2006
DOI: 10.1074/jbc.m600140200
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N-Linked Oligosaccharides on Chondroitin 6-Sulfotransferase-1 Are Required for Production of the Active Enzyme, Golgi Localization, and Sulfotransferase Activity toward Keratan Sulfate

Abstract: We have shown previously that purified chondroitin 6-sulfotransferase-1 (C6ST-1) was a glycoprotein abundant in N-linked oligosaccharides and could sulfate both chondroitin (C6ST activity) and keratan sulfate (KSST activity); however, functional roles of the N-glycans have remained unclear. In the present study, we show essential roles of N-glycans attached to C6ST-1 in the generation of the active enzyme and in its KSST activity. Treatment with tunicamycin of COS-7 cells transfected with C6ST-1 cDNA totally a… Show more

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Cited by 23 publications
(19 citation statements)
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“…However, the CS6OST showed significant differences between the two culture conditions and the length of time in culture, with a fourfold increase in expression under MM culture conditions. The CS6OST enzyme transfers the sulfate to the C-6 position of the Nacetylgalactosamine, with mutations in this gene resulting in chondrodysplasia with major involvement of the spine (Yusa et al, 2006; Fig. 5C).…”
Section: Gene Expression Of Sulfotransferases Associated With Osteogementioning
confidence: 96%
“…However, the CS6OST showed significant differences between the two culture conditions and the length of time in culture, with a fourfold increase in expression under MM culture conditions. The CS6OST enzyme transfers the sulfate to the C-6 position of the Nacetylgalactosamine, with mutations in this gene resulting in chondrodysplasia with major involvement of the spine (Yusa et al, 2006; Fig. 5C).…”
Section: Gene Expression Of Sulfotransferases Associated With Osteogementioning
confidence: 96%
“…It is imperative to remove the viral chondroitinase contamination from the enzyme preparations [17] as the chondroitinase degrades chondroitin oligosaccharide backbones,the substrates used by both CS4OST and CS6OST.T he expression of CS6OST in E. coli was unsuccessful possibly owing to the fact that glycosylation is required for the sulfotransferase activity. [18] Thep roducts were analyzed in terms of their purity and structure by high-resolution anion-exchange HPLC,e lectrospray ionization mass spectrometry (ESI-MS), and NMR spectroscopy.T he majority of products gave rise to as ingle symmetric peak in the HPLC trace,c onfirming their purity (Table S1 and Figures S1-S60). One exception is compound 4, which displayed ap urity of only 59 %b ecause the trifluoroacetyl group on residue Di sl abile,a nd am ixture of compound 4 and detrifluoroacetylated compound 6 was obtained, as demonstrated by ESI-MS analysis ( Figure S13).…”
Section: Zuschriftenmentioning
confidence: 99%
“…The chondroitinase degrades chondroitin oligosaccharide backbones, the substrates used by both CS4OST and CS6OST. The expression of CS6OST in E. coli was unsuccessful possibly due to the fact that glycosylation is required for the sulfotransferase activity [18] .…”
mentioning
confidence: 99%
“…Several enzymes involved in the biosynthesis of dermatan sulfate have been shown to be dependent on N-glycosylation for proper function (27,28). We therefore investigated the importance of N-glycosylation for enzymatic activity of DS-epimerase 1.…”
Section: N-glycosylation Is Required For Ds-epimerase 1 Activity-mentioning
confidence: 99%