Human chitotriosidase CHIT1 cross reacts with mammalian-like substrates
2014
Larsen, Tanja | Yoshimura, Yayoi | Voldborg, Bjørn G.R. | Cazzamali, Giuseppe | Bovin, Nicolai V. | Westerlind, Ulrika | Palcic, Monica M. | Leisner, Jørgen J.
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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