Linked Life Data

8888280

Source:http://linkedlifedata.com/resource/pubmed/id/8888280

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-2-18
pubmed:abstractText
Carnitine palmitoyltransferase (CPT) consists of two activities located in the outer (CPT I) and the inner (CPT II) mitochondrial membranes. CPT II deficiency in the adult as well as in the infantile form of the disease has been shown to result from mutations in the CPT II cDNA. Nothing is known regarding the genetic defect in CPT I deficiency. We carried out complementation experiments between CPT I- and infantile CPT II-deficient cell lines. Restoration of 3H2O release from [9,10(n)-3H]-palmitate was chosen as criterion of complementation. As expected, no complementation was observed in heteropolykaryons resulting from fusions between CPT II-deficient cells. Similar results were obtained in fusions between CPT I-deficient cells, suggesting that the enzymatic defect in these cell lines results from mutations in the same gene. Conversely, complementation was observed in fusions between CPT I- and CPT II-deficient cells. These data support that CPT I and CPT II defects result from mutations in distinct genes. Palmitate oxidation by control or CPT I-deficient cell lines was decreased when cocultured with infantile CPT II-deficient cell lines. This effect, not observed in coculture including an adult CPT II-deficient cell line, was carnitine-dependent. The possible mechanism of this effect, suppressed by a high carnitine concentration, is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0031-3998
pubmed:author
pubmed:issnType
Print
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
542-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Complementation analysis of carnitine palmitoyltransferase I and II defects.
pubmed:affiliation
Laboratoire de Biochimie, CHU de Bicêtre, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't