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Molecular genetic studies in muscle phosphoglycerate mutase (PGAM‐M) deficiency
Author(s) -
Tsujino Seiichi,
Shanske Sara,
Sakoda Saburo,
Toscano Antonio,
DiMauro Salvatore
Publication year - 1995
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880181412
Subject(s) - phosphoglycerate mutase , missense mutation , nonsense mutation , genetics , mutation , compound heterozygosity , nonsense , myoglobinuria , heterozygote advantage , biology , genotype , myopathy , gene , biochemistry , glycolysis , medicine , enzyme , rhabdomyolysis
Phosphoglycerate mutase (PGAM; EC 2.7.5.3) catalyzes the interconversion of 2‐phosphoglycerate and 3‐phosphoglycerate in the glycolytic pathway. Hereditary muscle PGAM deficiency has been identified in 9 patients with myopathy. All patients had exercise introlerance and 6 had myoglobinuria. Seven of the 9 patients were African‐Americans: 5 of them were homozygous for a nonsense mutation, TGG(Trp) to TAG at codon 78; 1 was a compound heterozygote for the nonsense mutation and a missense mutation, GAG(Glu) to GCG(Ala) at codon 89; and 1 could not be tested. The only 2 Caucasian patients, a brother and sister, were homozygous for a different missense mutation, CGG(Arg) to TGG(Trp) at codon 90. Despite the small number of patients identified, these findings indicate that there is a common mutation in African‐Americans while there may be molecular genetic heterogeneity in other ethnic groups. © 1995 John Wiley & Sons, Inc.