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

Research output: Contribution to journalArticlepeer-review

92 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)331-336
Number of pages6
JournalFEBS Letters
Issue number2
Publication statusPublished - 2007 Jan 23


  • Disialyl-T
  • Disialyl-corel
  • Platelet aggregation
  • Podoplanin

ASJC Scopus subject areas

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


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