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Am J Physiol Cell Physiol 290: C1256-C1262, 2006. First published December 7, 2005; doi:10.1152/ajpcell.00480.2005
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EXTRACELLULAR MATRIX, CELL INTERACTIONS

Novel role for {alpha}vbeta5-integrin in retinal adhesion and its diurnal peak

Emeline F. Nandrot,1 Monika Anand,1 Mousumi Sircar,1 and Silvia C. Finnemann1,2,3

1Margaret M. Dyson Vision Research Institute, Department of Ophthalmology, 2Department of Cell and Developmental Biology, and 3Department of Physiology and Biophysics, Weill Medical College of Cornell University, New York, New York

Submitted 27 September 2005 ; accepted in final form 1 December 2005

{alpha}vbeta5-Integrin is the sole integrin receptor at the retinal pigment epithelium (RPE)-photoreceptor interface and promotes RPE phagocytic signaling to the tyrosine kinase Mer tyrosine kinase (MerTK) once a day in response to circadian photoreceptor shedding. Herein we identify a novel role for {alpha}vbeta5-integrin in permanent RPE-photoreceptor adhesion that is independent of {alpha}vbeta5's function in retinal phagocytosis. To compare retinal adhesion of wild-type and beta5-integrin–/– mice, we mechanically separated RPE and neural retina and quantified RPE protein and pigment retention with the neural retina. Lack of {alpha}vbeta5-integrin with normal expression of other RPE integrins greatly weakened retinal adhesion in young mice and accelerated its age-dependent decline. Unexpectedly, the strength of wild-type retinal adhesion varied with a diurnal rhythm that peaked 3.5 h after light onset, after the completion of phagocytosis, when integrin signaling to MerTK is minimal. Permanent {alpha}vbeta5 receptor deficiency attenuated the diurnal peak of retinal adhesion in beta5-integrin–/– mice. These results identify {alpha}vbeta5-integrin as the first RPE receptor that contributes to retinal adhesion, a vital mechanism for long-term photoreceptor function and viability. Furthermore, they indicate that {alpha}vbeta5 receptors at the same apical plasma membrane domain of RPE cells fulfill two separate functions that are synchronized by different diurnal rhythms.

circadian rhythm; knockout; photoreceptors; retinal pigment epithelium


Address for reprint requests and other correspondence: S. C. Finnemann, Dyson Vision Research Institute, LC305, Box 233, Weill Medical College of Cornell Univ., 1300 York Ave., New York, NY 10021 (e-mail:sfinne{at}med.cornell.edu)




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