Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1987-12-11
pubmed:abstractText
Carnitine palmitoyltransferase (CPT) activity is located on both the outer and inner sides of the mitochondrial inner membrane and is influenced by the surrounding lipids of the inner mitochondrial membrane. Both adriamycin and galactosamine interact with mitochondrial lipids as a part of their mechanism of toxicity, and thus these agents might be expected to affect CPT activity. Addition of adriamycin to both intact rat liver and heart mitochondria (CPT-A, outer CPT) and inverted submitochondrial vesicles (CPT-B, inner CPT) depressed CPT in the forward direction of reaction (palmitoyl-l-carnitine formation), but the CPT-B activity was more sensitive to the inhibitor. Adriamycin depressed the CPT-A reverse reaction (palmitoyl-CoA formation) to 40% of control, but it had no effect on the CPT-B reverse reaction. In vivo galactosamine administration depressed CPT-A and CPT-B 20-30% and did not affect subsequent action of in vitro adriamycin. Addition of cardiolipin (0.25 to 1.0 mg/assay) increased activity of the CPT-A forward reaction of both control and galactosamine-treated rats, but it did not affect CPT-B activity. The results suggest that CPT-A and CPT-B may be influenced differently by perturbants that affect lipids of the membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3419-23
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Hepatic and cardiac carnitine palmitoyltransferase activity. Effects of adriamycin and galactosamine.
pubmed:affiliation
Department of Food Science and Human Nutrition, Washington State University, Pullman 99164-2032.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't