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Sialidases in Vertebrates: a Family of Enzymes Tailored for Several Cell Functions*

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Provided for non-commercial research and educational use only. Not for reproduction, distribution or commercial use. This chapter was originally published in the book Advances in Carbohydrate Chemistry and Biochemistry (Volume 64). The copy attached is provided by Elsevier for the author’s benefit and for the benefit of the author’s institution, for non-commercial research, and educational use. This includes without limitation use in instruction at your institution, distribution to specific colleagues, and providing a copy to your institution’s administrator. All other uses, reproduction and distribution, including without limitation commercial reprints, selling or licensing copies or access, or posting on open internet sites, your personal or institution’s website or repository, are prohibited. For exceptions, permission may be sought for such use through Elsevier's permissions site at: http://www.elsevier.com/locate/permissionusematerial From Eugenio Monti, Erik Bonten, Alessandra D’Azzo, Roberto Bresciani, Bruno Venerando, Giuseppe Borsani, Roland Schauer and Guido Tettamanti for Several Cell Functions. In: Derek Horton, editor, Advances in Carbohydrate Chemistry and Biochemistry (Volume 64). Academic Press, 2010, p. 402. ISBN: 978-0-12-380854-7 © Copyright 2010, Elsevier Inc. Academic Press. Author's personal copy ADVANCES IN CARBOHYDRATE CHEMISTRY AND BIOCHEMISTRY, VOL. 64 SIALIDASES IN VERTEBRATES: A FAMILY OF ENZYMES TAILORED * FOR SEVERAL CELL FUNCTIONS a b b a BY EUGENIO MONTI ,ERIK BONTEN ,ALESSANDRA D’AZZO ,ROBERTO BRESCIANI , c a d BRUNO VENERANDO ,GIUSEPPE BORSANI ,ROLAND SCHAUER and e GUIDO TETTAMANTI a Department of Biomedical Science and Biotechnology, University of Brescia, 25123, Italy b Department of Genetics, St. Jude Children’s Research Hospital, Memphis, TN, 28105-2794, USA c Department of Medical Chemistry, Biochemistry and Biotechnology, University of Milan, Segrate, 20090, Italy d Institute of Biochemistry, University of Kiel, Kiel, D-24098, Germany e Laboratory of Stem Cells for Tissue Engineering, IRCCS Policlinico San Donato, San Donato Milanese, 20097, Italy I. Introduction 405 II. The Lysosomal Sialidase NEU1 406 1. Background 406 2. Lysosomal Routing and Formation of the Multienzyme Complex 409 3. Human NEU1 Deficiency 411 4. New Functions of NEU1 in Tissue Remodeling and Homeostasis 413 5. Mouse Model of NEU1 Deficiency and Study of Disease Pathogenesis 418 III. The Cytosolic Sialidase NEU2 422 1. General Properties of NEU2 422 2. Crystal Structure of Human Sialidase NEU2 423 3. Functional Implication of NEU2 425 IV. The Plasma Membrane-Associated Sialidase NEU3 429 1. General Properties of NEU3 429 2. Functional Implication of NEU3 431 V. The Particulate Sialidase NEU4 435 1. General Properties of NEU4 435 2. Functional Implication of NEU4 436 VI. Sialidases and Cancer 438 VII. Sialidases and Immunity 439 VIII. Further Evidence for Possible Functional Implications of Sialidases 442 IX. In silico Analysis of Sialidase Gene Expression Patterns 444 X. Amino Acid Sequence Variants in Human Sialidases 448 XI. Sialidases in Teleosts 449 ISBN: 978-0-12-380854-7 DOI: 10.1016/S0065-2318(10)64007-3 403 � 2010 Elsevier Inc. All rights reserved. Author's personal copy 404 EUGENIO MONTI ET AL. XII. Trans-sialidases: What Distinguishes Them from Sialidases? 452 XIII. Final Remarks 459 References 460 ABBREVIATIONS 9-OAcGD3, 9-O-acetylated disialo-ganglioside GD3; ACF, aberrant crypt foci; AKT, serine/theonine-specific protein kinase family; ALL, acute lymphoblastic leukemia; ARIs, axon regeneration inhibitors; ASMC, aortic smooth muscle cells; BCL-2, B-cell leukemia/lymphoma 2 integral membrane protein; BM, bone mar­ row; BMT, bone marrow transplantation; BMEF, bone marrow extracellular fluid; CD, cluster of differentiation; CFU-E, colony-forming unit-erythroid cells; CG, cathepsin G; CHO, Chinese Hamster Ovary (cells); CSER, cell-surface elastin receptor; DRMs, detergent-resistant microdomains; EBP, Elastin-Binding Protein; EBP, human gene encoding the Elastin-Binding Protein; EGF, epidermal growth factor; EGFR, epidermal growth-factor receptor; ELISA, enzyme-linked immuno­ sorbent assay; EMH, extramedullary hematopoiesis; ER, endoplasmic reticulum; ERK, extracellular signal-regulated kinase; EST, Expressed Sequence Tag; β-GAL, human gene encoding the β-galactosidase; β-GAL, β-galactosidase; GEMs, glyco­ sphingolipid-enriched microdomains; GS, galactosialidosis; HeLa, cell line was derived from cervical cancer cells taken from a patient named Henrietta Lacks; HLA, human leukocyte antigen; HPCs, hematopoietic progenitor cells; ICAM-1, Intercellular Adhesion Molecule 1 (also known as cluster of differentiation 54 (CD54)); IFN, interferon; IGF-1R, receptor of insulin-like growth factor-1; IL, interleukin; JNK, protein kinase member of the MAP kinase; LacCer, lacto­ syl-ceramide; LAMP, lysosome-associated membrane protein; Lex,Lewisx anti­ gens; LIMP, lysosome integral membrane protein; M6P, mannose 6-phosphate; MAG, myelin-associated glycoprotein; MAPK, mitogen-activated protein kinase; MEK, mitogen-activated or extracellular signal-regulated protein kinase; MHC, major histocompatibility complex; MMP9, gene encoding the matrix metallopro­ teinase-9; MMP9, matrix metalloproteinase-9; MU, methylumbelliferone; NCAM, neural cell adhesion molecule; NCBI, National Center for Biotechnology Informa­ tion; NE, neutrophil elastase; NEU1, gene encoding the lysosomal sialidase; NEU1, human lysosomal sialidase; Neu1, mouse gene encoding the mouse lysosomal Author contributions: Erik Bonten and Alessandra D’Azzo contributed Section II. Giuseppe Borsani contributed Sections IX–X. Roland Schauer contributed Section XII. The remaining authors, together with Giuseppe Borsani, contributed the other sections. Author's personal copy SIALIDASES IN VERTEBRATES 405 sialidase; Neu1, mouse lysosomal sialidase; Neu5Ac, N-acetylneuraminic acid; NGF, nerve growth factor; NMR, nuclear magnetic resonance; nsSNP, non-synon­ ymous single nucleotide polymorphism; PAG, phosphoprotein associated with GEMs; PDGF, platelet-derived growth factor; PDGFR, platelet-derived growth- factor receptor; PI3K, phosphoinositide-3 kinase; PKC, protein kinase C; PLC, phosphoinositide-specific phospholipase C; PMA, phorbol 12-tetradecanoate 13-acetate; PPCA, protective protein/cathepsin A; Rac, subfamily of the Rho family of GTPases; RD, cell line derived from a human rhabdomyosarcoma; RMS, rhabdomyosarcoma; RSV, respiratory syncytial virus; RT-PCR, reverse tran­ scription-polymerase chain reaction; SFK, Src family protein tyrosine kinases; x x shRNA, short hairpin RNA; sLe , sialyl Lewis antigens; SNP, single nucleotide polymorphism; TERMs, tetraspanin-enriched microdomains; THP-1, human acute monocytic leukemia cell line; TLR, toll-like receptor; TNF, tumor necrosis factor; TrKA, high-affinity catalytic receptor for nerve growth factor; TS, trans-sialidase; Tsk, tight-skin (mouse); VCAM, vascular cell adhesion molecule; VSMC, vascular smooth muscle cells. NOTE Gene and protein symbols are reported according to: H. M. Wain, E. A. Bruford, R. C. Lovering, M. J. Lush, M. W. Wright, and S. Povey, Guidelines for human gene nomenclature, Genomics 79 (2002) 464–470; Refer Guidelines for Nomenclature of Genes, Genetic Markers, Alleles, and Muta­ tions in Mouse and Rat at the Mouse Genome Informatics (MGI) website (http://www. informatics.jax.org/mgihome/nomen/gene.shtml); and Zebrafish Nomenclature Guidelines at the ZFIN website (http://zfin.org/zf_info/nomen.html). Ganglioside nomenclature is according to: L. Svennerholm, Ganglioside designation, Adv. Exp. Med. Biol. 125 (1980) 11. I. INTRODUCTION Sialidases or neuraminidases (EC 3.2.1.18; N-acylneuraminyl glycohydrolases) are a family of exo-glycosidases that catalyze the hydrolytic cleavage of non-reducing sialic acid residues1 ketosidically linked to the saccharide chains of glycoproteins and glycolipids (gangliosides) as well as to oligo- and poly-saccharides. They are widely distributed in nature, from viruses and microorganisms (such as bacteria, protozoa, and fungi) to vertebrates, but are absent in plants, insects, and yeast.2 The molecular Author's personal copy 406 EUGENIO MONTI ET AL. cloning of several mammalian sialidases since 1993 and the great development that 3,4 followed early afterward has been summarized in two reviews. In vertebrates, mammalian sialidases and their target substrates have been impli­ cated in crucial biological processes, including the regulation of cell proliferation/­ differentiation, clearance of plasma proteins, control of cell adhesion, metabolism of gangliosides and glycoproteins, immunocyte function, modification of receptors, and the developmental modeling of myelin. The pivotal and diverse functions of these enzymes, many of which have not yet been discovered, probably account for the existence of four mammalian sialidases, encoded by different genes and defined as lysosomal (NEU1), cytosolic (NEU2), plasma-membrane (NEU3), and mitochondrial/­ lysosomal/-intracellular membranes (NEU4). These enzymes differ in their subcellular localizations, pH optima, kinetic properties, responses to ions and detergents, and substrate specificities. There appears to be little overlap in function of the individual sialidases, even though they share a common mechanism of action. Here we survey the data published since 2002 on vertebrate (mainly mammalian) sialidase biology. The subject is organized as follows: (i) a description of the four different sialidase forms and their functional
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    University of Groningen Gestational diabetes mellitus and fetoplacental vasculature alterations Silva Lagos, Luis DOI: 10.33612/diss.113056657 IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2020 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Silva Lagos, L. (2020). Gestational diabetes mellitus and fetoplacental vasculature alterations: Exploring the role of adenosine kinase in endothelial (dys)function. University of Groningen. https://doi.org/10.33612/diss.113056657 Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 26-09-2021 Adenosine kinase and cardiovascular fetal programming in gestational diabetes mellitus Luis Silva1,2, Torsten Plösch3, Fernando Toledo1,4, Marijke M. Faas2,3, Luis Sobrevia1,5,6 1 Cellular and Molecular Physiology Laboratory (CMPL), Department of Obstetrics, Division of Obstetrics and Gynaecology, School of Medicine, Faculty of Medicine, Pontificia Universidad Católica de Chile, Santiago 8330024, Chile.
  • Neuraminidase Inhibitor Zanamivir Ameliorates Collagen-Induced Arthritis

    Neuraminidase Inhibitor Zanamivir Ameliorates Collagen-Induced Arthritis

    International Journal of Molecular Sciences Article Neuraminidase Inhibitor Zanamivir Ameliorates Collagen-Induced Arthritis Bettina Sehnert 1,*, Juliane Mietz 1, Rita Rzepka 1, Stefanie Buchholz 1, Andrea Maul-Pavicic 1, Sandra Schaffer 1, Falk Nimmerjahn 2 and Reinhard E. Voll 1,* 1 Department of Rheumatology and Clinical Immunology, Medical Center–University of Freiburg, Faculty of Medicine, University of Freiburg, 79106 Freiburg, Germany; [email protected] (J.M.); [email protected] (R.R.); [email protected] (S.B.); [email protected] (A.M.-P.); [email protected] (S.S.) 2 Department of Biology, Institute of Genetics, Friedrich-Alexander University Erlangen-Nürnberg (FAU), 91058 Erlangen, Germany; [email protected] * Correspondence: [email protected] (B.S.); [email protected] (R.E.V.); Tel.: +49-761-270-71021 (B.S.); +49-761-270-34490 (R.E.V.) Abstract: Altered sialylation patterns play a role in chronic autoimmune diseases such as rheumatoid arthritis (RA). Recent studies have shown the pro-inflammatory activities of immunoglobulins (Igs) with desialylated sugar moieties. The role of neuraminidases (NEUs), enzymes which are responsible for the cleavage of terminal sialic acids (SA) from sialoglycoconjugates, is not fully understood in RA. We investigated the impact of zanamivir, an inhibitor of the influenza virus neuraminidase, and mammalian NEU2/3 on clinical outcomes in experimental arthritides studies. The severity of arthritis was monitored and IgG titers were measured by ELISA. (2,6)-linked SA was determined on IgG by ELISA and on cell surfaces by flow cytometry. Zanamivir at a dose of 100 mg/kg (zana- Citation: Sehnert, B.; Mietz, J.; 100) significantly ameliorated collagen-induced arthritis (CIA), whereas zana-100 was ineffective Rzepka, R.; Buchholz, S.; in serum transfer-induced arthritis.