro I-TSANG CHIANG1,2, WEI-SHU WANG3, HSIN-CHUNG LIU4, SU-TSO YANG5, NOU-YING TANG6 and JING-GUNG CHUNG4,7 1Department of Radiation Oncology, National Yang‑Ming University Hospital, Yilan 260; 2Department of Radiological Technology, Central Taiwan University of Science and Technology, Taichung 40601; 3Department of Internal Medicine, National Yang‑Ming University Hospital, Yilan 260; 4Department of Biological Science and Technology, China Medical University, Taichung 404; 5Department of Radiology, China Medical University Hospital, Taichung 404; 6Graduate Institute of Chinese Medicine, China Medical University, Taichung 404; 7Department of Biotechnology, Asia University, Taichung 404, Taiwan, R.O.C. Received March 31, 2015; Accepted June 26, 2015 DOI: 10.3892/or.2015.4159 Abstract. Lung cancer is the most common cause of cancer CARD6, ID1 and ID2 genes, associated with cell survival and mortality and new cases are on the increase worldwide. the BRMS1L, associated with cell migration and invasion. However, the treatment of lung cancer remains unsatisfactory. Additionally, 59 downregulated genes exhibited a >4-fold Curcumin has been shown to induce cell death in many human change, including the DDIT3 gene, associated with DNA cancer cells, including human lung cancer cells. However, the damage; while 97 genes had a >3- to 4-fold change including the effects of curcumin on genetic mechanisms associated with DDIT4 gene, associated with DNA damage; the CCPG1 gene, these actions remain unclear. Curcumin (2 µM) was added associated with cell cycle and 321 genes with a >2- to 3-fold to NCI-H460 human lung cancer cells and the cells were including the GADD45A and CGREF1 genes, associated with incubated for 24 h.
  • In This Table Protein Name, Uniprot Code, Gene Name P-Value

    In This Table Protein Name, Uniprot Code, Gene Name P-Value

    Supplementary Table S1: In this table protein name, uniprot code, gene name p-value and Fold change (FC) for each comparison are shown, for 299 of the 301 significantly regulated proteins found in both comparisons (p-value<0.01, fold change (FC) >+/-0.37) ALS versus control and FTLD-U versus control. Two uncharacterized proteins have been excluded from this list Protein name Uniprot Gene name p value FC FTLD-U p value FC ALS FTLD-U ALS Cytochrome b-c1 complex P14927 UQCRB 1.534E-03 -1.591E+00 6.005E-04 -1.639E+00 subunit 7 NADH dehydrogenase O95182 NDUFA7 4.127E-04 -9.471E-01 3.467E-05 -1.643E+00 [ubiquinone] 1 alpha subcomplex subunit 7 NADH dehydrogenase O43678 NDUFA2 3.230E-04 -9.145E-01 2.113E-04 -1.450E+00 [ubiquinone] 1 alpha subcomplex subunit 2 NADH dehydrogenase O43920 NDUFS5 1.769E-04 -8.829E-01 3.235E-05 -1.007E+00 [ubiquinone] iron-sulfur protein 5 ARF GTPase-activating A0A0C4DGN6 GIT1 1.306E-03 -8.810E-01 1.115E-03 -7.228E-01 protein GIT1 Methylglutaconyl-CoA Q13825 AUH 6.097E-04 -7.666E-01 5.619E-06 -1.178E+00 hydratase, mitochondrial ADP/ATP translocase 1 P12235 SLC25A4 6.068E-03 -6.095E-01 3.595E-04 -1.011E+00 MIC J3QTA6 CHCHD6 1.090E-04 -5.913E-01 2.124E-03 -5.948E-01 MIC J3QTA6 CHCHD6 1.090E-04 -5.913E-01 2.124E-03 -5.948E-01 Protein kinase C and casein Q9BY11 PACSIN1 3.837E-03 -5.863E-01 3.680E-06 -1.824E+00 kinase substrate in neurons protein 1 Tubulin polymerization- O94811 TPPP 6.466E-03 -5.755E-01 6.943E-06 -1.169E+00 promoting protein MIC C9JRZ6 CHCHD3 2.912E-02 -6.187E-01 2.195E-03 -9.781E-01 Mitochondrial 2-
  • Supplementary Table 1. the List of Proteins with at Least 2 Unique

    Supplementary Table 1. the List of Proteins with at Least 2 Unique

    Supplementary table 1. The list of proteins with at least 2 unique peptides identified in 3D cultured keratinocytes exposed to UVA (30 J/cm2) or UVB irradiation (60 mJ/cm2) and treated with treated with rutin [25 µM] or/and ascorbic acid [100 µM]. Nr Accession Description 1 A0A024QZN4 Vinculin 2 A0A024QZN9 Voltage-dependent anion channel 2 3 A0A024QZV0 HCG1811539 4 A0A024QZX3 Serpin peptidase inhibitor 5 A0A024QZZ7 Histone H2B 6 A0A024R1A3 Ubiquitin-activating enzyme E1 7 A0A024R1K7 Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein 8 A0A024R280 Phosphoserine aminotransferase 1 9 A0A024R2Q4 Ribosomal protein L15 10 A0A024R321 Filamin B 11 A0A024R382 CNDP dipeptidase 2 12 A0A024R3V9 HCG37498 13 A0A024R3X7 Heat shock 10kDa protein 1 (Chaperonin 10) 14 A0A024R408 Actin related protein 2/3 complex, subunit 2, 15 A0A024R4U3 Tubulin tyrosine ligase-like family 16 A0A024R592 Glucosidase 17 A0A024R5Z8 RAB11A, member RAS oncogene family 18 A0A024R652 Methylenetetrahydrofolate dehydrogenase 19 A0A024R6C9 Dihydrolipoamide S-succinyltransferase 20 A0A024R6D4 Enhancer of rudimentary homolog 21 A0A024R7F7 Transportin 2 22 A0A024R7T3 Heterogeneous nuclear ribonucleoprotein F 23 A0A024R814 Ribosomal protein L7 24 A0A024R872 Chromosome 9 open reading frame 88 25 A0A024R895 SET translocation 26 A0A024R8W0 DEAD (Asp-Glu-Ala-Asp) box polypeptide 48 27 A0A024R9E2 Poly(A) binding protein, cytoplasmic 1 28 A0A024RA28 Heterogeneous nuclear ribonucleoprotein A2/B1 29 A0A024RA52 Proteasome subunit alpha 30 A0A024RAE4 Cell division cycle 42 31
  • Inhibition of the MID1 Protein Complex

    Inhibition of the MID1 Protein Complex

    Matthes et al. Cell Death Discovery (2018) 4:4 DOI 10.1038/s41420-017-0003-8 Cell Death Discovery ARTICLE Open Access Inhibition of the MID1 protein complex: a novel approach targeting APP protein synthesis Frank Matthes1,MoritzM.Hettich1, Judith Schilling1, Diana Flores-Dominguez1, Nelli Blank1, Thomas Wiglenda2, Alexander Buntru2,HannaWolf1, Stephanie Weber1,InaVorberg 1, Alina Dagane2, Gunnar Dittmar2,3,ErichWanker2, Dan Ehninger1 and Sybille Krauss1 Abstract Alzheimer’s disease (AD) is characterized by two neuropathological hallmarks: senile plaques, which are composed of amyloid-β (Aβ) peptides, and neurofibrillary tangles, which are composed of hyperphosphorylated tau protein. Aβ peptides are derived from sequential proteolytic cleavage of the amyloid precursor protein (APP). In this study, we identified a so far unknown mode of regulation of APP protein synthesis involving the MID1 protein complex: MID1 binds to and regulates the translation of APP mRNA. The underlying mode of action of MID1 involves the mTOR pathway. Thus, inhibition of the MID1 complex reduces the APP protein level in cultures of primary neurons. Based on this, we used one compound that we discovered previously to interfere with the MID1 complex, metformin, for in vivo experiments. Indeed, long-term treatment with metformin decreased APP protein expression levels and consequently Aβ in an AD mouse model. Importantly, we have initiated the metformin treatment late in life, at a time-point where mice were in an already progressed state of the disease, and could observe an improved behavioral phenotype. These 1234567890 1234567890 findings together with our previous observation, showing that inhibition of the MID1 complex by metformin also decreases tau phosphorylation, make the MID1 complex a particularly interesting drug target for treating AD.
  • Electronic Supplementary Material (ESI) for Chemcomm. This Journal Is © the Royal Society of Chemistry 2015

    Electronic Supplementary Material (ESI) for Chemcomm. This Journal Is © the Royal Society of Chemistry 2015

    Electronic Supplementary Material (ESI) for ChemComm. This journal is © The Royal Society of Chemistry 2015 tel26 Nuclear proteins identification ‐ Summary Accession Score Mass Matches tel26 Exp 1 Matches tel26 Exp 2 Protein(s) name* scr26 Exp1** scr26 Exp2** XRCC5_HUMAN 450 83222 39 49 X‐ray repair cross‐complementing protein 5 OS=Homo sapiens GN=XRCC5 PE=1 SV=3 yes yes XRCC6_HUMAN 444 70084 35 53 X‐ray repair cross‐complementing protein 6 OS=Homo sapiens GN=XRCC6 PE=1 SV=2 no no HMGB1_HUMAN 88 25049 9 25 High mobility group protein B1 OS=Homo sapiens GN=HMGB1 PE=1 SV=3 no no HMGB2_HUMAN 69 24190 4 17 High mobility group protein B2 OS=Homo sapiens GN=HMGB2 PE=1 SV=2 yes yes FUBP2_HUMAN 126 73355 9 9 Far upstream element‐binding protein 2 OS=Homo sapiens GN=KHSRP PE=1 SV=4 no no RFA1_HUMAN 67 68723 7 10 Replication protein A 70 kDa DNA‐binding subunit OS=Homo sapiens GN=RPA1 PE=1 SV=2 no no PPIA_HUMAN 95 18229 11 3 Peptidyl‐prolyl cis‐trans isomerase A OS=Homo sapiens GN=PPIA PE=1 SV=2 yes yes LMNB1_HUMAN 64 66653 6 8 Lamin‐B1 OS=Homo sapiens GN=LMNB1 PE=1 SV=2 no no ROAA_HUMAN 52 36316 3 10 Heterogeneous nuclear ribonucleoprotein A/B OS=Homo sapiens GN=HNRNPAB PE=1 SV=2 no no EHD4_HUMAN 70 61365 6 7 EH domain‐containing protein 4 OS=Homo sapiens GN=EHD4 PE=1 SV=1 no no FUBP1_HUMAN 49 67690 5 8 Far upstream element‐binding protein 1 OS=Homo sapiens GN=FUBP1 PE=1 SV=3 no yes MCM7_HUMAN 53 81884 5 7 DNA replication licensing factor MCM7 OS=Homo sapiens GN=MCM7 PE=1 SV=4 no no SEPT9_HUMAN 41 65646 3 9 Septin‐9 OS=Homo sapiens GN=SEPT9 PE=1
  • A Review of Isozymes in Cancer1

    A Review of Isozymes in Cancer1

    Cancer Research VOLUME31 NOVEMBER 1971 NUMBER11 [CANCER RESEARCH 31, 1523-1542, November 1971] A Review of Isozymes in Cancer1 Wayne E. Criss Department of Obstetrics and Gynecology, University of Florida College of Medicine, Gainesville, Florida 32601 TABLE OF CONTENTS postulated role for that particular isozymic system in cellular metabolism. Summary 1523 Introduction 1523 Normal enzyme differentiation 1523 INTRODUCTION Tumor enzyme differentiation 1524 Isozymes 1524 Normal Enzyme Differentiation DNA polymerase 1524 Enzyme differentiation is the process whereby, during the Hexokinase 1525 Fructose 1,6-diphosphatase 1525 development of an organ in an animal, the organ acquires the quantitative and qualitative adult enzyme patterns (122). Key Aldolase 1526 pathway enzymes in several metabolic processes have been Pyruvate kinase 1527 found to undergo enzymatic differentiation. The enzymes Láclatedehydrogenase 1527 Isocitrate dehydrogenase 1527 involved in nitrogen metabolism, and also in urea cycle Malate dehydrogenase 1528 metabolism (180), are tyrosine aminotransferase (123, 151, Glycerol phosphate dehydrogenase 1529 330, 410), tryptophan pyrrolase (261), serine dehydratase Glutaminase 1529 (123, 410), histidine ammonia lyase (11), and aspartate Aspartate aminotransferase 1530 aminotransferase (337, 388). The enzymes involved in nucleic Adenylate kinase 1531 acid metabolism are DNA polymerase (156, 277) and RNase (52). In glycolysis the enzymes are hexokinase-glucokinase Carbamyl phosphate synthetase 1531 Lactose synthetase 1533 (98, 389), galactokinase 30, aldolase (267, 315), pyruvate Discussion 1533 kinase (73, 386), and lactate dehydrogenase (67, 69). In References 1533 mitochondrial oxidation they are NADH oxidase, succinic oxidase, a-glycero-P oxidase, ATPase, cytochrome oxidase, and flavin content (84, 296). In glycogen metabolism the SUMMARY enzymes involved are UDPG pyrophosphorylase and UDPG glucosyltransferase (19).
  • Structure–Function Relationships Between Aldolase C/Zebrin II Expression and Complex Spike Synchrony in the Cerebellum

    Structure–Function Relationships Between Aldolase C/Zebrin II Expression and Complex Spike Synchrony in the Cerebellum

    The Journal of Neuroscience, January 14, 2015 • 35(2):843–852 • 843 Systems/Circuits Structure–Function Relationships between Aldolase C/Zebrin II Expression and Complex Spike Synchrony in the Cerebellum Shinichiro Tsutsumi,1 Maya Yamazaki,2 Taisuke Miyazaki,3 Masahiko Watanabe,3 Kenji Sakimura,2 Masanobu Kano,1 and Kazuo Kitamura1,4 1Department of Neurophysiology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan, 2Department of Cellular Neurobiology, Brain Research Institute, Niigata University, Niigata 951-8585, Japan, 3Department of Anatomy, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan, and 4PRESTO, JST, Saitama 332-0012, Japan Simple and regular anatomical structure is a hallmark of the cerebellar cortex. Parasagittally arrayed alternate expression of aldolase C/zebrin II in Purkinje cells (PCs) has been extensively studied, but surprisingly little is known about its functional significance. Here we found a precise structure–function relationship between aldolase C expression and synchrony of PC complex spike activities that reflect climbing fiber inputs to PCs. We performed two-photon calcium imaging in transgenic mice in which aldolase C compartments can be visualized in vivo, and identified highly synchronous complex spike activities among aldolase C-positive or aldolase C-negative PCs, but not across these populations. The boundary of aldolase C compartments corresponded to that of complex spike synchrony at single-cell resolution. Sensory stimulation evoked aldolase C compartment-specific