WFRF:(Lindahl Maria)
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Assessment of glycosaminoglycan-protein linkage tetrasaccharides as acceptors for GalNAc- and GlcNAc-transferases from mouse mastocytoma.
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- Lidholt, Kerstin (author)
- Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi
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- Fjelstad, Maria (author)
- Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi
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- Lindahl, Ulf (author)
- Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi
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- Goto, F (author)
- Ogawa, T (author)
- Kitagawa, H (author)
- Sugahara, K (author)
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- (creator_code:org_t)
- 1997
- 1997
- English.
- In: Glycoconjugate Journal. - 0282-0080 .- 1573-4986. ; 14:6, s. 737-742
- Journal article (peer-reviewed)
Abstract
Subject headings
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- Two glycosaminoglycan-protein linkage tetrasaccharide-serine compounds, GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser and GlcA beta 1-3Gal(4-O-sulfate)beta 1-3Gal beta 1-4Xyl beta 1-O-Ser, were tested as hexosamine accepters, using UDP-[H-3]GlcNAc and UDP-[H-3]GalNAc as sugar donors, and solubilized mouse mastocytoma microsomes as enzyme source. The nonsulfated Ser-tetrasaccharide was found to function as an acceptor for a GalNAc residue, whereas the Ser-tetrasaccharide containing a sulfated galactose unit was inactive. Characterization of the radio-labelled product by digestion with alpha-N-acetylgalactosaminidase and beta-N-acetylhexosaminidase revealed that the [H-3]GalNAc unit was alpha-linked, as in the product previously synthesized using serum enzymes, and not beta-linked as found in the chondroitin sulfate polymer. Heparan sulfate/heparin biosynthesis could not be primed by either of the two linkage Ser-tetrasaccharides, since no transfer of [H-3]GlcNAc from UDP-[H-3]GlcNAc could be detected. By contrast, transfer of a [H-3]GlcNAc unit to a [GlcA beta 1-4GlcNAca1-4](2)-GlcA beta 1-4-aMan hexasaccharide acceptor used to assay the GlcNAc transferase involved in chain elongation, was readily detected. These results are in agreement with the recent proposal that two different N-acetylglucosaminyl transferases catalyse the biosynthesis of heparan sulfate. Although the mastocytoma system contains both the heparan sulfate/heparin and chondroitin sulfate biosynthetic enzymes the Ser-tetrasaccharides do not seem to fulfil the requirements to serve as accepters for the first HexNAc transfer reactions involved in the formation of these polysaccharides.
Keyword
- Biosynthesis
- GalNAc transferase
- GlcNAc transferase
- glycosaminoglycan
- proteoglycan
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- ref (subject category)
- art (subject category)
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