NDLI: Effect of elevated intracellular cAMP levels on actomyosin contraction in bovine trabecular meshwork cells.

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Effect of elevated intracellular cAMP levels on actomyosin contraction in bovine trabecular meshwork cells.

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Effect of elevated intracellular cAMP levels on actomyosin contraction in bovine trabecular meshwork cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Srinivas, Sangly P. Ramachandran, Charanya Sharif, Najam A. Patil, Rajkumar V.
Description	Country affiliation: United States Author Affiliation: Ramachandran C ( School of Optometry, Indiana University, Bloomington, Indiana 47405, USA.)
Abstract	PURPOSE: Elevated cAMP in the trabecular meshwork (TM) cells increases the aqueous humor outflow facility. The authors investigated the mechanisms by which elevated cAMP opposes the RhoA-Rho kinase pathway, leading to the relaxation of the actomyosin system in bovine TM cells. METHODS: Forskolin (Fsk) and rolipram were used to elevate cAMP levels. Changes in the phosphorylation of RhoA at Ser188 (a putative inhibitory site), the regulatory light chain of myosin (pMLC), and the regulatory subunit of myosin phosphatase (MYPT1) were determined by Western blot analysis. The actomyosin contraction was measured by collagen gel contraction (CGC) assay. The impact of cAMP on cell-matrix adhesion was followed by immunostaining of focal adhesion proteins and by electric cell-substrate impedance sensing. RESULTS: Elevated cAMP led to an increase in the phosphorylation of RhoA at Ser188, to the inhibition of endothelin-1 (ET-1)-induced activation of RhoA, and to the formation of stress fibers. The loss of pMLC along the stress fibers was comparable to that induced by Y-27632 (Rho kinase inhibitor). A concomitant reduction in both MYPT1 phosphorylation and pMLC was observed. Elevated cAMP also reduced (ET-1)-induced CGC and the cell-substrate resistance by >50%. CONCLUSIONS: In TM cells, elevated cAMP leads to the phosphorylation of RhoA at Ser188. Consequent inhibition of RhoA activity reduces the phosphorylation of MYPT1 at Thr853, leading to a reduction in MLC phosphorylation and actomyosin contraction. These actions, similar to those of the Rho kinase inhibitors, possibly underlie the reported increase in outflow facility in response to Fsk perfusion ex vivo.
ISSN	01460404
e-ISSN	15525783
DOI	10.1167/iovs.10-6241
Journal	Investigative Opthalmology & Visual Science
Issue Number	3
Volume Number	52
Language	English
Publisher	Association for Research in Vision and Ophthalmology
Publisher Date	2011-03-18
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Actomyosin Metabolism Cyclic Amp Trabecular Meshwork Drug Effects Actin Depolymerizing Factors Adenylate Cyclase Genetics Animals Blotting, Western Cell Shape Cells, Cultured Colforsin Pharmacology Electric Impedance Electrophoresis, Polyacrylamide Gel Fluorescent Antibody Technique, Indirect Focal Adhesions Myosin Light Chains Myosin-light-chain Phosphatase Phosphorylation Reverse Transcriptase Polymerase Chain Reaction Rolipram Serine Cytology Rhoa Gtp-binding Protein Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Discipline Ophthalmology
Content Type	Text
Resource Type	Article
Subject	Ophthalmology Sensory Systems Cellular and Molecular Neuroscience

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