Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-7-19
pubmed:abstractText
The first stage in the formation of glucose from acetone involves two oxidation steps catalyzed by isozymes of the cytochrome P-450 II E1 gene subfamily; methylglyoxal formed this way is further converted to pyruvate by a reversible conjugation with reduced glutathione. The effect of methylglyoxal on glucose formation, oxidation of aminopyrine, aniline and on reduced glutathione content was investigated in isolated hepatocytes prepared from (i) fasted or (ii) fasted and acetone (known to induce isozymes of P-450 II E1 gene subfamily) pretreated mice. Glucose formation and drug oxidation were increased by methylglyoxal at concentrations below 1 mM, but were severely decreased above 1 mM. Methylglyoxal also decreased protein synthesis at concentrations above 1 mM. If the addition of methylglyoxal was combined with that of other gluconeogenic precursors and glucose the initial increasing effect on drug oxidation was moderated or diminished and the decreasing effect (at high concentrations) was enhanced. The glutathione content of the cells was decreased by methylglyoxal in a concentration dependent manner. Acetone pretreatment of mice also resulted in a decreased glutathione content of the liver. Based on these observations it is assumed that methylglyoxal has contrasting effects in hepatocytes, and can contribute to the disturbed metabolism under circumstances when the acetone production is elevated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
1092
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
284-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Effect of methylglyoxal on glucose formation, drug oxidation and glutathione content in isolated murine hepatocytes.
pubmed:affiliation
1st Institute of Biochemistry, Semmelweis University, Medical School, Budapest, Hungary.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't