Somat Cell Mol Genet. 1990 Mar;16(2):97-108.

Intragenic interspecific complementation of glucose 6-phosphate dehydrogenase in human-hamster cell hybrids.

Town M, Athanasiou-Metaxa M, Luzzatto L.

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Department of Haematology, Royal Postgraduate Medical School, Hammersmith Hospital, London, United Kingdom.

Abstract

A new variant of human glucose 6-phosphate dehydrogenase (G6PD), provisionally designated G6PD Harilaou, was observed in a Greek boy affected by severe hemolytic anemia. G6PD Harilaou was associated with very severe deficiency of enzyme activity, which measured about 1% of normal in the patient's fibroblasts. By fusion of Harilaou fibroblasts with a similarly enzyme-deficient mutant CHO cell line, we have isolated a hybrid cell line that has a G6PD activity 5-10 times higher than either of the parental cells. By electrophoretic analysis we show that most of this activity is associated with a hybrid dimeric G6PD molecule consisting of one hamster and one human subunit. We suggest that this heterologous quasi-interallelic complementation is effected by a catalytically abnormal hamster subunit stabilizing a catalytically abnormal and unstable Harilaou subunit. This approach may be useful for the study of dimer formation and stability in human G6PD.

PMID:: 2157298; [PubMed - indexed for MEDLINE]

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Cited by 2 PubMed Central articles

Somatic-cell selection is a major determinant of the blood-cell phenotype in heterozygotes for glucose-6-phosphate dehydrogenase mutations causing severe enzyme deficiency. [Am J Hum Genet. 1996]
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Identification of a single base change in a new human mutant glucose-6-phosphate dehydrogenase gene by polymerase-chain-reaction amplification of the entire coding region from genomic DNA.
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