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Structure and function of glucose-6-phosphate dehydrogenase-deficient variants in Chinese population.

Authors :
Jiang W
Yu G
Liu P
Geng Q
Chen L
Lin Q
Ren X
Ye W
He Y
Guo Y
Duan S
Wen J
Li H
Qi Y
Jiang C
Zheng Y
Liu C
Si E
Zhang Q
Tian Q
Du C
Source :
Human genetics [Hum Genet] 2006 Jun; Vol. 119 (5), pp. 463-78. Date of Electronic Publication: 2006 Apr 11.
Publication Year :
2006

Abstract

A systematic study on the structure and function of Glucose-6-phosphate dehydrogenase (G6PD) variations was carried out in China. A total of 155,879 participants were screened for G6PD deficiency by the G6PD/6PGD ratio method and 6,683 cases have been found. The prevalence of G6PD deficiency ranged from 0 to 17.4%. With informed consent, 1,004 cases from 11 ethnic-based groups were subjected to molecular analysis. Our results showed the followings: (1) The G6PD variants are consistent across traditional ethnic boundaries, but vary in frequencies across ethnic-based groups in Chinese population, (2) The G6PD variants in Chinese population are different from those in African, European, and Indian populations, (3) A novel G6PD-deficiency mutation, 274C-->T, has been found, and (4) Denaturing high performance liquid chromatography is of great advantage to detecting G6PD-deficient mutations for diagnosis and genetic counseling. Moreover, functional analysis of the human G6PD variants showed the following: (1) The charge property, polarity, pK-radical and side-chain radical of the substituting amino acid have an effect on G6PD activity, (2) The G6PDArg459 and Arg463 play important roles in anchoring NADP+ to the catalytic domain to maintain the enzymatic activity, and (3) The sequence from codon 459 to the carboxyl terminal is essential for the enzymatic function.

Details

Language :
English
ISSN :
0340-6717
Volume :
119
Issue :
5
Database :
MEDLINE
Journal :
Human genetics
Publication Type :
Academic Journal
Accession number :
16607506
Full Text :
https://doi.org/10.1007/s00439-005-0126-5