2. Academic Validation
  3. Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor

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

  • FEBS Lett. 2007 Jan 23;581(2):331-6. doi: 10.1016/j.febslet.2006.12.044.
Mika Kato Kaneko 1,  Yukinari Kato,  Akihiko Kameyama,  Hiromi Ito,  Atsushi Kuno,  Jun Hirabayashi,  Tomomi Kubota,  Koh Amano,  Yasunori Chiba,  Yasushi Hasegawa,  Isoji Sasagawa,  Kazuhiko Mishima,  Hisashi Narimatsu
Affiliations

Affiliation

  • 1 Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan.
PMID: 17222411 DOI: 10.1016/j.febslet.2006.12.044
Abstract

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 (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-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.

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