Linked Life Data

6112081

Source:http://linkedlifedata.com/resource/pubmed/id/6112081

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1981-7-9
pubmed:abstractText
Multiple carboxylase deficiency has previously been characterized by deficient activity of three biotin-dependent enzymes: propionyl CoA carboxylase, pyruvate carboxylase and beta-methylcrotonyl CoA carboxylase. We have demonstrated that the activity of a fourth carboxylase, acetyl CoA carboxylase (ACC), is also deficient in fibroblasts from two patients with this disorder. Furthermore, ACC activity increased six- to eight-fold when cells from these patients were incubated in culture medium containing supplemental biotin. If the primary defect in multiple carboxylase deficiency is due to deficient activity of holocarboxylase synthetase, our results would indicate that there may be a common holocarboxylase synthetase, or at least a common subunit, for all the carboxylases. Finally, since ACC catalyzes the initial step in fatty acid biosynthesis, our results further suggest the importance of dietary supplementation with fatty acids in addition to treating these patients with pharmacologic doses of biotin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
147-51
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Deficient acetyl CoA carboxylase activity in multiple carboxylase deficiency.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't