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N-acetylgalactosami...
N-acetylgalactosamine (GalNAc) transfer to the common carbohydrate-protein linkage region of sulfated glycosaminoglycans : identification of UDP-GaINAc:chondro oligosaccharide aNacetylgalactosaminyltransferase in fetal bovine serum
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Kitagawa, H (författare)
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Tanaka, Y (författare)
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Tsuchida, K (författare)
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Goto, F (författare)
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Ogawa, T (författare)
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- Lidholt, Kerstin (författare)
- Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi
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- Lindahl, Ulf (författare)
- Uppsala universitet,Institutionen för medicinsk och fysiologisk kemi
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Sugahara, K (författare)
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(creator_code:org_t)
- 1995
- 1995
- Engelska.
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Ingår i: The Journal of Biological Chemsitry. - 0021-9258. ; 270:38, s. 22190-22195
- Relaterad länk:
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https://urn.kb.se/re...
Abstract
Ämnesord
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- During the course of a study to elucidate the role ofmodification of the common polysaccharide-protein linkagestructure, GlcAb1–3Galb1–3Galb1–4Xylb1-O-Ser, inbiosynthetic sorting mechanisms of the different sulfatedglycosaminoglycan chains, a novel N-acetylgalactosamine(GalNAc) transferase was discovered in fetalbovine serum. The enzyme catalyzed the transfer of[3H]GalNAc from UDP-[3H]GalNAc to linkage tetrasaccharideand hexasaccharide serines synthesized chemicallyand to various regular oligosaccharides containingterminal D-glucuronic acid (GlcA), which were preparedfrom chondroitin and chondroitin sulfate using testicularhyaluronidase digestion. The labeled products obtainedwith the linkage tetra- and hexasaccharideserines and with the tetrasaccharide (GlcAb1–3GalNAc)2were resistant to digestion with chondroitinase AC-IIand b-N-acetylhexosaminidase but sensitive to a-Nacetylgalactosaminidasedigestion, indicating that theenzyme is an a-N-acetylgalactosaminyltransferase. Thisfinding is in contrast to that of Rohrmann et al. (Rohrmann,K., Niemann, R., and Buddecke, E. (1985) Eur. J.Biochem., 148, 463–469), who reported that a correspondingproduct was susceptible to digestion with b-Nacetylhexosaminidase.The presence of a sulfate groupat C4 of the penultimate GalNAc or Gal units markedlyinhibited the transfer of GalNAc to the terminal GlcA,while a sulfate group at C6 of the GalNAc had little effecton the transfer. Moreover, a slight but significant transferof [3H]GalNAc was observed to an oligosaccharidecontaining terminal 2-O-sulfated GlcA as acceptor,whereas no incorporation was detected into oligosaccharidescontaining terminal unsaturated or 3-O-sulfatedGlcA units. These results suggest that this novelserum enzyme is a UDP-GalNAc:chondro-oligosaccharidea1–3- or 1–4-N-acetylgalactosaminyltransferase.
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- NATURAL SCIENCES
- NATURVETENSKAP
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