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

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

doi:10.1016/j.febslet.2006.12.044

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Volume 581, Issue 2 , Pages 331-336, 23 January 2007

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

Edited by Judit Ovádi

Mika Kato Kaneko
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
- These authors contributed equally to this work.
Yukinari Kato
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
- These authors contributed equally to this work.
Akihiko Kameyama
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
Hiromi Ito
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
Atsushi Kuno
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
Jun Hirabayashi
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
Tomomi Kubota
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
Koh Amano
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
Yasunori Chiba
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
Yasushi Hasegawa
- Department of Surgery, School of Medicine, Keio University, Tokyo, Japan
Isoji Sasagawa
- Yamagata Tokushukai Hospital, Yamagata, Japan
Kazuhiko Mishima
- Department of Neurosurgery, Saitama Medical School, Saitama, Japan
Hisashi Narimatsu
- Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), C-2, 1-1-1 Umezono, Tsukuba, Ibaraki 305 8568, Japan
- Corresponding author. Fax: +81 29 861 3191.

Received 4 December 2006; received in revised form 20 December 2006; accepted 21 December 2006. published online 05 January 2007.

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 (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.

Abbreviations: PLAG, platelet-aggregation-stimulating, CHO, Chinese hamster ovary, MALDI-TOF-MS, matrix-assisted laser desorption/ionization time of-flight mass spectrometry, QIT, quadrupole ion trap, HPLC, high performance liquid chromatography