Báo cáo khoa học: Distinct but critical roles for integrin aIIbb3 in platelet lamellipodia formation on fibrinogen, collagen-related peptide and thrombin

Distinct But Critical Roles For Integrin αIIbβ3 In Platelet Lamellipodia Formation On Fibrinogen, Collagen-Related Peptide And Thrombin

Authors: Kelly Thornber, Owen J. T. McCarty, Steve P. Watson, and Catherine J. Pears

Field: Biochemistry

Document Summary: This study investigates the role of the platelet integrin αIIbβ3 in lamellipodia formation on various surfaces. While αIIbβ3 is crucial for lamellipodia formation on fibrinogen, collagen-related peptide (CRP), and thrombin, the requirement for integrin signaling varies. The research reveals that αIIbβ3 acts as an adhesive receptor, and its engagement, often through the release of ligands from platelet granules, is essential for lamellipodia formation. Notably, thrombin can facilitate lamellipodia formation independently of αIIbβ3 outside-in signaling, highlighting the complex interplay of receptors and signaling pathways in platelet responses.

Detailed Table of Contents:

• Abstract
• Introduction
• Results
• Morphological changes of human platelets on fibrinogen, CRP and thrombin
• Different Ca²⁺ mobilization patterns in platelets exposed to fibrinogen, CRP and thrombin
• αIIbβ3 is required for platelet lamellipodia formation on fibrinogen, CRP and thrombin
• Thrombin can bypass αIIbβ3 outside-in signaling in mediating lamellipodia formation
• The roles of αIIbβ3 and α2β1 in platelet lamellipodia formation on collagen
• Discussion
• Experimental procedures
• Reagents
• Preparation of washed platelets
• Adhesion assays
• Single-platelet Ca²⁺ measurement
• Analysis of data
• Acknowledgements
• References
• Supplementary material