Mouse platelets lacking the extracellular domain of GPIbalpha and human platelets treated with GPIbalpha-blocking antibodies display a reduced aggregation response to synthetic glycopolymers. We found that synthetic sulfated glycopolymers bind directly to GPIbalpha substantiating that GPIbalpha facilitates the interaction of synthetic glycopolymers with CLEC-2 or PEAR1.
Platelet protein disulfide isomerase-facilitated cleavage of the allosteric disulfide bonds tightly regulates GPIbalpha function promoting platelet-neutrophil interactions vascular occlusion and tissue damage under thromboinflammatory conditions.
A 2- to 3-fold decrease occurred in circulating TPO in GPIbalpha(-/-) mice compared with wild-type. Lower TPO levels in GPIbalpha-/- mice are due to impaired platelet-stimulated hepatic TPO production. The N terminus of GPIbalpha is required for platelet-mediated hepatic TPO generation.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.