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.
Originalsprog | Engelsk |
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Tidsskrift | F E B S Letters |
Vol/bind | 588 |
Udgave nummer | 5 |
Sider (fra-til) | 746-751 |
Antal sider | 6 |
ISSN | 0014-5793 |
DOI | |
Status | Udgivet - 3 mar. 2014 |
Emneord
- Det Sundhedsvidenskabelige Fakultet