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Mutation of the 97‐197‐197‐1subunit of the pyruvate dehydrogenase complex, in relation to heterogeneity
Author(s) -
Kitano A.,
Endo F.,
Matsuda I.,
Miyabayashi S.,
Dahl HH. M.
Publication year - 1989
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01800710
Subject(s) - pyruvate dehydrogenase complex , protein subunit , dihydrolipoyl transacetylase , dehydrogenase , mutation , pyruvate dehydrogenase phosphatase , pyruvate decarboxylation , enzyme , pyruvate dehydrogenase lipoamide kinase isozyme 1 , branched chain alpha keto acid dehydrogenase complex , biochemistry , biology , chemistry , microbiology and biotechnology , gene
Summary Pyruvate dehydrogenase complex was studied using bio‐ and immunochemical methods in cultured cells derived from two patients with the severe type and one patient with the mild type of pyruvate dehydrogenase complex deficiency. In patients 1 and 2, enzyme activity was all but undetectable and associated with the absence of E 1α subunit of the complex. Patient 3 had a slightly reduced level of enzyme activity, and this was associated with a larger form of E 1α subunit. The amount and size of E 1α mRNA in the three patients was similar to that of control samples. Thus, the severity of E 1α deficiency in these three patients is likely to depend on the type of mutation in the pyruvate dehydrogenase E 1α subunit and the synthesis and degradation rate of the subunit.