Evidence map›Paper›PMID 20238010›Full record

ArticleAdvances in experimental medicine and biology2010

Neural retina and MerTK-independent apical polarity of alphavbeta5 integrin receptors in the retinal pigment epithelium.

Mallika Mallavarapu, Silvia C Finnemann

Abstract read
In one paragraph

Article in Advances in experimental medicine and biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 16 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Phagocytosis by the retinal pigment epithelium: New insights into polarized cell mechanics.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  4. Review
  5. Above the Matrix: Functional Roles for Apically Localized Integrins.Frontiers in cell and developmental biology · 2021
    Review
  6. New Therapies of Neovascular AMD-Beyond Anti-VEGFs.Vision (Basel, Switzerland) · 2018
    Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Mallika MallavarapuGraduate School of Medical Sciences, Weill Cornell Medical College, New York, USA.
Silvia C Finnemann
Cornell University · USFordham University · US

Funding

Regulation of RPE phagocytosis via avb5 integrinR01EY013295 · NEI · WEILL MEDICAL COLL OF CORNELL UNIV · PI FINNEMANN, SILVIA C · 2003 to 2012
$4.8M
NEI NIH HHS R01 EY013295NEI NIH HHS R01-EY13295
6 · The paper itself

Abstract

The apical plasma membrane domain of retinal pigment epithelial (RPE) cells in the eye faces the outer segment portions of rods and cones and the interphotoreceptor matrix in the subretinal space. Two important receptor-mediated interactions between the apical surface of the retinal pigment epithelium (RPE) and adjacent photoreceptors are adhesion ensuring outer segment alignment and diurnal phagocytosis of shed outer segment fragments contributing to outer segment renewal. Both depend on the apical distribution of the integrin family adhesion receptor alphavbeta5 as lack of alphavbeta5 in mice causes weakened retinal adhesion and asynchronous phagocytosis. With age, lack of alphavbeta5 leads to accumulation of harmful lipofuscin in the RPE and to vision loss. Here, we discuss three different possible mechanisms that could generate the exclusive apical distribution of alphavbeta5 integrin receptors in the RPE. (1) alphavbeta5 could be apical in the RPE because RPE attachment to neural retina generally or alphavbeta5 ligands specifically in the subretinal space stabilize apical but not basolateral alphavbeta5 surface receptors. (2) alphavbeta5 could be apical in the RPE because it resides in a complex with other components of the phagocytic machinery that assembles at the apical, phagocytic surface of the RPE. (3) alphavbeta5 could be apical due to mechanisms intrinsic to this receptor protein and specifically to its beta5 integrin subunit.

Indexed as

Cell PolarityAnimalsBasic-Leucine Zipper Transcription FactorsCell Adhesionc-Mer Tyrosine KinaseEye ProteinsHumansMiceModels, BiologicalPhagocytosisProtein Structure, TertiaryProto-Oncogene ProteinsRatsReceptor Protein-Tyrosine KinasesReceptors, VitronectinRetinal Pigment EpitheliumBasic-Leucine Zipper Transcription Factorsc-Mer Tyrosine KinaseEye Proteinsintegrin alphaVbeta5Mertk protein, mouseNrl protein, mouseProto-Oncogene ProteinsReceptor Protein-Tyrosine KinasesReceptors, Vitronectin

Identifiers

PMID20238010
PMCPMC3235687
OpenAlexW189406518

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.