Effect of monensin on the synthesis of beta-D-xyloside-initiated glycosaminoglycan and its linkage region oligosaccharides in human skin fibroblasts.
K Takagaki, T Tazawa, H Munakata, T Nakamura, M Endo
Index: J. Biochem. 122(6) , 1129-32, (1997)
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Abstract
Human 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.
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