Linked Life Data

7696329

Source:http://linkedlifedata.com/resource/pubmed/id/7696329

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-4-28
pubmed:abstractText
The effects of sulfur-substituted fatty acid analogues on the subcellular distribution and activities of acetyl-CoA and propionyl-CoA hydrolases in rats fed a high carbohydrate diet were studied. Among subcellular fractions of liver homogenates from rats fed a high carbohydrate diet (20%), the acetyl-CoA and propionyl-CoA hydrolase activities are found in the mitochondrial, peroxisome-enriched and cytosolic fractions. We have shown that the subcellular distribution of acetyl-CoA hydrolase appears to be different from the distribution propionyl-CoA hydrolase activity. Thus, the highest specific activity of acetyl-CoA hydrolase was found in the mitochondrial fraction, whereas the highest specific activity of propionyl-CoA hydrolase was found in the peroxisome-enriched fraction. Rats treated with sulfur-substituted fatty acids, i.e., 3-thiadicarboxylic acid (400 mg/day per kg body weight), showed a significant increase in acetyl-CoA hydrolase activity where the peroxisomal and cytosolic hydrolases were increased 3.9- and 2.7-fold, respectively, compared to palmitic acid treated rats. Similar results were obtained with tetradecylthioacetic acid treated rats. Propionyl-CoA hydrolase activities, in rats treated with these two peroxisome proliferating fatty acid analogues showed increased activity mainly in the mitochondrial and the cytosolic subcellular fractions. Acetyl-CoA hydrolase activity was sensitive to NADH, whereas no stimulation of the propionyl-CoA hydrolase activity was observed in the presence of NADH. The hepatic amounts of acetyl-CoA, propionyl-CoA, and free CoASH were elevated after sulfur-substituted fatty acid treatment. Sulfur-substituted fatty acids also elevated the specific acetyl-CoA hydrolase activity in the mitochondrial fraction and the propionyl-CoA hydrolase activity in the light-mitochondrial fraction. These results, therefore, suggest that acetyl-CoA hydrolase and propionyl-CoA hydrolase are two distinct proteins and that these two enzymes have a multiorganelle localisation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1,10-bis(carboxymethylthiodecane), http://linkedlifedata.com/resource/pubmed/chemical/1-(carboxymethylthio)tetradecane, http://linkedlifedata.com/resource/pubmed/chemical/Acetyl Coenzyme A, http://linkedlifedata.com/resource/pubmed/chemical/Acetyl-CoA Hydrolase, http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A, http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A, http://linkedlifedata.com/resource/pubmed/chemical/Dicarboxylic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Dietary Carbohydrates, http://linkedlifedata.com/resource/pubmed/chemical/Lipids, http://linkedlifedata.com/resource/pubmed/chemical/NAD, http://linkedlifedata.com/resource/pubmed/chemical/Sulfides, http://linkedlifedata.com/resource/pubmed/chemical/Thiolester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/propionyl CoA hydrolase, http://linkedlifedata.com/resource/pubmed/chemical/propionyl-coenzyme A
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
1255
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
154-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Subcellular localisation and induction of NADH-sensitive acetyl-CoA hydrolase and propionyl-CoA hydrolase activities in rat liver under lipogenic conditions after treatment with sulfur-substituted fatty acids.
pubmed:affiliation
University of Bergen, Department of Clinical Biology, Haukeland Hospital, Norway.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't