Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00023884%3A_____%2F20%3A00008775" target="_blank" >RIV/00023884:_____/20:00008775 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0141813020342653#" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813020342653#</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2020.08.173" target="_blank" >10.1016/j.ijbiomac.2020.08.173</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity

Popis výsledku v původním jazyce

Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been attracting research interest due totheir involvement invariouspathologicalconditions such as Gaucher's disease and asthma,respectively.Both en-zymes are highly expressed in mice, while the level of AMCase mRNA was low in human tissues. In addition, thechitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counter-part. Here, we revealed a substantially higher chitinolytic and transglycosylation activity of human Chit1 againstartificial and natural chitin substrates as compared to the mouse enzyme. We found that the substitution of leu-cine (L) by tryptophan (W) at position 218 markedly reduced both activities in human Chit1. Conversely, theL218W substitution in mouse Chit1 increased the activity of the enzyme. These results suggest that Chit1 maycompensate for the low of AMCase activity in humans, while in mice, highly active AMCase may supplementslow Chit1 activity.

Název v anglickém jazyce

Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity

Popis výsledku anglicky

Chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) have been attracting research interest due totheir involvement invariouspathologicalconditions such as Gaucher's disease and asthma,respectively.Both en-zymes are highly expressed in mice, while the level of AMCase mRNA was low in human tissues. In addition, thechitinolytic activity of the recombinant human AMCase was significantly lower than that of the mouse counter-part. Here, we revealed a substantially higher chitinolytic and transglycosylation activity of human Chit1 againstartificial and natural chitin substrates as compared to the mouse enzyme. We found that the substitution of leu-cine (L) by tryptophan (W) at position 218 markedly reduced both activities in human Chit1. Conversely, theL218W substitution in mouse Chit1 increased the activity of the enzyme. These results suggest that Chit1 maycompensate for the low of AMCase activity in humans, while in mice, highly active AMCase may supplementslow Chit1 activity.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30101 - Human genetics

Projekt

—

Návaznosti

N - Vyzkumna aktivita podporovana z neverejnych zdroju

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

International Journal Of Biological Macromolecules

ISSN

0141-8130

e-ISSN

—

Svazek periodika

164

Číslo periodika v rámci svazku

December

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

2895-2902

Kód UT WoS článku

000588093700272

EID výsledku v databázi Scopus

2-s2.0-85090005388