Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase.

Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase. Research Abstract Details 

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Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase. Abstract Text:

We have previously cloned keratan sulfate Gal-6-sulfotransferase (KSGal6ST), which transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate to position 6 of Gal residue of keratan sulfate. In this study, we examined whether KSGal6ST could transfer sulfate to sialyl N -acetyllactosamine oligosaccharides or fetuin oligo-saccharides. KSGal6ST expressed in COS-7 cells catalyzed transfer of sulfate to NeuAcalpha2-3Galbeta1-4GlcNAc (3'SLN), NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-3Galbeta1-4Gl cNAc (SL1L1), NeuAcalpha2-3Galbeta1-4(6-sulfo)GlcNAcbeta1-3(6-sulfo) Galbeta1-4(6-su lfo)GlcNAc (SL2L4), and their desialylated derivatives except for Galbeta1-4GlcNAc, but not to NeuAcalpha2-3Galbeta1-4(Fucalpha1-3)GlcNAc (SLex). When the sulfated product formed from 3'SLN was degraded with neuraminidase and reduced with NaBH(4), the resulting sulfated disaccharide alditol showed the same retention time in SAX-HPLC as that of [(3)H]Gal(6SO(4))beta1-4GlcNAc-ol. KSGal6ST also catalyzed sulfation of fetuin. When the sulfated oligosaccharides released from the sulfated fetuin after sequential digestion with proteinase and neuraminidase were subjected to a reaction sequence of hydrazin-olysis, deaminative cleavage and NaBH(4)reduction, the major product was co-eluted with [(3)H]Gal(6SO(4))beta1-4anhydromannitol in SAX-HPLC. These observations show that KSGal6ST is able to sulfate position 6 of Gal residue of 3'SLN and fetuin oligosaccharides. The relative rates of the sulfation of SL2L4 was much higher than the rate of the sulfation of keratan sulfate. These results suggest that KSGal6ST may function in the sulfation of sialyl N -acetyllactosamine oligosaccharide chains attached to glycoproteins.

Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase. Publishing Authors By Initials

For similar proteins: fetal proteins: alpha-fetoproteins research abstracts see: proteins: fetal proteins: alpha-fetoproteins research

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Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Glycobiology

VOLUME: 10

Page Numbers: 203-11

Journal Abbreviation: Glycobiology

ISSN: 0959-6658

DAY: 30

MONTH: Feb

YEAR: 2000

Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase. Information

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LANGUAGE: eng

NlmUniqueID: 9104124

Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase. Keywords Mesh Terms:

KEYWORDS: alpha-Fetoproteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase. Information

Substance Name: carbohydrate sulfotransferases

Registry Number: EC 2.8.2.-

Grant and Affiliation Information for Sulfation of sialyl N-acetyllactosamine oligosaccharides and fetuin oligosaccharides by keratan sulfate Gal-6-sulfotransferase.

AFFILIATION: Department of Life Science, Aichi University of Education, Igaya-cho, Kariya, Aichi 448-8542, Japan.

Country: ENGLAND

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MEDLINETA: Glycobiology

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