Three new exon 10 glucose-6-phosphate dehydrogenase mutations. Blood Cells Mol Dis 1995;21(1):64-72
Date
01/01/1995Pubmed ID
7655862DOI
10.1006/bcmd.1995.0010Scopus ID
2-s2.0-0029003588 (requires institutional sign-in at Scopus site) 22 CitationsAbstract
Three previously undescribed mutations of the glucose-6-phosphate dehydrogenase (G6PD) gene have been documented in patients with hereditary non-spherocytic hemolytic anemia (HNSHA). In none of the cases have we been able to obtain a sufficient volume of blood to characterize the residual enzyme biochemically. "G6PD Calvo Mackenna" was due to an A-->G transition in cDNA nucleotide 1138 creating an Aat II site and resulting in a substitution of valine for isoleucine at amino acid 380. "G6PD Riley" was due to a T-->C transition at cDNA nucleotide 1139 also changing the 380 isoleucine, in this case to a threonine. "G6PD Wisconsin" was due to an C-->G transversion in cDNA nucleotide 1177, destroying a Aci I site and resulting in a substitution of glycine for arginine at amino acid 393. All of these mutations were in exon 10, where mutations that cause HNSHA appear to be clustered. We present a list of the 83 mutations of G6PD that have been documented to the end of April, 1995.
Author List
Beutler E, Westwood B, Melemed A, Dal Borgo P, Margolis DAuthor
David A. Margolis MD Chair, Professor in the Pediatrics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Anemia, Hemolytic, Congenital NonspherocyticChild
Child, Preschool
DNA Mutational Analysis
DNA, Complementary
Erythroblastosis, Fetal
Exons
Glucosephosphate Dehydrogenase
Glucosephosphate Dehydrogenase Deficiency
Humans
Infant, Newborn
Male
Polymorphism, Single-Stranded Conformational