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