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Human chitotriosidase CHIT1 cross reacts with mammalian-like substrates.
Larsen, Tanja; Yoshimura, Yayoi; Voldborg, Bjørn G R; Cazzamali, Giuseppe; Bovin, Nicolai V; Westerlind, Ulrika; Palcic, Monica M; Leisner, Jørgen J.
Afiliação
  • Larsen T; Department of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Grønnegaardsvej 15, 1870 Frederiksberg C, Denmark.
  • Yoshimura Y; Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-1799 Copenhagen V, Denmark.
  • Voldborg BG; Novo Nordisk Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen N, Denmark.
  • Cazzamali G; Novo Nordisk Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen N, Denmark.
  • Bovin NV; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow 117997, Russian Federation.
  • Westerlind U; Gesellschaft zur Förderung der Analytischen Wissenschaften e.V., ISAS - Leibniz Institute for Analytical Sciences, Otto-Hahn-Str. 6b, D-44227 Dortmund, Germany.
  • Palcic MM; Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-1799 Copenhagen V, Denmark.
  • Leisner JJ; Department of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Grønnegaardsvej 15, 1870 Frederiksberg C, Denmark. Electronic address: jjl@sund.ku.dk.
FEBS Lett ; 588(5): 746-51, 2014 Mar 03.
Article em En | MEDLINE | ID: mdl-24462685
ABSTRACT
Humans do not synthesize chitin, yet they produce a number of active and inactive chitinases. One of the active enzymes is chitotriosidase whose serum levels are elevated in a number of diseases such as Gaucher's disease and upon fungal infection. Since the biological role of chitotriosidase in disease pathogenesis is not understood we screened a panel of mammalian GlcNAc-containing glycoconjugates as alternate substrates. LacNAc and LacdiNAc-terminating substrates are hydrolyzed, the latter with a turnover comparable to that of pNP-chitotriose. Glycolipids or glycoproteins with LacNAc and LacdiNAc represent potential chitinase substrates and the subsequent alteration of glycosylation pattern could be a factor in disease pathogenesis.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Hexosaminidases Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Hexosaminidases Idioma: En Ano de publicação: 2014 Tipo de documento: Article