Targeting the Glycome of Major Milk Proteins

Total Page:16

File Type:pdf, Size:1020Kb

Targeting the Glycome of Major Milk Proteins Provided by the author(s) and NUI Galway in accordance with publisher policies. Please cite the published version when available. Title Targeting the glycome of major milk proteins Author(s) O'Riordan, Noelle Publication Date 2016-10-20 Item record http://hdl.handle.net/10379/6092 Downloaded 2021-09-25T01:55:26Z Some rights reserved. For more information, please see the item record link above. Targeting the glycome of major milk proteins A Thesis Presented to National University of Ireland, Galway for the degree of Doctor of Philosophy (Science) Noelle O’Riordan, B.Sc. 1Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork 2National University of Ireland, Galway (NUIG), Co. Galway Research Supervisors: Dr. Rita M. Hickey1, Prof. Lokesh Joshi2 i Table of Contents !Unexpected End of Formula Thesis Abstract ...................................................................................................... vii Publications ............................................................................................................. x Oral Communications ............................................................................................ xi Abstracts ................................................................................................................ xii Abbreviations ....................................................................................................... xiii List of tables .......................................................................................................... xv List of figures ...................................................................................................... xvii Acknowledgements ............................................................................................... xx Thesis introduction ............................................................................................... xxi Chapter 1 Literature review: Structural and functional characteristics of bovine milk protein glycosylation Abstract ................................................................................................................... 2 1. Introduction ......................................................................................................... 3 2. The glycome of bovine milk proteins ................................................................. 5 3. Bovine milk glycoproteins .................................................................................. 6 3.1 Lactoferrin .............................................................................................................. 6 3.1.1 Lactoferrin glycosylation ........................................................................ 6 3.1.2 Glycosylation and protein structure ........................................................ 9 3.1.3 Biological activities associated with Lactoferrin glycosylation ........... 10 3.2 Kappa-casein and Caseinomacropeptide .......................................................... 12 3.2.1 GMP Glycosylation .............................................................................. 13 3.2.2 Biological activities associated with GMP glycosylation..................... 15 3.3 Milk fat globule membrane ................................................................................ 17 ii 3.3.1 The mucins ............................................................................................ 19 3.3.2 Butyrophilin .......................................................................................... 21 3.3.3 Lactadherin ........................................................................................... 21 3.3.4 Cluster of Differentiation 36 ................................................................. 22 3.3.5 Proteose peptone component 3 ............................................................. 23 3.4 Immunoglobulins ................................................................................................. 24 3.5. Minor milk glycoproteins .................................................................................. 26 4. Commercialisation and current patents relating to bovine milk glycoproteins. 28 5. Future directions of glycoprotein investigation ................................................ 33 6. Reference………………………………………………………………………35 Chapter 2 Glycosidase activities in bovine milk over lactation Abstract ................................................................................................................. 52 1. Introduction ....................................................................................................... 53 2 Methods and materials ....................................................................................... 54 2.1 Materials ............................................................................................................... 54 2.2 Milk samples ........................................................................................................ 55 2.3 Glycosidase activity............................................................................................. 55 3. Results ............................................................................................................... 55 4. Discussion ......................................................................................................... 57 5. Conclusions ....................................................................................................... 65 6. References ......................................................................................................... 66 Chapter 3 Profiling temporal changes in bovine milk lactoferrin glycosylation using lectin microarrays Abstract ................................................................................................................. 72 1. Introduction ....................................................................................................... 73 iii 2 Methods and materials ....................................................................................... 75 2.1 Materials ............................................................................................................... 75 2.2 Sample collection ................................................................................................. 76 2.3 Lactoferrin isolation ............................................................................................ 76 2.4 Fluorescent labeling of glycoproteins ............................................................... 77 2.5 Construction and incubation of lectin microarrays ......................................... 77 2.6 Data extraction ..................................................................................................... 78 2.7 Statistical analysis ................................................................................................ 78 2.8 Monosaccharide analysis .................................................................................... 79 3. Results and Discussion ...................................................................................... 80 3.1 Purification of bLF from milk ............................................................................ 80 3.2 Lectin microarray profiling bLF glycosylation................................................ 82 3.3 Monosaccharide analysis of bLF samples ........................................................ 84 3.4 Temporal changes in glycosylation ................................................................... 88 3.5 Temporal changes in sialylation ........................................................................ 91 4. Conclusions ....................................................................................................... 93 5. References ......................................................................................................... 94 6. Supplementary figures and tables ..................................................................... 98 Chapter 4 Investigating the influence of glycosylation variation on the bacterial binding functionality of bovine lactoferrin Abstract ............................................................................................................... 104 1. Introduction ..................................................................................................... 105 2. Methods and materials .................................................................................... 107 2.1 Materials .................................................................................................... 107 2.2 Bacterial strains and culture conditions ..................................................... 107 2.3 Biotinylation of Lactoferrin ....................................................................... 108 iv 2.5 Biacore assay ............................................................................................. 108 2.6 Statistical analysis ..................................................................................... 108 3. Results ............................................................................................................. 109 4. Discussion ....................................................................................................... 113 References ........................................................................................................... 117 Chapter 5 Bovine glycomacropeptide promotes the growth of Bifidobacterium longum subsp. infantis and modulates its gene expression
Recommended publications
  • Platelet Membrane Glycoproteins: a Historical Review*
    577 Platelet Membrane Glycoproteins: A Historical Review* Alan T. Nurden, PhD1 1 L’Institut de Rhythmologie et Modélisation Cardiaque (LIRYC), Address for correspondence Alan T. Nurden, PhD, L’Institut de Plateforme Technologique et d’Innovation Biomédicale (PTIB), Rhythmologie et Modélisation Cardiaque, Plateforme Technologique Hôpital Xavier Arnozan, Pessac, France et d’Innovation Biomédicale, Hôpital Xavier Arnozan, Avenue du Haut- Lévèque, 33600 Pessac, France (e-mail: [email protected]). Semin Thromb Hemost 2014;40:577–584. Abstract The search for the components of the platelet surface that mediate platelet adhesion and platelet aggregation began for earnest in the late 1960s when electron microscopy demonstrated the presence of a carbohydrate-rich, negatively charged outer coat that was called the “glycocalyx.” Progressively, electrophoretic procedures were developed that identified the major membrane glycoproteins (GP) that constitute this layer. Studies on inherited disorders of platelets then permitted the designation of the major effectors of platelet function. This began with the discovery in Paris that platelets of patients with Glanzmann thrombasthenia, an inherited disorder of platelet aggregation, Keywords lacked two major GP. Subsequent studies established the role for the GPIIb-IIIa complex ► platelet (now known as integrin αIIbβ3)inbindingfibrinogen and other adhesive proteins on ► inherited disorder activated platelets and the formation of the protein bridges that join platelets together ► membrane in the platelet aggregate. This was quickly followed by the observation that platelets of glycoproteins patients with the Bernard–Soulier syndrome, with macrothrombocytopenia and a ► Glanzmann distinct disorder of platelet adhesion, lacked the carbohydrate-rich, negatively charged, thrombasthenia GPIb. It was shown that GPIb, through its interaction with von Willebrand factor, ► Bernard–Soulier mediated platelet attachment to injured sites in the vessel wall.
    [Show full text]
  • Surface Glycoproteomic Analysis of Hepatocellular Carcinoma Cells by Affinity Enrichment and Mass Spectrometric Identification
    Glycoconj J (2012) 29:411–424 DOI 10.1007/s10719-012-9420-3 Surface glycoproteomic analysis of hepatocellular carcinoma cells by affinity enrichment and mass spectrometric identification Wei Mi & Wei Jia & Zhaobin Zheng & Jinglan Wang & Yun Cai & Wantao Ying & Xiaohong Qian Received: 14 April 2012 /Revised: 5 June 2012 /Accepted: 12 June 2012 /Published online: 1 July 2012 # Springer Science+Business Media, LLC 2012 Abstract Cell surface glycoproteins are one of the most surface-capturing (CSC) technique was an approach specif- frequently observed phenomena correlated with malignant ically targeted at membrane glycoproteins involving the growth. Hepatocellular carcinoma (HCC) is one of the most affinity capture of membrane glycoproteins using glycan malignant tumors in the world. The majority of hepatocel- biotinylation labeling on intact cell surfaces. To characterize lular carcinoma cell surface proteins are modified by glyco- the cell surface glycoproteome and probe the mechanism of sylation in the process of tumor invasion and metastasis. tumor invasion and metastasis of HCC, we have modified Therefore, characterization of cell surface glycoproteins can and evaluated the cell surface-capturing strategy, and ap- provide important information for diagnosis and treatment plied it for surface glycoproteomic analysis of hepatocellu- of liver cancer, and also represent a promising source of lar carcinoma cells. In total, 119 glycosylation sites on 116 potential diagnostic biomarkers and therapeutic targets for unique glycopeptides were identified, corresponding to 79 hepatocellular carcinoma. However, cell surface glycopro- different protein species. Of these, 65 (54.6 %) new pre- teins of HCC have been seldom identified by proteomics dicted glycosylation sites were identified that had not pre- approaches because of their hydrophobic nature, poor solu- viously been determined experimentally.
    [Show full text]
  • Immunological Approaches to Biomass Characterization and Utilization
    REVIEW published: 28 October 2015 doi: 10.3389/fbioe.2015.00173 Immunological approaches to biomass characterization and utilization Sivakumar Pattathil1,2* , Utku Avci1,2 , Tiantian Zhang1 , Claudia L. Cardenas1† and Michael G. Hahn1,2 1 Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA, 2 Oak Ridge National Laboratory, BioEnergy Science Center (BESC), Oak Ridge, TN, USA Plant biomass is the major renewable feedstock resource for sustainable generation of alternative transportation fuels to replace fossil carbon-derived fuels. Lignocellulosic cell walls are the principal component of plant biomass. Hence, a detailed understanding of plant cell wall structure and biosynthesis is an important aspect of bioenergy research. Cell walls are dynamic in their composition and structure, varying considerably among Edited by: Jason Lupoi, different organs, cells, and developmental stages of plants. Hence, tools are needed that University of Queensland, USA are highly efficient and broadly applicable at various levels of plant biomass-based bioen- Reviewed by: ergy research. The use of plant cell wall glycan-directed probes has seen increasing use Xu Fang, Shandong University, China over the past decade as an excellent approach for the detailed characterization of cell Arumugam Muthu, walls. Large collections of such probes directed against most major cell wall glycans are Council of Scientific and Industrial currently available worldwide. The largest and most diverse set of such probes consists Research, India of cell wall glycan-directed monoclonal antibodies (McAbs). These McAbs can be used *Correspondence: Sivakumar Pattathil as immunological probes to comprehensively monitor the overall presence, extractability, [email protected] and distribution patterns among cell types of most major cell wall glycan epitopes using †Present address: two mutually complementary immunological approaches, glycome profiling (an in vitro Claudia L.
    [Show full text]
  • 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
    [Show full text]
  • Tnfa-Induced Mucin 4 Expression Elicits Trastuzumab Resistance in HER2-Positive Breast Cancer María F
    Published OnlineFirst October 3, 2016; DOI: 10.1158/1078-0432.CCR-16-0970 Cancer Therapy: Clinical Clinical Cancer Research TNFa-Induced Mucin 4 Expression Elicits Trastuzumab Resistance in HER2-Positive Breast Cancer María F. Mercogliano1, Mara De Martino1, Leandro Venturutti1, Martín A. Rivas2, Cecilia J. Proietti1, Gloria Inurrigarro3, Isabel Frahm3, Daniel H. Allemand4, Ernesto Gil Deza5, Sandra Ares5, Felipe G. Gercovich5, Pablo Guzman 6, Juan C. Roa6,7, Patricia V. Elizalde1, and Roxana Schillaci1 Abstract Purpose: Although trastuzumab administration improved the Results: TNFa overexpression turned trastuzumab-sensitive outcome of HER2-positive breast cancer patients, resistance cells and tumors into resistant ones. Histopathologic findings events hamper its clinical benefits. We demonstrated that TNFa revealed mucin foci in TNFa-producing tumors. TNFa induced stimulation in vitro induces trastuzumab resistance in HER2- upregulation of MUC4 that reduced trastuzumab binding to its positive breast cancer cell lines. Here, we explored the mechanism epitope and impaired ADCC. Silencing MUC4 enhanced trastu- of TNFa-induced trastuzumab resistance and the therapeutic zumab binding, increased ADCC, and overcame trastuzumab and strategies to overcome it. trastuzumab-emtansine antiproliferative effects in TNFa-overex- Experimental Design: Trastuzumab-sensitive breast cancer pressing cells. Accordingly, administration of TNFa-blocking cells, genetically engineered to stably overexpress TNFa,and antibodies downregulated MUC4 and sensitized de novo trastu- de novo trastuzumab-resistant tumors, were used to evaluate zumab-resistant breast cancer cells and tumors to trastuzumab. In trastuzumab response and TNFa-blocking antibodies effective- HER2-positive breast cancer samples, MUC4 expression was ness respectively. Immunohistochemistry and antibody-depen- found to be an independent predictor of poor disease-free survival dent cell cytotoxicity (ADCC), together with siRNA strategy, (P ¼ 0.008).
    [Show full text]
  • ADAM10 Site-Dependent Biology: Keeping Control of a Pervasive Protease
    International Journal of Molecular Sciences Review ADAM10 Site-Dependent Biology: Keeping Control of a Pervasive Protease Francesca Tosetti 1,* , Massimo Alessio 2, Alessandro Poggi 1,† and Maria Raffaella Zocchi 3,† 1 Molecular Oncology and Angiogenesis Unit, IRCCS Ospedale Policlinico S. Martino Largo R. Benzi 10, 16132 Genoa, Italy; [email protected] 2 Proteome Biochemistry, IRCCS San Raffaele Scientific Institute, 20132 Milan, Italy; [email protected] 3 Division of Immunology, Transplants and Infectious Diseases, IRCCS San Raffaele Scientific Institute, 20132 Milan, Italy; [email protected] * Correspondence: [email protected] † These authors contributed equally to this work as last author. Abstract: Enzymes, once considered static molecular machines acting in defined spatial patterns and sites of action, move to different intra- and extracellular locations, changing their function. This topological regulation revealed a close cross-talk between proteases and signaling events involving post-translational modifications, membrane tyrosine kinase receptors and G-protein coupled recep- tors, motor proteins shuttling cargos in intracellular vesicles, and small-molecule messengers. Here, we highlight recent advances in our knowledge of regulation and function of A Disintegrin And Metalloproteinase (ADAM) endopeptidases at specific subcellular sites, or in multimolecular com- plexes, with a special focus on ADAM10, and tumor necrosis factor-α convertase (TACE/ADAM17), since these two enzymes belong to the same family, share selected substrates and bioactivity. We will discuss some examples of ADAM10 activity modulated by changing partners and subcellular compartmentalization, with the underlying hypothesis that restraining protease activity by spatial Citation: Tosetti, F.; Alessio, M.; segregation is a complex and powerful regulatory tool.
    [Show full text]
  • A Stealth Cloak for Cancer Cells
    BMB Rep. 2021; 54(7): 344-355 BMB www.bmbreports.org Reports Invited Mini Review Mucin in cancer: a stealth cloak for cancer cells Dong-Han Wi1, Jong-Ho Cha2,3 & Youn-Sang Jung1,* 1Department of Life Science, Chung-Ang University, Seoul, 06974, 2Department of Biomedical Sciences, College of Medicine, Inha University, Incheon 22212, 3Department of Biomedical Science, Program in Biomedical Science and Engineering, Graduate school, Inha University, Incheon 22212, Korea Mucins are high molecular-weight epithelial glycoproteins and mucinous colorectal carcinoma (MCC) (3). Since tumor growth are implicated in many physiological processes, including epit- sites induce inhospitable conditions for them to survive, helial cell protection, signaling transduction, and tissue home- mucins are suggested as an oncogenic microenvironment that ostasis. Abnormality of mucus expression and structure contri- avoids hypoxia, acidic, and other biological hurdles. The com- butes to biological properties related to human cancer progress- position and structure of mucins enable them to mimic the ion. Tumor growth sites induce inhospitable conditions. Many surface of tumor cells like the surface of normal epithelial cells kinds of research suggest that mucins provide a microenviron- (4). Additionally, the mucus layer captures growth factors or ment to avoid hypoxia, acidic, and other biological conditions cytokines, contributing to cell growth of the tumor. Alter- that promote cancer progression. Given that the mucus layer natively, these properties interfere with the interaction bet- captures growth factors or cytokines, we propose that mucin ween the immune system and tumor cells. Indeed, a high helps to ameliorate inhospitable conditions in tumor-growing concentration of soluble mucins downregulates the motility sites.
    [Show full text]
  • Digitalcommons@UNMC Regulation of the Transmembrane Mucin MUC4
    University of Nebraska Medical Center DigitalCommons@UNMC Theses & Dissertations Graduate Studies Fall 12-18-2015 Regulation of the transmembrane mucin MUC4 by Wnt/β-catenin in gastrointestinal cancers Priya Pai University of Nebraska Medical Center Follow this and additional works at: https://digitalcommons.unmc.edu/etd Part of the Biochemistry Commons, and the Molecular Biology Commons Recommended Citation Pai, Priya, "Regulation of the transmembrane mucin MUC4 by Wnt/β-catenin in gastrointestinal cancers" (2015). Theses & Dissertations. 58. https://digitalcommons.unmc.edu/etd/58 This Dissertation is brought to you for free and open access by the Graduate Studies at DigitalCommons@UNMC. It has been accepted for inclusion in Theses & Dissertations by an authorized administrator of DigitalCommons@UNMC. For more information, please contact [email protected]. i Regulation of the transmembrane mucin MUC4 by Wnt/β- catenin in gastrointestinal cancers By PRIYA PAI A DISSERTATION Presented to the Faculty of The University of Nebraska Graduate College In Partial Fulfillment of the Requirements For the Degree of Doctor of Philosophy Department of Biochemistry and Molecular Biology Graduate Program Under the Supervision of Professor Surinder K. Batra University of Nebraska Medical Center Omaha, Nebraska November, 2015 ii Regulation of the transmembrane mucin MUC4 by Wnt/β-catenin in gastrointestinal cancers Priya Pai, PhD. University of Nebraska Medical Center, 2015 Supervisor: Surinder K. Batra, PhD. The transmembrane mucin MUC4 is a high molecular weight glycoprotein that is expressed de novo in pancreatic ductal adenocarcinoma (PDAC). MUC4 has been shown to play a tumor-promoting role in malignancies such as PDAC, ovarian cancer and breast cancer.
    [Show full text]
  • And HPV18-Infected Early Stage Cervical Cancers and Normal
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Virology 331 (2005) 269–291 www.elsevier.com/locate/yviro Gene expression profiles of primary HPV16- and HPV18-infected early stage cervical cancers and normal cervical epithelium: identification of novel candidate molecular markers for cervical cancer diagnosis and therapy Alessandro D. Santina,*, Fenghuang Zhanb, Eliana Bignottia, Eric R. Siegelc, Stefania Cane´ a, Stefania Bellonea, Michela Palmieria, Simone Anfossia, Maria Thomasd, Alexander Burnetta, Helen H. Kaye, Juan J. Romana, Timothy J. O’Briena, Erming Tianb, Martin J. Cannonf, John Shaughnessy Jr.b, Sergio Pecorellig aDivision of Gynecologic Oncology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA bMyeloma Institute for Research and Therapy, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA cDepartment of Biostatistics, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA dDepartment of Pathology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA eDepartment of Obstetrics and Gynecology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA fDepartment of Microbiology and Immunology, University of Arkansas, Little Rock, AR 72205, USA gDivision of Gynecologic Oncology, University of Brescia, Brescia, Italy Received 2 July 2004; returned to author for revision 18 August 2004; accepted 9 September 2004 Available online 21 November 2004 Abstract With the goal of identifying genes with a differential pattern of expression between invasive cervical carcinomas (CVX) and normal cervical keratinocytes (NCK), we used oligonucleotide microarrays to interrogate the expression of 14,500 known genes in 11 primary HPV16 and HPV18-infected stage IB–IIA cervical cancers and four primary normal cervical keratinocyte cultures.
    [Show full text]
  • Supplementary Table S4. FGA Co-Expressed Gene List in LUAD
    Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase
    [Show full text]
  • Designing Tools for Studying the Dynamic Glycome John F
    Marshall University Marshall Digital Scholar Chemistry Faculty Research Chemistry Winter 12-2012 Designing Tools for Studying the Dynamic Glycome John F. Rakus Marshall University, [email protected] Follow this and additional works at: http://mds.marshall.edu/chemistry_faculty Part of the Organic Chemistry Commons Recommended Citation Rakus, J. F. (2012, December). Designing tools for studying the dynamic glycome. Invited Lecture at Sonoma State University, Rohnert Park, CA. This Presentation is brought to you for free and open access by the Chemistry at Marshall Digital Scholar. It has been accepted for inclusion in Chemistry Faculty Research by an authorized administrator of Marshall Digital Scholar. For more information, please contact [email protected]. NYU Cover Cells are primarily compose of three types of biomolecules Protein (50% dry weight) HeLa cell Nucleic acid (25% dry weight) Carbohydrate (10% dry weight) Carbohydrates are pervasive and involved in many cellular interactions Holgersson et al, Immuno Cell Biol, 2005 Laughlin et al, Science, 2008 Nucleic acids and proteins are synthesized with a defined template and dedicated polymerases Macromolecule: Nucleic acid Macromolecule: polypeptide Polymerase: DNA Pol or RNA Pol Polymerase: Ribosome Template: DNA strand Template: mRNA strand Glycan biosynthesis lacks a dedicated polymerase and genetic template Formation of Glc3Man9GlcNAc2-DolPP, an intermediate in the N-linked glycosylation pathway, requires 12 separate enzymes Essentially, each linkage in an oligosaccharide is
    [Show full text]
  • Combinatorial Glycomic Analyses to Direct Cazyme Discovery for the Tailored Degradation of Canola Meal Non-Starch Dietary Polysaccharides
    microorganisms Article Combinatorial Glycomic Analyses to Direct CAZyme Discovery for the Tailored Degradation of Canola Meal Non-Starch Dietary Polysaccharides Kristin E. Low 1 , Xiaohui Xing 1,2, Paul E. Moote 1,3, G. Douglas Inglis 1,3,4 , Sivasankari Venketachalam 5,6, Michael G. Hahn 5,6,7 , Marissa L. King 1, Catherine Y. Tétard-Jones 8, Darryl R. Jones 1, William G. T. Willats 8, Bogdan A. Slominski 9 and D. Wade Abbott 1,2,4,* 1 Lethbridge Research and Development Centre, Agriculture and Agri-Food Canada, Lethbridge, AB T1J 4B1, Canada; [email protected] (K.E.L.); [email protected] (X.X.); [email protected] (P.E.M.); [email protected] (G.D.I.); [email protected] (M.L.K.); [email protected] (D.R.J.) 2 Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, AB T1K 3M4, Canada 3 Department of Agricultural, Food & Nutritional Science, University of Alberta, Edmonton, AB T6G 2P5, Canada 4 Department of Biological Sciences, University of Lethbridge, Lethbridge, AB T1K 3M4, Canada 5 Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USA; [email protected] (S.V.); [email protected] (M.G.H.) 6 Center for Bioenergy Innovation, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA 7 Department of Plant Biology, University of Georgia, Athens, GA 30602, USA 8 School of Natural and Environmental Sciences, Newcastle University, Newcastle Upon Tyne NE1 7RU, UK; [email protected] (C.Y.T.-J.); [email protected] (W.G.T.W.) 9 Department of Animal Science, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; [email protected] * Correspondence: [email protected] Received: 30 September 2020; Accepted: 20 November 2020; Published: 29 November 2020 Abstract: Canola meal (CM), the protein-rich by-product of canola oil extraction, has shown promise as an alternative feedstuff and protein supplement in poultry diets, yet its use has been limited due to the abundance of plant cell wall fibre, specifically non-starch polysaccharides (NSP) and lignin.
    [Show full text]