Human chitotriosidase CHIT1 cross reacts with mammalian‐like substrates | Zendy

Larsen Tanja | Zendy; Yoshimura Yayoi | Zendy; Voldborg Bjørn G.R. | Zendy; Cazzamali Giuseppe | Zendy; Bovin Nicolai V. | Zendy; Westerlind Ulrika | Zendy; Palcic Monica M. | Zendy; Leisner Jørgen J. | Zendy

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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.

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