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Human chitotriosidase CHIT1 cross reacts with mammalian‐like substrates
Author(s) -
Larsen Tanja,
Yoshimura Yayoi,
Voldborg Bjørn G.R.,
Cazzamali Giuseppe,
Bovin Nicolai V.,
Westerlind Ulrika,
Palcic Monica M.,
Leisner Jørgen J.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.12.035
Subject(s) - chitinase , glycoconjugate , pathogenesis , glycoprotein , chitin , n acetylglucosamine , glycolipid , glycosylation , enzyme , microbiology and biotechnology , biochemistry , biology , chemistry , immunology , chitosan
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 p NP‐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.