期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
卷 1573, 期 3, 页码 377-381出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0304-4165(02)00406-3
关键词
galactosyltransferase 1; Ehlers-Danlos syndrome; mutation
A human cDNA encoding a novel galactosyltransferase was identified based on BLAST analysis of expressed sequence tags, and the cDNA clones were isolated, showing a type H membrane protein with 327 amino acids and 38% homology to the Caenorhabditis elegans sqv-3 gene involved in vulval invagination and oocyte development. This cDNA exhibited marked galactosyltransferase activity specific for p-nitrophenyl-beta-D-xylopyranoside, and also restored glycosaminoglycan (GAG) synthesis to galactosyltransferase I-deficient CHO mutant pgsB-761 cells. The enzyme product contained beta-1,4-linked galactosyl residues, indicating that the enzyme is galactosyltransferase I (UDP-D-galactose: D-Xylose beta-1,4-D-galactosyltransferase; EC 2.4.1.133) involved in the synthesis of the GAG-protein linkage region of proteoglycans. Mutations of this gene were investigated in a case of Ehlers-Danlos syndrome (progeroid variant), since reduced activity of galactosyltransferase I had been reported in this disease by others. As expected, the patient gene contained two different mutations (A186D, L206P). The mutations showed, respectively, 10-50% and 0% of the enzyme activity compared with wild type, suggesting that galactosytransferase I (XGal-T1) is at least one of the genes responsible for Ehlers-Danlos syndrome (progeroid variant). (C) 2002 Elsevier Science B.V. All rights reserved.
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