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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/7808

Title: Barrier integrity of the corneal endothelium: regulation by contractility of the actin cytoskeleton
Authors: JANS, Danny
Mahesh, Shivanna
Ramachandran, Charanya
Jalimarada, Supriya
Srinivas, Sangly P.
Issue Date: 2007
Citation: FASEB JOURNAL, 21(6). p. A913-A913
Abstract: Purpose: This study demonstrates endothelial cell signalling, influencing its barrier integrity through actin cytoskeleton contraction. Methods: In cultured bovine corneal endothelia, myosin light chain (MLC) phosphorylation was assayed by Westens blotting after urea-glycerol gel electrophoresis. Actin cytoskeleton reorganisation was evaluated by phalloidin staining. Barrier integrity was assayed as tracer solute (HRP and /or carboxyfluorescein) permeability and transendothelial electrical resistance (TER) changes. Results: Resting corneal endothelial cells show a hexagonal morphology with a thick band of cortical actin. The PAR-1 agonist thrombin (2 U/ml) induced MLC phosphorylation, cortical actin disruption and appearance of interendothelial gaps. HRP permeability increased several fold. Responses were inhibited by Y-27632 or adenosine. Histamine caused MLC phosphorylation, a significan tincrease in carboxyfluorescein permeability and actin cytoskeleton disruption. Responses were inhibited by adenosine, by ML-7 (an MLCK inhibitor) or chelerythrine (PKC inhibitor). Adenosine increased TER and its inhibitory effects were mimicked by forskolin. Conclusions: MLC phosphorylation is inhibited by PKA but stimulated by Rho kinase. These results provide further understanding how corneal endothelium regulates stromal hydration through active modulation of its barrier integrity.
Notes: Hasselt Univ, Diepenbeek, B-3590 Belgium. Indiana Univ, Sch Optometry, Bloomington, IN 47405 USA.
URI: http://hdl.handle.net/1942/7808
ISI #: 000245708701295
ISSN: 0892-6638
Category: M
Type: Journal Contribution
Appears in Collections: Research publications

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