A novel 4-methylumbelliferyl-beta-D-xyloside derivative, sulfate-O-3- xylosylbeta1-(4-methylumbelliferone), isolated from culture medium of human skin fibroblasts, and its role in methylumbelliferone-initiated glycosaminoglycan biosynthesis |
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Authors: | Tazawa T; Takagaki K; Matsuya H; Nakamura T; Sasaki M; Endo M |
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Institution: | Department of Biochemistry and Second Department of Surgery, Hirosaki University School of Medicine, Hirosaki 036-8562, Japan. |
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Abstract: | Human skin fibroblasts were incubated in the presence of 4-
methylumbelliferyl-beta-D-xyloside (Xyl-MU). The culture medium was
recovered and Xyl-MU derivatives which were initiated by the Xyl-MU acting
as a primer were purified. As a result, a novel Xyl-MU derivative was
isolated, in addition to previously reported Xyl-MU derivatives such as
glycosaminoglycan-MU, Gal-Gal-Xyl-MU, Gal-Xyl-MU, SA-Gal-Xyl-MU,
Xyl-Xyl-MU, GlcA-Xyl-MU, and sulfate-GlcA-Xyl-MU. This Xyl-MU derivative
was subjected to carbohydrate composition analysis, enzyme digestion,
ion-spray mass spectrometric analysis, and Smith degradation. The results
indicated that it was sulfate- O -3-Xyl-MU. When Xyl-MU was incubated with
35S]PAPS using a homogenate prepared from the same cultured skin
fibroblasts, 35S]sulfate- O -3-Xyl-MU was produced. Moreover, when Xyl-MU
was incubated with UDP-3H]Gal, 3H]galactose was transferred to Xyl-MU,
but when sulfate- O -3-Xyl-MU was incubated with UDP-3H]Gal, 3H]galactose
was not transferred. These results indicate that chain elongation from
Xyl-MU is inhibited by sulfation of Xyl-MU, and that Xyl-MU sulfation is
involved in the control of Xyl-MU-initiated glycosaminoglycan biosynthesis.
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