Interactions of Platelets with Subendothelium and Endothelium
- 5 April 2005
- journal article
- review article
- Published by Wiley in Microcirculation
- Vol. 12 (3), 235-246
- https://doi.org/10.1080/10739680590925484
Abstract
In this review, the authors summarize how platelets interact with subendothelium when the vessel wall is damaged or with intact endothelium in the inflammatory state. When subendothelium is exposed to rapidly flowing blood upon vessel damage, platelets adhere rapidly to the exposed surface, decelerate, and aggregate to arrest bleeding. Under high shear stress, such as is found in the microcirculation, the interaction between subendothelial von Willebrand factor (VWF) and its platelet receptor, glycoprotein (GP) Ib‐IX‐V, is required to slow down platelets and allow the platelet collagen receptors α2β1 and GP VI to bind to collagen. GP VI and α2β1 play important roles to activate platelets in the early stage and work with GP Ib‐IX‐V to fully activate platelets to form thrombi. GP Ib‐IX‐V and GP VI employ similar signaling pathways for platelet activation and the signals from both receptors are down‐modulated by PECAM‐1 (platelet–endothelial–cell adhesion molecule 1) to prevent unnecessary platelet activation under high shear. During inflammatory states, intact endothelial cells release VWF and P‐selectin from their Weibel‐Palade bodies. Both molecules are ligands for GP Ib‐IX‐V. The newly released VWF is larger and stickier than the form normally found in plasma and binds platelets spontaneously. Normally, VWF is processed by proteolysis by the plasma metalloprotease ADAMTS‐13. Failure of this processing results in the microvascular thrombotic disorder thrombotic thrombocytopenic purpura. In this review, the authors also use available crystal structures of platelet receptors and ligands to explain the details of their interactions.Keywords
This publication has 77 references indexed in Scilit:
- ADAMTS13 gene mutation in congenital thrombotic thrombocytopenic purpura with previously reported normal VWF cleaving protease activityBlood, 2003
- Localization of the Adhesion Receptor Glycoprotein Ib-IX-V Complex to Lipid Rafts Is Required for Platelet Adhesion and ActivationThe Journal of Experimental Medicine, 2002
- Crystal Structure of the Platelet Glycoprotein Ibα N-terminal Domain Reveals an Unmasking Mechanism for Receptor ActivationJournal of Biological Chemistry, 2002
- Differential role of glycolipid-enriched membrane domains in glycoprotein VI- and integrin-mediated phospholipase Cγ2 regulation in plateletsBiochemical Journal, 2002
- Lipid Rafts Orchestrate Signaling by the Platelet Receptor Glycoprotein VIPublished by Elsevier BV ,2002
- Interaction of von Willebrand Factor Domain A1 with Platelet Glycoprotein Ibα-(1–289)Journal of Biological Chemistry, 2000
- Signal-transducing Mechanisms Involved in Activation of the Platelet Collagen Receptor Integrin α2β1Published by Elsevier BV ,2000
- Interaction between GPIbα and FcγIIA Receptor in Human PlateletsBiochemical and Biophysical Research Communications, 1999
- The Platelet Reactivity of Synthetic Peptides Based on the Collagen III Fragment α1(III)CB4Published by Elsevier BV ,1997
- Unusually Large Plasma Factor VIII: von Willebrand Factor Multimers in Chronic Relapsing Thrombotic Thrombocytopenic PurpuraNew England Journal of Medicine, 1982