Animal cells utilize β-D-xylosides as primers for glycosaminoglycan synthesis. However, most xylosides preferentially stimulate chondroitin sulfate synthesis and only weakly prime heparan sulfate synthesis. To test if the structure of the aglycone determines the type of glycosaminoglycan made, the priming activity of methyl, n-octyl, p-nitrophenyl, 4-methylumbelliferyl, trans, trans-farnesyl, cholesteryl, and estradiol β-D-xylosides was compared. Their potency was tested in pgsA-745 cells, a Chinese hamster ovary cell mutant unable to initiate glycosaminoglycan synthesis due to a defect in xylosyltransferase. All of the xylosides stimulated chondroitin sulfate synthesis in the mutant, but only estradiol β-D-xyloside primed heparan sulfate synthesis efficiently. When incubated with 30 μM estradiol β-D-xyloside, mutant cells made about 3-fold more glycosaminoglycan than untreated wild-type cells and as much as 50% was heparan sulfate. Estradiol β-D-xyloside also induced heparan sulfate synthesis in cycloheximide-treated wild-type Chinese hamster ovary cells, bovine aortic endothelial cells, baby hamster kidney cells, and Balb/c 3T3 fibroblasts. In addition to stimulating heparan sulfate synthesis, low concentrations of estradiol β-D-xyloside inhibited the formation of endogenous heparan sulfate proteoglycans.
|Original language||English (US)|
|Number of pages||4|
|Journal||Journal of Biological Chemistry|
|State||Published - 1991|
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology