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Analysis of novel over- and under-sulfated glycosaminoglycan sequences by enzyme cleavage and multiple stage MS

Domenii publicaţii > Chimie + Tipuri publicaţii > Articol în revistã ştiinţificã

Autori: A.D. Zamfir, C.Flangea, E.Sisu, A.F.Serb, N.Dinca,P.Bruckner,D.G. Seidler

Editorial: WILEY-VCH, Proteomics, 9(13), p.3435-3444, 2009.

Rezumat:

We report on a novel strategy for identification of specific sulfation motifs in chondroitin/
dermatan sulfate (CS/DS) chain derived from decorin (Dcn), based on enzyme cleavage and
multistage MS (MSn). Released CS/DS chains were digested with chondroitin B and in
parallel with AC I lyases to obtain oligosaccharides of known hexuronic acid (HexA)
epimerization. The depolymerized chains were separated by gel filtration, and collected
di- and hexasaccharides were analyzed by ESI MSn. MS2 on bisulfated 4,5-D-HexAGalNAc
revealed an additional sulfate ester group at 4,5-D-HexA. MS2 data provided evidence upon
GlcA sulfation in Dcn due to the fact that 4,5-D-HexA derived from GlcA after chondroitin
AC I lyase treatment. Hexasaccharide screening in the MS1 mode indicated direct correlation
between the sulfate distribution and HexA epimerization. MSn performed on ions that,
according to mass calculation, correspond to pentasulfated [4,5-D-HexAGalNAc(GlcAGalNAc)
2], trisulfated [4,5-D-HexAGalNAc(GlcAGalNAc)2] with IdoA-derived 4,5-D-HexA at
the nonreducing end, tetrasulfated [4,5-D-HexAGalNAc(IdoAGalNAc)2] and monosulfated
[4,5-D-HexAGalNAc(IdoAGalNAc)2] with GlcA-derived 4,5-D-HexA at the nonreducing end
rendered fragmentation patterns confirming the presence of over-, regular, and undersulfated
regions as well as structural motifs having both types of HexA sulfated within Dcn
CS/DS.

Cuvinte cheie: Decorina.Glicozaminoglicani.Fibroblaste din piele.Spectrometrie de masa cu fragmentare multipla // Decorin / Glycosaminoglycans / Multistage mass spectrometry / Skin fibroblasts / Sulfation