Key result
Selective engagement of platelet GPIbalpha by VWF-A1/R543W cells caused rapid, spontaneous platelet aggregation and tyrosine phosphorylation of Syk comparable to GPVI activation by collagen.
Population
Washed platelets and COS-7 cells expressing the VWF-A1 domain containing an R543W mutation
Comparison
Selective engagement of platelet GPIbα by… vs Engagement of GPVI by collagen or…
Design
Preclinical
Authors
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GPIb-IX-V functions as both adhesion and signaling receptor; extends mechanistic models in animals but leaves open human translation.
Specific ligation of GPIbα leads to robust platelet activation, defining GPIb-IX-V as both an adhesion and signaling receptor.
Gardiner et al. (2010) studied this question. Selective engagement of platelet GPIbalpha by VWF-A1/R543W cells vs. Engagement of GPVI by collagen or collagen-related peptide (CRP) was evaluated on Platelet aggregation and signaling (tyrosine phosphorylation of Syk). Selective engagement of platelet GPIbalpha by VWF-A1/R543W cells caused rapid, spontaneous platelet aggregation and tyrosine phosphorylation of Syk comparable to GPVI activation by collagen.
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