Sulfation of sialyl lactosamine oligosaccharides by chondroitin 6-sulfotransferase.
Sulfation of sialyl lactosamine oligosaccharides by chondroitin 6-sulfotransferase.
复制标题
软骨素 6-磺基转移酶对唾液酸乳糖胺寡糖进行硫酸化。
作者：
O. Habuchi;Y. Suzuki;M. Fukuta
我们先前已经证明，软骨素6-磺酸转移酶(C6ST)不仅催化硫酸盐转移到软骨素的GalNAc残基的第6位，而且还催化硫酸盐转移到角蛋白的GalNAc残基的第6位。在本研究中，我们用C6ST考察了唾液酸乳糖胺低聚糖的硫酸盐化反应。C6ST催化硫酸盐转移到NeuAcα2-3Galβ1-4GlcNAc(SLN)，NeuAcα2-3Galβ1-4GlcNAcβ1-3Galβ1-4GlcNAc(SL1L1)，NeuAcα2-3Galβ1-4(6-磺酸)GlcNAcβ1-3(6-磺酸)Galβ1-4(6-磺酸)GlcNAc(SL2L4)，但不转移到NeuAcα2-3Gal Beta 1-4(Fucα1-3)GlcNAc(SLE(X))。SLN形成的硫酸产物用神经氨酸酶降解，用NaBH4还原。得到的二糖硫酸酯在SAX-HPLC中的保留时间与[~3H]Gal(6SO4)β1-4GlcNAc-ol的保留时间相同。由SLN形成的硫酸产物还通过神经氨酸酶消化、肼分解、脱氨和NaBH4还原的反应序列进行降解。最终产物用[~3H]Gal(6SO4)β1-4脱水甘露醇在SAX-HPLC中洗脱。这些观察结果表明，C6ST可以将硫酸盐转移到SLN的Gal残基的第6位。硫酸盐在SL2L4中的掺入比在SL1L1中的掺入要高得多，这表明附着在相邻GlcNAc残基上的硫酸盐部分可能会刺激硫酸盐向Gal残基的转移。重组C6ST还催化唾液酸乳糖胺低聚糖的硫化，表明单一蛋白质催化软骨素、硫酸角蛋白和唾液酰乳糖胺低聚糖的硫化。这些结果表明，C6ST可能是L-选择素的硫酸唾液酸化Lewis x配体生物合成的候选者之一。
We have previously shown that chondroitin 6-sulfotransferase (C6ST) catalyzes transfer of sulfate not only to position 6 of GalNAc residue of chondroitin but also to position 6 of Gal residue of keratan sulfate. In this study, we examined the sulfation of sialyl lactosamine oligosaccharides by C6ST. C6ST catalyzed transfer of sulfate to NeuAc alpha 2-3Gal beta 1-4GlcNAc (SLN), NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-3Gal beta 1-4GlcNAc (SL1L1), NeuAc alpha 2-3Gal beta 1-4(6-sulfo)GlcNAc beta 1-3(6-sulfo)Gal beta 1-4(6-sulfo)GlcNAc (SL2L4), and their desialylated derivatives, but not to NeuAc alpha 2-3Gal beta 1-4(Fuc alpha 1-3)GlcNAc (SLe(x)). The sulfated product formed from SLN was degraded with neuraminidase and reduced with NaBH4. The resulting sulfated disaccharide alditol showed the same retention time in SAX-HPLC as that of [3H]Gal(6SO4) beta 1-4GlcNAc-ol. The sulfated product formed from SLN was also degraded by a reaction sequence of neuraminidase digestion, hydrazinolysis, deamination, and NaBH4 reduction. The final product was coeluted with [3H]Gal(6SO4) beta 1-4anhydromannitol in SAX-HPLC. These observations show that C6ST could transfer sulfate to position 6 of Gal residue of SLN. Incorporation of sulfate into SL2L4 was much higher than the incorporation into SL1L1, suggesting that sulfate moiety attached to adjacent GlcNAc residue may stimulate the transfer of sulfate to Gal residue. The recombinant C6ST also catalyzed sulfation of the sialyl lactosamine oligosaccharides, indicating that a single protein catalyzes sulfation of chondroitin, keratan sulfate, and sialyl lactosamine oligosaccharides. These results raised a possibility that C6ST may be one of the candidates involved in the biosynthesis of sulfated sialyl Lewis x ligand for L-selectin.
影响因子：
2.9
作者：
GUO, Y;CONRAD, HE
通讯作者：
CONRAD, HE