A comparison of the main structures of N-glycans of porcine islets with those from humans

Shuji Miyagawa, Akira Maeda, Takuji Kawamura, Takehisa Ueno, Noriaki Usui, Sachiko Kondo, Shinichi Matsumoto, Teru Okitsu, Masafumi Goto, Hiroshi Nagashima

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


After producing α1-3-galactosyltransferase knockout (GKO) pigs, most of the organs of these pigs showed less antigenicity to the human body. However, wild-type adult pig islets (API) that originally contained negligible levels of α-galactosidase now showed a clear antigenicity to human serum. In this study, N-glycans were isolated from both APIs and human islets. Their structures were then analyzed by a mapping technique based on their high-performance liquid chromatography elution positions and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometric data. Both preparations contained substantial amounts of high-mannose structures. The N-glycans from human islets were separated into 17 neutral, 8 mono-sialyl and 4 di-sialyl glycans, and the API glycans were comprised of 11 neutral, 8 mono-sialyl, 3 di-sialyl, 2 mono-sulfated, 3 mono-sialyl-mono-sulfated and 1 di-sulfated glycans. Among them, the API preparation contained one neutral, five mono-sialyl glycans and six sulfated glycans that were not detected in human islets. The structures of 9 of these 12 could be clearly determined. In addition, a study of the sulfate-depleted API suggests that sulfate residues could be antigenic to humans. The data herein will be helpful for future studies of the antigenicity associated with API.

Original languageEnglish
Pages (from-to)125-138
Number of pages14
Issue number2
Publication statusPublished - 2014 Feb


  • N-glycan
  • pig islets
  • sulfated glycan
  • xenotransplantation


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