The role of actin-binding proteins in the control of endothelial barrier integrity

Alexander García-Ponce; Alí Francisco Citalán-Madrid; Martha Velázquez-Avila; Hilda Vargas-Robles; Michael Schnoor

doi:10.1160/TH14-04-0298

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 2015; 113(01): 20-36
DOI: 10.1160/TH14-04-0298

Review Article

Schattauer GmbH

The role of actin-binding proteins in the control of endothelial barrier integrity

Authors

Alexander García-Ponce

¹Department of Molecular Biomedicine, Center for Investigation and Advanced Studies of the National Polytechnic Institute (Cinvestav), Mexico-City, Mexico
Alí Francisco Citalán-Madrid

¹Department of Molecular Biomedicine, Center for Investigation and Advanced Studies of the National Polytechnic Institute (Cinvestav), Mexico-City, Mexico
Martha Velázquez-Avila

¹Department of Molecular Biomedicine, Center for Investigation and Advanced Studies of the National Polytechnic Institute (Cinvestav), Mexico-City, Mexico
Hilda Vargas-Robles

¹Department of Molecular Biomedicine, Center for Investigation and Advanced Studies of the National Polytechnic Institute (Cinvestav), Mexico-City, Mexico
Michael Schnoor

¹Department of Molecular Biomedicine, Center for Investigation and Advanced Studies of the National Polytechnic Institute (Cinvestav), Mexico-City, Mexico

Abstract

Summary

The endothelial barrier of the vasculature is of utmost importance for separating the blood stream from underlying tissues. This barrier is formed by tight and adherens junctions (TJ and AJ) that form intercellular endothelial contacts. TJ and AJ are integral membrane structures that are connected to the actin cytoskeleton via various adaptor molecules. Consequently, the actin cytoskeleton plays a crucial role in regulating the stability of endothelial cell contacts and vascular permeability. While a circumferential cortical actin ring stabilises junctions, the formation of contractile stress fibres, e. g. under inflammatory conditions, can contribute to junction destabilisation. However, the role of actin-binding proteins (ABP) in the control of vascular permeability has long been underestimated. Naturally, ABP regulate permeability via regulation of actin remodelling but some actin-binding molecules can also act independently of actin and control vascular permeability via various signalling mechanisms such as activation of small GTPases. Several studies have recently been published highlighting the importance of actin-binding molecules such as cortactin, ezrin/ radixin/moesin, Arp2/3, VASP or WASP for the control of vascular permeability by various mechanisms. These proteins have been described to regulate vascular permeability under various pathophysiological conditions and are thus of clinical relevance as targets for the development of treatment strategies for disorders that are characterised by vascular hyperpermeability such as sepsis. This review highlights recent advances in determining the role of ABP in the control of endothelial cell contacts and vascular permeability.

Keywords

Actin cytoskeleton - cell-cell interactions - endothelial cells - GTPases - inflammation - vascular permeability

Full Text

References

References
1 Neunert C, Lim W, Crowther M. et al. The American Society of Hematology 2011 evidence-based practice guideline for immune thrombocytopenia. Blood 2011; 117: 4190-4207.
2 Stasi R, Evangelista ML, Stipa E. et al. Idiopathic thrombocytopenic purpura: current concepts in pathophysiology and management. Thromb Haemost 2008; 99: 4-13.
3 Louwes H, Zeinali Lathori OA, Vellenga E. et al. Platelet kinetic studies in patients with idiopathic thrombocytopenic purpura. Am J Med 1999; 106: 430-434.
4 Webster ML, Sayeh E, Crow M. et al. Relative efficacy of intravenous immunog-lobulin G in ameliorating thrombocytopenia induced by antiplatelet GPIIblIIa versus GPIbalpha antibodies. Blood 2006; 108: 943-946.
5 McMillan R, Wang L, Tani P. Prospective evaluation of the immunobead assay for the diagnosis of adult chronic immune thrombocytopenic purpura (ITP). J Thromb Haemost 2003; 01: 485-491.
6 Andrews RK, Gardiner EE, Shen Y. et al. Glycoprotein Ib-IX-V. Int J Biochem Cell Biol 2003; 35: 1170-1174..
7 Li R, Emsley J. The organizing principle of the platelet glycoprotein Ib-IX-V complex. J Thromb Haemost 2013; 11: 605-614.
8 Li Z, Delaney MK, O’Brien KA. et al. Signalling during platelet adhesion and activation. Arterioscler Thromb Vasc Biol 2010; 30: 2341-2349.
9 Dai K, Bodnar R, Berndt MC. et al. A critical role for 14-3-3zeta protein in regulating the VWF binding function of platelet glycoprotein Ib-IX and its therapeutic implications. Blood 2005; 106: 1975-1981.
10 Beardsley DS, Ertem M. Platelet autoantibodies in immune thrombocytopenic purpura. Transfus Sci 1998; 19: 237-244.
11 Ruan C, Tobelem G, McMichael AJ. et al. Monoclonal antibody to human platelet glycoprotein I. II. Effects on human platelet function. Br J Haematol 1981; 49: 511-519.
12 Yanabu M, Ozaki Y, Nomura S. et al. Tyrosine phosphorylation and p72syk activation by an anti-glycoprotein Ib monoclonal antibody. Blood 1997; 89: 1590-1598.
13 Becker BH, Miller JL. Effects of an antiplatelet glycoprotein Ib antibody on he-mostatic function in the guinea pig. Blood 1989; 74: 690-694.
14 Cadroy Y, Hanson SR, Kelly AB. et al. Relative antithrombotic effects of monoclonal antibodies targeting different platelet glycoprotein-adhesive molecule interactions in nonhuman primates. Blood 1994; 83: 3218-3224.
15 Bergmeier W, Rackebrandt K, Schröder W. et al. Structural and functional characterisation of the mouse von Willebrand factor receptor GPIb-IX with novel monoclonal antibodies. Blood 2000; 95: 886-893.
16 Ruan CG, Du XP, Xi XD. et al. A murine antiglycoprotein Ib complex monoclonal antibody, SZ 2, inhibits platelet aggregation induced by both ristocetin and collagen. Blood 1987; 69: 570-577.
17 Du X, Beutler L, Ruan C. et al. Glycoprotein Ib and glycoprotein IX are fully complexed in the intact platelet membrane. Blood 1987; 69: 1524-1527.
18 Ruan CG. Monoclonal antibody SZ-21 to platelet membrane glycoprotein IIIa. Chin Med 1987; 67: 76-78.
19 Du X, Fox JE, Pei S. Identifcation of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Iba. J Biol Chem 1996; 271: 7362-7367.
20 Dai K, Wang Y, Yan R. et al. Effects of microgravity and hypergravity on platelet functions. Thromb Haemost 2009; 101: 902-910.
21 Hoffmeister KM, Felbinger TW, Falet H. et al. The clearance mechanism of chilled blood platelets. Cell 2003; 112: 87-97.
22 Hoffmeister KM, Josefsson EC, Isaac NA. et al. Glycosylation restores survival of chilled blood platelets. Science 2003; 301: 1531-1534.
23 Rumjantseva V, Grewal PK, Wandall HH. et al. Dual roles for hepatic lectin receptors in the clearance of chilled platelets. Nat Med 2009; 15: 1273-1280.
24 Jansen AJ, Josefsson EC, Rumjantseva V. et al. Desialylation accelerates platelet clearance after refrigeration and initiates GPIba metalloproteinase-mediated cleavage in mice. Blood 2012; 119: 1263-1273.
25 Miura S, Sakurai Y, Takatsuka H. et al. Total inhibition of high shear stress induced platelet aggregation by homodimeric von Willebrand factor A1-loop fragments. Br J Haematol 1999; 105: 1092-1100.