Primary hepatocytes from mice lacking cysteine dioxygenase show increased cysteine concentrations and higher rates of metabolism of cysteine to hydrogen sulfide and thiosulfate

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F14%3A10285448" target="_blank" >RIV/00216208:11110/14:10285448 - isvavai.cz</a>

Alternative codes found

RIV/00064165:_____/14:10285448

Result on the web

<a href="http://dx.doi.org/10.1007/s00726-014-1700-8" target="_blank" >http://dx.doi.org/10.1007/s00726-014-1700-8</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00726-014-1700-8" target="_blank" >10.1007/s00726-014-1700-8</a>

Result language

angličtina

Original language name

Primary hepatocytes from mice lacking cysteine dioxygenase show increased cysteine concentrations and higher rates of metabolism of cysteine to hydrogen sulfide and thiosulfate

Original language description

The oxidation of cysteine in mammalian cells occurs by two routes: a highly regulated direct oxidation pathway in which the first step is catalyzed by cysteine dioxygenase (CDO) and by desulfhydration-oxidation pathways in which the sulfur is released ina reduced oxidation state. To assess the effect of a lack of CDO on production of hydrogen sulfide (H2S) and thiosulfate (an intermediate in the oxidation of H2S to sulfate) and to explore the roles of both cystathionine gamma-lyase (CTH) and cystathionine beta-synthase (CBS) in cysteine desulfhydration by liver, we investigated the metabolism of cysteine in hepatocytes isolated from Cdo1-null and wild-type mice. Hepatocytes from Cdo1-null mice produced more H2S and thiosulfate than did hepatocytes from wild-type mice. The greater flux of cysteine through the cysteine desulfhydration reactions catalyzed by CTH and CBS in hepatocytes from Cdo1-null mice appeared to be the consequence of their higher cysteine levels, which were due to th

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

—

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2014

Confidentiality

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

Name of the periodical

Amino Acids

ISSN

0939-4451

e-ISSN

—

Volume of the periodical

46

Issue of the periodical within the volume

5

Country of publishing house

AT - AUSTRIA

Number of pages

13

Pages from-to

1353-1365

UT code for WoS article

000334516700022

EID of the result in the Scopus database

—