Myopathy and parkinsonism in phosphoglycerate kinase deficiency

Abstract

A 25-year-old man with exertional myoglobinuria had no evidence of hemolytic anemia, but he had severe parkinsonism that was responsive to levodopa. Phosphoglycerate kinase (PGK) activity was markedly decreased in muscle, and molecular analysis of the PGK1 gene identified the p.T378P mutation that was recently reported in a patient with isolated myopathy. This case reinforces the concept that PGK deficiency is a clinically heterogeneous disorder and raises the question of a relationship between PGK deficiency and idiopathic juvenile Parkinson disease.

FIGURE 1.

(A) Sequence of part of exon 10 of the PGK1 gene. The arrow indicates the hemizygous A>C mutation at nt position 1132 that changes an encoded threonine to a proline at amino acid position 378. (B) The region of the Pgk1 peptide containing the T378P mutation is aligned with sequences of Pgk1 proteins from other species.