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pubmed-article:9498555pubmed:abstractTextHuman skin fibroblasts were cultured with a fluorogenic xyloside, 4-methylumbelliferyl-beta-D-xyloside (Xyl-MU) as an initiator, and the effects of monensin, which destroys the normal structure of the Golgi complex, on the synthesis of Xyl-MU-initiated glycosaminoglycan (GAG-MU) and its linkage region oligosaccharides were investigated. When the cells were incubated with Xyl-MU in the presence of monensin, the synthesis of GAG-MU was inhibited. In addition, the synthesis of Galbeta1-3Galbeta1-4Xylbeta1-MU as an intermediate of GAG-MU was inhibited, whereas the synthesis of Galbeta1-4Xylbeta1-MU, which is formed prior to Galbeta1-3Galbeta1-4Xylbeta1-MU, was not. These results indicate that inhibition of GAG-MU synthesis by monensin occurs at the point where the second galactose is joined to Galbeta1-4Xylbeta1-MU.lld:pubmed
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pubmed-article:9498555pubmed:dateRevised2007-12-19lld:pubmed
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pubmed-article:9498555pubmed:articleTitleEffect of monensin on the synthesis of beta-D-xyloside-initiated glycosaminoglycan and its linkage region oligosaccharides in human skin fibroblasts.lld:pubmed
pubmed-article:9498555pubmed:affiliationDepartment of Biochemistry, Hirosaki University School of Medicine, Aomori.lld:pubmed
pubmed-article:9498555pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9498555pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed