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PMID: 10494030 Published · ppublish English Journal Article Review

Platelet signal transduction pathways: could we organize them into a 'hierarchy'?

Haemostasis ·Vol. 29 ·No. 1 ·1999-09-00 ·Pages 4-15

Lévy-Toledano S

Abstract

Platelet activation results in shape change, release of granule contents, aggregation and clot retraction. An intense intracellular 'machinery' is engaged to achieve these functions. Thrombin is one of the most important agonists for platelet recruitment and aggregation which is mediated by the binding of fibrinogen to its adhesive receptor: the glycoprotein (GP) IIb/IIIa complex or integrin alphaIIbbeta(3). The numerous biological processes consecutive to thrombin binding to platelet membrane are mainly controlled by phosphorylation mechanisms organized into signalling pathways. Schematically, the phospholipase Cbeta pathway activated by G protein coupled to the seven transmembrane thrombin receptors, provides the first intracellular relay and would generate regulators such as protein kinase C, phosphorylated pleckstrin but also modifications of the intracellular domain of beta(3). This inside-out signalling would lead to some changes in the extracellular domain of GPIIb/IIIa increasing access of fibrinogen to the receptor. Ligand interaction with GPIIb/IIIa induced reorganization of the cytoskeleton and would mediate the outside-in signals which involve a series of intracellular events including tyrosine kinases, phosphatidylinositol 3 kinases, MAP kinases and phosphatases. Some of these pathways and/or signalling metabolites could be associated to some well-characterized platelet functions: cortactin phosphorylation is involved in platelet shape change, phosphatidylinositol 3 kinase (p85) in the stabilisation of platelet aggregates and MAP kinase (p44) in postaggregation events. But in fact the sequence of events which has been described has to be viewed as integrated networks. At least three biochemical processes govern the highly integrated organization to send just the appropriate quanta of signal for a specific need: the reorganisation of the cytoskeleton following the binding of fibrinogen to alphaIIbbeta(3), the structure of the signal transducers that contain SH2, SH3, and PH domains leading to the formation of macromolecules of signalling and the crosstalk phenomena between the different pathways. Elucidating the mechanisms of such networks becomes an increasingly exciting project.

MeSH Terms
Animals Blood Platelets/metabolism Blood Proteins/chemistry,physiology Fibrinogen/physiology Humans MAP Kinase Signaling System Models, Biological Phosphatidylinositol 3-Kinases/physiology Phosphatidylinositol Diacylglycerol-Lyase Phosphoprotein Phosphatases/physiology Phosphoproteins Platelet Activation/physiology Platelet Glycoprotein GPIIb-IIIa Complex/physiology Protein Kinases/physiology Protein Processing, Post-Translational Signal Transduction/physiology Thrombin/physiology Type C Phospholipases/physiology src Homology Domains src-Family Kinases/physiology
Chemicals
Blood Proteins Phosphoproteins Platelet Glycoprotein GPIIb-IIIa Complex platelet protein P47 Fibrinogen Protein Kinases Phosphatidylinositol 3-Kinases src-Family Kinases Phosphoprotein Phosphatases Type C Phospholipases Thrombin Phosphatidylinositol Diacylglycerol-Lyase
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Lévy-Toledano S
INSERM U348, IFR 'Circulation Lariboisière', Hôpital Lariboisière, Paris, France.
Article Info
Journal
Haemostasis
Abbr.
Haemostasis
ISSN
0301-0147
Published
1999-09-00
Pages
4-15
Language
English
Region
Switzerland
NLM ID
0371574
Subset
IM
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