Linked Life Data

1508605

Source:http://linkedlifedata.com/resource/pubmed/id/1508605

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-9-22
pubmed:abstractText
Defects in pyruvate dehydrogenase, the first catalytic component of the pyruvate dehydrogenase complex, are the most common cause of pyruvate dehydrogenase complex deficiency. A family with variable pyruvate dehydrogenase complex deficiency had been described in which cultured skin fibroblasts of affected family members had normal pyruvate dehydrogenase complex activity, but different tissues and blood lymphocytes had significantly diminished activities. Enzymatic activity and immunoblot studies indicated that pyruvate dehydrogenase was affected. Further evidence is presented here showing that the defect affecting pyruvate dehydrogenase complex activity is posttranscriptional. Sequencing of the coding region of the alpha-subunit of pyruvate dehydrogenase revealed a point mutation in the codon for amino acid 234 resulting in a substitution of glycine for arginine. Study of other members of the family suggested that this mutation is inherited in a sex-linked mode. The point mutation is located in a highly conserved region of the pyruvate dehydrogenase alpha-subunit gene that contains both hydrophobic and positively charged amino acid residues. Variable expression of pyruvate dehydrogenase complex deficiency in this case may be due to instability of the pyruvate dehydrogenase heterotetramer in specific tissues because of a disruption in subunit-subunit interaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0031-3998
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
169-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
A mutation in the E1 alpha subunit of pyruvate dehydrogenase associated with variable expression of pyruvate dehydrogenase complex deficiency.
pubmed:affiliation
Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't