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Functional glycosylation of human podoplanin: Glycan structure of platelet aggregation‐inducing factor
Author(s) -
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
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.12.044
Subject(s) - podoplanin , glycosylation , sialoglycoprotein , chemistry , glycan , biochemistry , sialic acid , edman degradation , platelet , mucin , glycoprotein , peptide sequence , biology , immunology , immunohistochemistry , gene
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.