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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
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Supplemental Analysis for N-linked Sugars in Adult Pig Islets.

H Eguchi1, T Kawamura1, N Kashiyama1

  • 1Department of Surgery, Osaka University Graduate School of Medicine, Suita, Osaka, Japan.

Transplantation Proceedings
|June 21, 2016
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Summary
This summary is machine-generated.

Researchers identified novel N-glycan structures in adult pig islets (APIs), including sulfated glycans. This advances understanding of non-Gal epitopes and pig islet antigenicity for xenotransplantation.

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Area of Science:

  • Immunology
  • Glycobiology
  • Transplantation Science

Background:

  • Pig islets are promising for xenotransplantation, but antigenicity remains a challenge.
  • While α-Gal knockout pigs show reduced antigenicity, non-Gal epitopes on wild-type adult pig islets (APIs) still pose risks.
  • Previous studies identified 28 N-glycan structures in APIs, but knowledge of non-Gal glycoantigens is incomplete.

Purpose of the Study:

  • To identify additional N-glycan structures in APIs beyond previously reported findings.
  • To further characterize the non-Gal glycoantigens present on APIs.
  • To contribute to understanding API antigenicity for xenotransplantation.

Main Methods:

  • N-glycans were isolated from APIs using a modified O'Neil et al. method.
  • Liquid chromatography-mass spectrometry (LC-MS) was employed for structural analysis.
  • Glycan structures were predicted using FLexAnalysis software and the GlyocoMod Tool.

Main Results:

  • Analysis identified 11 N-glycan peaks and 16 N-linked sugar structures.
  • Five sulfated glycans were detected, confirming the presence of sulfate structures in API N-glycans.
  • The findings supplement previous reports, particularly regarding N-glycans with deoxyhexose units like fucose.

Conclusions:

  • This study elucidates additional N-glycan structures in APIs, including novel sulfated glycans.
  • The identified structures contribute to a more complete understanding of non-Gal glycoantigens.
  • These findings are crucial for future research on API antigenicity and xenotransplantation strategies.