Functional glycosylation of human podoplanin: Glycan structure of platelet aggregation-inducing factor

Mika Kato Kaneko, Yukinari Kato, Akihiko Kameyama, Hiromi Ito, Atsushi Kuno, Jun Hirabayashi, Tomomi Kubota, Koh Amano, Yasunori Chiba, Yasushi Hasegawa, Isoji Sasagawa, Kazuhiko Mishima, Hisashi Narimatsu

研究成果: Article査読

79 被引用数 (Scopus)

抄録

Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation. Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity. Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray. Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAcα2-3Galβl-3(NeuAcα2-6)GalNAcαl-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52. Sialic acid-deficient podoplanin recovered its activity after additional sialylation. These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.

本文言語English
ページ(範囲)331-336
ページ数6
ジャーナルFEBS Letters
581
2
DOI
出版ステータスPublished - 2007 1 23

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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