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BibTeX
Thrombin promotes actin stress fiber formation in RPE through Rho/ROCK-mediated MLC phosphorylation
Journal of cellular physiology, 2011-02, Vol.226 (2), p.414-423
Ruiz-Loredo, Ariadna Yolanda
López, Edith
López-Colomé, Ana María
2011
Details
Autor(en) / Beteiligte
Ruiz-Loredo, Ariadna Yolanda
López, Edith
López-Colomé, Ana María
Titel
Thrombin promotes actin stress fiber formation in RPE through Rho/ROCK-mediated MLC phosphorylation
Ist Teil von
Journal of cellular physiology, 2011-02, Vol.226 (2), p.414-423
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2011
Link zum Volltext
Quelle
Wiley
Beschreibungen/Notizen
The retinal pigment epithelium (RPE) forms the outer blood–retina barrier (BRB). Most retinal diseases involve BRB breakdown, whereupon thrombin contained in serum directly contacts the RPE. Thrombin is known to promote actin stress fiber formation, an important determinant in eye diseases involving the epithelial–mesenchymal transition (EMT) and migration of RPE cells, such as proliferative vitreoretinopathy. We analyzed thrombin effect on signaling pathways leading to myosin light chain (MLC) phosphorylation and actin stress fiber formation in primary cultures of rat RPE cells, in order to support a role for thrombin in RPE transdifferentiation. MLC phosphorylation was measured by Western blot; actin cytoskeleton was visualized using immunofluorescent phalloidin, and Rho GTPase activation was assessed by ELISA. We showed that thrombin/PAR‐1 induces the time‐ and dose‐dependent phosphorylation of MLC through the activation of Rho/ROCK and myosin light chain kinase (MLCK). ROCK increased phospho‐MLC by phosphorylating MLC and by inhibiting MLC phosphatase. Thrombin effect was abolished by the ROCK inhibitor Y‐27632, whereas MLCK inhibitor ML‐7 and PLC‐β inhibitor U73122 attenuated MLC phosphorylation by ≈50%, suggesting the activation of MLCK by PLC‐β‐mediated calcium increase. Additionally, thrombin‐induced MLC phosphorylation was blocked by the inhibitory PKCζ pseudosubstrate, wortmannin, and LY294002, indicating IP3/PKCζ involvement in the control of MLC phosphorylation. Moreover, we demonstrated that thrombin effect on MLC induces actin stress fiber formation, since this effect was prevented by inhibiting the pathways leading to MLC phosphorylation. We conclude that thrombin stimulation of MLC phosphorylation and actin stress fiber formation may be involved in thrombin‐induced RPE cell transformation subsequent to BRB dysfunction. J. Cell. Physiol. 226: 414–423, 2011. © 2010 Wiley‐Liss, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 0021-9541
eISSN: 1097-4652
DOI: 10.1002/jcp.22347
Titel-ID: cdi_proquest_miscellaneous_815550821
Format
–
Schlagworte
Actins - metabolism
,
Animals
,
Blood-Retinal Barrier - metabolism
,
Cells, Cultured
,
Enzyme Activation
,
Enzyme Inhibitors - metabolism
,
Myosin Light Chains - metabolism
,
Myosin-Light-Chain Kinase - metabolism
,
Phosphatidylinositol 3-Kinases - metabolism
,
Phospholipase C beta - metabolism
,
Phosphorylation
,
Rats
,
Rats, Long-Evans
,
Retinal Pigment Epithelium - cytology
,
Retinal Pigment Epithelium - drug effects
,
Retinal Pigment Epithelium - metabolism
,
rho-Associated Kinases - metabolism
,
Signal Transduction - physiology
,
Stress Fibers - metabolism
,
Thrombin - pharmacology
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