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

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'...

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Bibliographic Details
Published in:Somatic cell and molecular genetics 1990-03, Vol.16 (2), p.97-108
Main Authors: TOWN, M, ATHANASIOU-METAXA, M, LUZZATTO, L
Format: Article
Language:English
Subjects:
Alleles
Animal cells
Animals
Biological and medical sciences
Cell cultures. Hybridization. Fusion
Cell Line
Cricetinae
Cricetulus
DNA - analysis
DNA - genetics
DNA Restriction Enzymes
Female
Fibroblasts - cytology
Fibroblasts - enzymology
Fundamental and applied biological sciences. Psychology
Gene Expression
Glucosephosphate Dehydrogenase - genetics
Glucosephosphate Dehydrogenase - metabolism
Glucosephosphate Dehydrogenase Deficiency - genetics
Glucosephosphate Dehydrogenase Deficiency - metabolism
Heterozygote
Humans
Hybrid Cells - analysis
Hybrid Cells - cytology
Hybrid Cells - enzymology
Immunoblotting
Immunohistochemistry
Molecular and cellular biology
Ovary - cytology
Ovary - enzymology
RNA, Messenger - genetics
RNA, Messenger - metabolism
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Summary: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.
ISSN:0740-7750
1572-9931
DOI:10.1007/BF01233040