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Comment
. 2020 Jul 3;31(5):621-623.
doi: 10.1080/09537104.2020.1764922. Epub 2020 Jun 4.

New insights into glycoprotein Ibα desialylation-mediated platelet clearance

Jack Yule  1   2 , Neil V Morgan  2 , Natalie S Poulter  1   2
Affiliations
Comment

New insights into glycoprotein Ibα desialylation-mediated platelet clearance

Jack Yule et al. Platelets. .
No abstract available

Keywords: Glycoprotein Ibα; O-glycans; platelet clearance; sialylation.

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Figures

Figure 1.
Figure 1.
Sialic acid molecules (green) are present at the end of glycans that decorate GPIbα, a highly abundant platelet surface glycoprotein. Exogenous neuraminidase (e.g. α2,3 or α2,3,6,8-neuraminidase (open orange circles)) from invading bacteria removes sialic acid from O-glycans of the GPIbα mechanosensory domain (MSD, red), leading to its unfolding. This propagates signaling through GPIb-IX, leading to Src family kinase signaling and potentially subsequent immunoreceptor tyrosine-based activation motif (ITAM) signaling, which is similar to what occurs when VWF-A1 binds to GPIba[17]. MSD unfolding also induces expression and surface presentation of endogenous Neuraminidase 1 (Neu1; filled orange circles) found in platelet granules. This increases the desialylation of N-glycans on other platelet glycoproteins, which then preferentially bind the hepatic Ashwell-Morell receptor (AMR), allowing the platelet to be taken up and cleared.
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