Human chitotriosidase CHIT1 cross reacts with mammalian-like substrates.
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.
Department of Veterinary Disease Biology, Faculty of Health and Medical Sciences, University of Copenhagen, Grønnegaardsvej 15, 1870 Frederiksberg C, Denmark.
Tanja
T
Larsen
Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-1799 Copenhagen V, Denmark.
Yayoi
Y
Yoshimura
Novo Nordisk Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen N, Denmark.
Bjørn G R
BG
Voldborg
Novo Nordisk Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3b, DK-2200 Copenhagen N, Denmark.
Giuseppe
G
Cazzamali
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow 117997, Russian Federation.
Nicolai V
NV
Bovin
Gesellschaft zur Förderung der Analytischen Wissenschaften e.V., ISAS - Leibniz Institute for Analytical Sciences, Otto-Hahn-Str. 6b, D-44227 Dortmund, Germany.
Ulrika
U
Westerlind
Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-1799 Copenhagen V, Denmark.
Monica M
MM
Palcic
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.
Jørgen J
JJ
Leisner
D002236:Carbohydrate Conformation; D004187:Disaccharides / Q000737:chemistry; D006017:Glycolipids / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry; D057809:HEK293 Cells; D006596:Hexosaminidases / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D009596:Nitrophenols / Q000737:chemistry; D013379:Substrate Specificity
D004187:Disaccharides; D006017:Glycolipids; D006023:Glycoproteins; D009596:Nitrophenols; D006596:Hexosaminidases; C086400:chitotriosidase
Chitinases; Family 18 glycosidases; GlcNAc-containing substrates; Glycoconjugates; Kinetics; LacNAc; LacdiNAc