[Identification of a novel T421C mutation of α-1,3-N-acetylgalactosaminyltransferase allele responsible for an A variant].

Autor:	Wang M; Shaanxi Blood Center, Xi'an, Shaanxi 710061, P. R. China. Email: drxuhua@163.com., Chen L, Wu D, Zuo Q, Ye S, Xu H
Jazyk:	čínština
Zdroj:	Zhonghua yi xue yi chuan xue za zhi = Zhonghua yixue yichuanxue zazhi = Chinese journal of medical genetics [Zhonghua Yi Xue Yi Chuan Xue Za Zhi] 2015 Feb; Vol. 32 (1), pp. 105-8.
DOI:	10.3760/cma.j.issn.1003-9406.2015.01.023
Abstrakt:	Objective: To investigate the molecular basis of an individual featuring weak A phenotype of ABO blood group system. Methods: Serologic investigations, serum transferases activity assay and absorption-elution test were carried out to identify the ABO blood group. The 7 exons and flanking introns of ABO glycosyltransferase gene were amplified with polymerase chain reaction (PCR). The products were sequenced bidirectinally following enzyme digestion. Haplotypes of exons 6 and 7 of the ABO gene were analyzed. Results: A weak A antigen was identified on red blood cells of the proband. Eight heterozygous sites in exons 6 and 7 (261delG 297A/G, 421C/T, 467C/T, 646T/A, 681G/A, 771C/T, 829G/A) of the ABO gene were identified. Based on haplotype analysis, one allele was determined as O02, while a novel mutation 421T>C was identified in another allele, which resulted in the amino acid change Ser141Pro of the A glycosyltransferase. Conclusion: Above results suggested that amino acid substitutions resulted from a novel mutation 421T>C of the ABO gene may decrease the enzymatic activity and result in the weak A phenotype.
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu