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Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity
M. Kimura, T. Watanabe, K. Sekine, H. Ishizuka, A. Ikejiri, M. Sakaguchi, M. Kamaya, D. Yamanaka, V. Matoska, PO. Bauer, F. Oyama
Language English Country Netherlands
Document type Comparative Study, Journal Article
- MeSH
- Chitin metabolism MeSH
- Chitinases genetics metabolism MeSH
- Escherichia coli genetics growth & development MeSH
- Glycosylation MeSH
- Hexosaminidases genetics metabolism MeSH
- Humans MeSH
- Mice MeSH
- Gene Expression Regulation, Enzymologic MeSH
- Recombinant Proteins metabolism MeSH
- Amino Acid Substitution * MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Comparative Study MeSH
Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been attracting research interest due to their involvement in various pathological conditions such as Gaucher's disease and asthma, respectively. Both enzymes are highly expressed in mice, while the level of AMCase mRNA was low in human tissues. In addition, the chitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counterpart. Here, we revealed a substantially higher chitinolytic and transglycosylation activity of human Chit1 against artificial and natural chitin substrates as compared to the mouse enzyme. We found that the substitution of leucine (L) by tryptophan (W) at position 218 markedly reduced both activities in human Chit1. Conversely, the L218W substitution in mouse Chit1 increased the activity of the enzyme. These results suggest that Chit1 may compensate for the low of AMCase activity in humans, while in mice, highly active AMCase may supplements low Chit1 activity.
Bioinova Ltd Videnska 1083 Prague 142 20 Czech Republic
Department of Applied Chemistry Kogakuin University Hachioji Tokyo 192 0015 Japan
Department of Chemistry and Life Science Kogakuin University Hachioji Tokyo 192 0015 Japan
References provided by Crossref.org
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- $a Kimura, Masahiro $u Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo 192-0015, Japan; Research Fellow of Japan Society for the Promotion of Science (PD), Koujimachi, Chiyoda-ku, Tokyo 102-0083, Japan; Laboratory for Immunopharmacology of Microbial Products, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan
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- $a Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity / $c M. Kimura, T. Watanabe, K. Sekine, H. Ishizuka, A. Ikejiri, M. Sakaguchi, M. Kamaya, D. Yamanaka, V. Matoska, PO. Bauer, F. Oyama
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- $a Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been attracting research interest due to their involvement in various pathological conditions such as Gaucher's disease and asthma, respectively. Both enzymes are highly expressed in mice, while the level of AMCase mRNA was low in human tissues. In addition, the chitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counterpart. Here, we revealed a substantially higher chitinolytic and transglycosylation activity of human Chit1 against artificial and natural chitin substrates as compared to the mouse enzyme. We found that the substitution of leucine (L) by tryptophan (W) at position 218 markedly reduced both activities in human Chit1. Conversely, the L218W substitution in mouse Chit1 increased the activity of the enzyme. These results suggest that Chit1 may compensate for the low of AMCase activity in humans, while in mice, highly active AMCase may supplements low Chit1 activity.
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- $a Oyama, Fumitaka $u Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo 192-0015, Japan. Electronic address: f-oyama@cc.kogakuin.ac.jp
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