2,8-Dihydroxyadenine lithiasis in a Japanese patient heterozygous at the adenine phosphoribosyltransferase locus.
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.
Sahota
A
A
Department of Medical Genetics, Indiana University School of Medicine, Indianapolis 46202-5251.
Chen
J
J
Behzadian
M A
MA
Ravindra
R
R
Takeuchi
H
H
Stambrook
P J
PJ
Tischfield
J A
JA
D000225:Adenine / Q000031:analogs & derivatives* / Q000378:metabolism; D000228:Adenine Phosphoribosyltransferase / Q000235:genetics* / Q000378:metabolism; D000328:Adult; D006580:Genetic Carrier Screening; D006579:Heterozygote; D006801:Humans; D007564:Japan; D007669:Kidney Calculi / Q000737:chemistry*; D008214:Lymphocytes / Q000201:enzymology; D008297:Male; D009154:Mutation / Q000235:genetics; D009711:Nucleotides / Q000378:metabolism; D012150:Polymorphism, Restriction Fragment Length
D009711:Nucleotides; C002993:2,8-dihydroxyadenine; D000228:Adenine Phosphoribosyltransferase; D000225:Adenine