-
Je něco špatně v tomto záznamu ?
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
Jazyk angličtina Země Nizozemsko
Typ dokumentu srovnávací studie, časopisecké články
- MeSH
- chitin metabolismus MeSH
- chitinasy genetika metabolismus MeSH
- Escherichia coli genetika růst a vývoj MeSH
- glykosylace MeSH
- hexosaminidasy genetika metabolismus MeSH
- lidé MeSH
- myši MeSH
- regulace genové exprese enzymů MeSH
- rekombinantní proteiny metabolismus MeSH
- substituce aminokyselin * MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- srovnávací studie 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
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc21019728
- 003
- CZ-PrNML
- 005
- 20210830101326.0
- 007
- ta
- 008
- 210728s2020 ne f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1016/j.ijbiomac.2020.08.173 $2 doi
- 035 __
- $a (PubMed)32853624
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a ne
- 100 1_
- $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
- 245 10
- $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
- 520 9_
- $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.
- 650 12
- $a substituce aminokyselin $7 D019943
- 650 _2
- $a zvířata $7 D000818
- 650 _2
- $a chitin $x metabolismus $7 D002686
- 650 _2
- $a chitinasy $x genetika $x metabolismus $7 D002688
- 650 _2
- $a Escherichia coli $x genetika $x růst a vývoj $7 D004926
- 650 _2
- $a regulace genové exprese enzymů $7 D015971
- 650 _2
- $a glykosylace $7 D006031
- 650 _2
- $a hexosaminidasy $x genetika $x metabolismus $7 D006596
- 650 _2
- $a lidé $7 D006801
- 650 _2
- $a myši $7 D051379
- 650 _2
- $a rekombinantní proteiny $x metabolismus $7 D011994
- 655 _2
- $a srovnávací studie $7 D003160
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Watanabe, Takashi $u Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo 192-0015, Japan
- 700 1_
- $a Sekine, Kazutaka $u Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo 192-0015, Japan
- 700 1_
- $a Ishizuka, Hitomi $u Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo 192-0015, Japan
- 700 1_
- $a Ikejiri, Aoi $u Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo 192-0015, Japan
- 700 1_
- $a Sakaguchi, Masayoshi $u Department of Chemistry and Life Science, Kogakuin University, Hachioji, Tokyo 192-0015, Japan
- 700 1_
- $a Kamaya, Minori $u Department of Applied Chemistry, Kogakuin University, Hachioji, Tokyo 192-0015, Japan
- 700 1_
- $a Yamanaka, Daisuke $u Laboratory for Immunopharmacology of Microbial Products, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo 192-0392, Japan
- 700 1_
- $a Matoska, Vaclav $u Laboratory of Molecular Diagnostics, Department of Clinical Biochemistry, Hematology and Immunology, Homolka Hospital, Roentgenova 37/2, Prague 150 00, Czech Republic
- 700 1_
- $a Bauer, Peter O $u Laboratory of Molecular Diagnostics, Department of Clinical Biochemistry, Hematology and Immunology, Homolka Hospital, Roentgenova 37/2, Prague 150 00, Czech Republic; Bioinova Ltd., Videnska 1083, Prague 142 20, Czech Republic
- 700 1_
- $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
- 773 0_
- $w MED00002295 $t International journal of biological macromolecules $x 1879-0003 $g Roč. 164, č. - (2020), s. 2895-2902
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/32853624 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y p $z 0
- 990 __
- $a 20210728 $b ABA008
- 991 __
- $a 20210830101326 $b ABA008
- 999 __
- $a ok $b bmc $g 1690521 $s 1140174
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2020 $b 164 $c - $d 2895-2902 $e 20200824 $i 1879-0003 $m International journal of biological macromolecules $n Int J Biol Macromol $x MED00002295
- LZP __
- $a Pubmed-20210728
