Deciphering the Roles of N‑Glycans on Collagen–Platelet Interactions

Collagen
is a potent agonist for platelet activation, presenting
itself as a key contributor to coagulation via interactions with platelet
glycoproteins. The fine details dictating platelet–collagen
interactions are poorly understood. In particular, glycosylation could
be a key determinant in the platelet–collagen interaction.
Here, we report an affinity purification coupled to a mass spectrometry-based
approach to elucidate the function of N-glycans in dictating platelet–collagen
interactions. By integrative proteomic and glycoproteomic analysis
of collagen–platelet interactive proteins with N-glycan manipulation,
we demonstrate that the interaction of platelet adhesive receptors
with collagen is highly N-glycan regulated, with glycans on many receptors
playing positive roles in collagen binding, with glycans on other
platelet glycoproteins exhibiting inhibitory roles on the binding
to collagen. Our results significantly enhance our understanding of
the details of glycans influencing the platelet–collagen interaction.