ReviewPlatelet-neutrophil-interactions: Linking hemostasis and inflammation
Section snippets
Platelets
Platelets are unnucleated fragments of bone marrow megakaryocytes. They contain few viable mitochondria, glycogen, at least three types of morphologically different granules (α-granules, dense core granules, lysosomes), and a complex membranous system. α-granules contain adhesion molecules important for platelet-platelet interactions and platelet interactions with other blood cells, mitogenic factors, plasma proteins, and factors relevant for coagulation and fibrinolysis (Table 1). Dense
Integrins
Integrins are a large family of receptors which are constitutively expressed on the surface of almost all cells. They consist of transmembrane αß heterodimers and can bind extracellular matrix proteins as well as immunoglobulin-like adhesion molecules. Many cell-cell and cell-extracellular matrix interaction are regulated by integrins, which modulate important events in different biological processes, e.g. hemostasis, thrombosis, immunology, inflammation, cell adhesion, growth, differentiation
Chemokine receptors
Chemokine receptors are members of the G-protein-coupled receptor family.52, 53, 54, 55 Platelets express the chemokine receptors CCR1, CCR3, CCR4, CXCR1, and CXCR4 (Table 3) that bind proinflammatory and homeostatic chemokines. One important ligand for CCR4, which is present and functional on platelets,56, 57 is CCL17 (Thymus and Activation Regulated Chemokine, TARC). This chemokine alone is not a potent platelet agonist, but it can enhance platelet stimulation in the presence of other
Shape change
Upon activation by thrombin, ADP or TXA2, platelets undergo shape change, and secrete contents of α- and dense granules.79 Rearrangement of cytoskeletal proteins, including the disassembly of a microtubule ring, occurs as one of the very first steps and results in a shape change from a disc-shaped cell into an intermediate spherical shape cell. This is followed by actin polymerization and extension of filopodia.80, 81 Agonist-dependent phosphorylation of platelet myosin induces its
Acknowledgement
A.Z. is supported by a grant of the Deutsche Forschungsgemeinschaft (DFG AZ 428/2–1). The original work from K.L.’s lab is supported by grants from the National Institutes of Health HL58108, 55798 and 73361.
References (140)
- et al.
Platelet-endothelial interactions in inflamed mesenteric venules
Blood.
(1998) Integrins: bidirectional, allosteric signaling machines
Cell.
(2002)- et al.
New insights into the structural basis of integrin activation
Blood.
(2003) - et al.
Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain
J Biol Chem.
(2000) - et al.
Aggregation of mammalian cells expressing the platelet glycoprotein (GP) Ib-IX complex and the requirement for tyrosine sulfation of GP Ib alpha
Blood.
(1995) - et al.
Identification of three tyrosine residues of glycoprotein Ib alpha with distinct roles in von Willebrand factor and alpha-thrombin binding
J Biol Chem.
(1995) - et al.
The von Willebrand factor-glycoprotein Ib/V/IX interaction induces actin polymerization and cytoskeletal reorganization in rolling platelets and glycoprotein Ib/V/IX-transfected cells
J Biol Chem.
(1999) - et al.
Synergistic adhesive interactions and signaling mechanisms operating between platelet glycoprotein Ib/IX and integrin alpha IIbbeta 3. Studies in human platelets ans transfected Chinese hamster ovary cells
J Biol Chem.
(2000) - et al.
Signaling across the platelet adhesion receptor glycoprotein Ib-IX induces alpha IIbbeta 3 activation both in platelets and a transfected Chinese hamster ovary cell system
J Biol Chem.
(2000) - et al.
Platelets and shear stress
Blood.
(1996)
Platelet physiology and thrombosis
Thromb Res.
Platelet-collagen interaction: is GPVI the central receptor?
Blood.
GPVI and alpha2beta1 play independent critical roles during platelet adhesion and aggregate formation to collagen under flow
Blood.
Von Willebrand factor, platelets and endothelial cell interactions
J Thromb Haemost.
Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura
J Biol Chem.
ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions
Blood.
The role of selectins in inflammation and disease
Trends Mol Med.
Selectins and their ligands: current concepts and controversies
Blood.
The biology of P-selectin glycoprotein ligand-1: its role as a selectin counterreceptor in leukocyte-endothelial and leukocyte-platelet interaction
Thromb Haemost.
Platelet/polymorphonuclear leukocyte interaction: P-selectin triggers protein-tyrosine phosphorylation-dependent CD11b/CD18 adhesion: role of PSGL-1 as a signaling molecule
Blood.
Neutrophil rolling, arrest, and transmigration across activated, surface-adherent platelets via sequential action of P-selectin and the beta 2-integrin CD11b/CD18
Blood.
Platelet/polymorphonuclear leukocyte interaction in dynamic conditions: evidence of adhesion cascade and cross talk between P-selectin and the beta 2 integrin CD11b/CD18
Blood.
Platelet P-selectin is required for pulmonary eosinophil and lymphocyte recruitment in a murine model of allergic inflammation
Blood.
Molecular properties of the chemokine receptor family
Trends Pharmacol Sci.
Chemokine receptor dimerization: two are better than one
Trends Immunol.
Adenosine diphosphate strongly potentiates the ability of the chemokines MDC, TARC, and SDF-1 to stimulate platelet function
Blood.
Functional expression of CCR1, CCR3, CCR4, and CXCR4 chemokine receptors on human platelets
Blood.
Phosphorylation of the thromboxane receptor alpha, the predominant isoform expressed in human platelets
J Biol Chem.
Protein kinase C activation is not a key step in ADP-mediated exposure of fibrinogen receptors on human platelets
FEBS Lett.
Concomitant activation of Gi protein-coupled receptor and protein kinase C or phospholipase C is required for platelet aggregation
FEBS Lett.
Molecular mechanism of thromboxane A(2)-induced platelet aggregation. Essential role for p2t(ac) and alpha(2a) receptors
J Biol Chem.
Ligand specificity and ticlopidine effects distinguish three human platelet ADP receptors
Eur J Pharmacol.
ADP is the cognate ligand for the orphan G protein-coupled receptor SP1999
J Biol Chem.
The platelet P2 receptors as molecular targets for old and new antiplatelet drugs
Pharmacol Ther.
Tyrosine phosphorylation of cortactin associated with Syk accompanies thromboxane analogue-induced platelet shape change
J Biol Chem.
Dissociation of the alphaIIbbeta3-integrin by EGTA stimulates the tyrosine kinase pp72(syk) without inducing platelet activation
J Biol Chem.
Neutrophil activating factor (NAF) induces polymorphonuclear leukocyte adherence to endothelial cells and to subendothelial matrix proteins
Biochem Biophys Res Commun.
Platelet factor 4-induced neutrophil-endothelial cell interaction: involvement of mechanisms and functional consequences different from those elicited by interleukin-8
Blood.
The CXC-chemokine neutrophil-activating peptide-2 induces two distinct optima of neutrophil chemotaxis by differential interaction with interleukin-8 receptors CXCR-1 and CXCR-2
Blood.
The platelet release reaction: granules’ constituents, secretion and functions
Platelets.
Platelets roll on stimulated endothelium in vivo: an interaction mediated by endothelial P-selectin
Proc Natl Acad Sci U S A.
Platelet-mediated lymphocyte delivery to high endothelial venules
Science.
Integrins: emerging paradigms of signal transduction
Annu Rev Cell Dev Biol.
Structure and function of the platelet integrin alphaIIbbeta3
J Clin Invest.
Talin binding to integrin beta tails: a final common step in integrin activation
Science.
Chemokine induction of integrin adhesiveness on rolling and arrested leukocytes local signaling events or global stepwise activation?
Microcirculation.
Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibalpha. Identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibalpha as a binding site for von Willebrand factor and alpha-thrombin
Biochemistry.
Analysis of the roles of 14-3-3 in the platelet glycoprotein Ib-IX-mediated activation of integrin alpha(IIb)beta(3) using a reconstituted mammalian cell expression model
J Cell Biol.
Mechanisms initiating platelet thrombus formation
Thromb Haemost.
Adhesion-dependent signalling and the initiation of haemostasis and thrombosis
Histol Histopathol.
Cited by (528)
Preparation of healing-promoting and fibrosis-inhibiting asymmetric poly(ethylene glycol-b-L-phenylalanine)/cRGD-modified hyaluronate sponges and their applications in hemorrhage and nasal mucosa repair
2024, International Journal of Biological MacromoleculesImmune evasion on the nanoscale: Small extracellular vesicles in pancreatic ductal adenocarcinoma immunity
2023, Seminars in Cancer BiologyCrosstalk between the plasminogen/plasmin system and inflammation resolution
2023, Journal of Thrombosis and Haemostasis