Cited by 72Retinal Development and DisordersCell Adhesion Molecules ResearchRetinal Diseases and Treatments

Novel role for α v β 5 -integrin in retinal adhesion and its diurnal peak

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Nandrot, Emeline F., Anand, Monika, Sircar, Mousumi, Finnemann, Silvia C.·2006·American Journal of Physiology-Cell Physiology

Abstract

alpha(v)beta(5)-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(v)beta(5)-integrin in permanent RPE-photoreceptor adhesion that is independent of alpha(v)beta(5)'s function in retinal phagocytosis. To compare retinal adhesion of wild-type and beta(5)-integrin(-/-) mice, we mechanically separated RPE and neural retina and quantified RPE protein and pigment retention with the neural retina. Lack of alpha(v)beta(5)-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(v)beta(5) receptor deficiency attenuated the diurnal peak of retinal adhesion in beta(5)-integrin(-/-) mice. These results identify alpha(v)beta(5)-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(v)beta(5) receptors at the same apical plasma membrane domain of RPE cells fulfill two separate functions that are synchronized by different diurnal rhythms.

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Crossref · 10.1152/ajpcell.00480.2005

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  • The strength of retinal adhesion peaked 3.5 h after light onset, past the phagocytic peak.

    “The strength of adhesion peaked 3.5 h after light onset, i.e., past the phagocytic peak (Nandrot et al., 2006).”

    From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Nandrot et al., 2006

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Authors
Nandrot, E. F., Anand, M., Sircar, M., & Finnemann, S. C.
Affiliations
Cornell University (US)
Venue
American Journal of Physiology-Cell Physiology
Published
2006-04
Volume
290
Issue
4
Pages
C1256-C1262
ISSN
  • 0363-6143 (ISSN-L)
  • 1522-1563
OpenAlex
W2337798073
Cited by
72
References
28
Citations by year
2026: 2 · 2025: 3 · 2024: 2 · 2023: 2 · 2022: 7 · 2021: 3 · 2020: 4 · 2019: 1 · 2017: 5 · 2016: 4 · 2015: 3 · 2014: 4 · 2013: 2 · 2012: 6
FWCI
1.76
Type
journal article
Language
en
Open access
Locations
  • American Journal of Physiology-Cell Physiology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Research to Prevent Blindness
  • National Eye Institute (R01EY013295, EY-13295, EY-14184, R03EY014184)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
  • Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
  • Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
Keywords
alpha v beta 5 integrin, retinal pigment epithelium, diurnal cycle, circadian rhythm, MERTK, integrin signaling, pigment retention
MeSH terms
Ezrin, Retinoid Isomerohydrolase, Animals, Carrier Proteins, Cell Adhesion, Circadian Rhythm, Cytoskeletal Proteins, Eye Proteins, Phagocytosis, Pigment Epithelium of Eye, Signal Transduction, Integrins, Mice, Knockout, Receptors, Vitronectin, cis-trans-Isomerases, Photoreceptor Cells, Vertebrate, Protein Subunits, Integrin beta Chains, Mice

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