2,8-Dihydroxyadenine lithiasis in a japanese patient heterozygous at the adenine phosphoribosyltransferase locus

• Published in: American journal of human genetics Vol. 48; no. 5; pp. 983 - 989
• Main Authors: SAHOTA, A, CHEN, J, BEHZADIAN, M. A, RAVINDRA, R, TAKEUCHI, H, STAMBROOK, P. J, TISCHFIELD, J. A
• Format: Journal Article
• Language: English
• Published: Chicago, IL University of Chicago Press 01.05.1991
• Subjects: Adenine - analogs & derivatives; Adenine - metabolism; Adenine Phosphoribosyltransferase - genetics; Adenine Phosphoribosyltransferase - metabolism; Adult; Biological and medical sciences; Genetic Carrier Screening; Heterozygote; Humans; Japan; Kidney Calculi - chemistry; Lymphocytes - enzymology; Male; Medical sciences; Metabolic diseases; Mutation - genetics; Nucleotides - metabolism; Polymorphism, Restriction Fragment Length; Asia; Japan; Human; Heterozygozity; Enzyme; Deficiency; Exploration; Metabolic diseases; Urinary stone; Polymerase chain reaction; Electrophoresis; Genetics; Mutation; Adenine phosphoribosyltransferase; Locus
• ISSN: 0002-9297; 1537-6605

All reported cases of 2,8-dihydroxyadenine (DHA) lithiasis have been due to functional homozygous deficiency of adenine phosphoribosyltransferase (APRT). Here we describe the first case of DHA lithiasis in a patient who has functional APRT activity in cultured lymphoblasts. The patient is heterozygous for Japanese-type (type II) APRT deficiency as demonstrated by starch-gel electrophoresis and DNA sequence analysis. We also demonstrate the use of starch-gel electrophoresis for differentiation between the type II mutant enzyme and the wild-type enzyme.