Evidence map›Paper›PMID 21511033›Full record

ArticleBiochimica et biophysica acta2011

Unique and analogous functions of aquaporin 0 for fiber cell architecture and ocular lens transparency.

S Sindhu Kumari, Subramaniam Eswaramoorthy, Richard T Mathias, Kulandaiappan Varadaraj

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

30 citing papers in PubMed, 36 citations in OpenAlex.

  1. CatExperimental eye research · 2026
    Article
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  3. Functional characterization of CatExperimental eye research · 2025
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  7. Review
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  11. Cleavage C-terminal to Asp leads to covalent crosslinking of long-lived human proteins.Biochimica et biophysica acta. Proteins and proteomics · 2019
    Article
  12. Article
  13. C-Terminal End of Aquaporin 0 Regulates Lens Gap Junction Channel Function.Investigative ophthalmology & visual science · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Aquaporin 5 promotes corneal wound healing.Experimental eye research · 2018
    Article
  18. Article
  19. Review
  20. 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

4 authors at 2 institutions in 1 country.

S Sindhu KumariDepartment of Physiology and Biophysics, State University of New York at Stony Brook, Stony Brook, NY 11794-8661, USA.
Subramaniam Eswaramoorthy
Richard T Mathias
Kulandaiappan Varadaraj
State University of New York · USBrookhaven National Laboratory · US

Funding

VOLUME REGULATION IN NORMAL AND CATARACTOUS LENSESR01EY006391 · NEI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MATHIAS, RICHARD T · 1985 to 2014
$5.4M
Role of Aquaporin-0 for cell-to-cell adhesion and lens transparencyR01EY020506 · NEI · STATE UNIVERSITY NEW YORK STONY BROOK · PI VARADARAJ, KULANDAIAPPAN · 2010 to 2013
$1.6M
NEI NIH HHS EY06391NEI NIH HHS R01 EY006391NEI NIH HHS R01 EY020506NEI NIH HHS R01 EY 20506
6 · The paper itself

Abstract

Aquaporin (AQP) 1 and AQP0 water channels are expressed in lens epithelial and fiber cells, respectively, facilitating fluid circulation for nourishing the avascular lens to maintain transparency. Even though AQP0 water permeability is 40-fold less than AQP1, AQP0 is selectively expressed in the fibers. Delimited AQP0 fiber expression is attributed to a unique structural role as an adhesion protein. To validate this notion, we determined if wild type (WT) lens ultrastructure and fiber cell adhesion are different in AQP0(-/-), and TgAQP1(+/+)/AQP0(-/-) mice that transgenically express AQP1 (TgAQP1) in fiber cells without AQP0 (AQP0(-/-)). In WT, lenses were transparent with 'Y' sutures. Fibers contained opposite end curvature, lateral interdigitations, hexagonal shape, and were arranged as concentric growth shells. AQP0(-/-) lenses were cataractous, lacked 'Y' sutures, ordered packing and well-defined lateral interdigitations. TgAQP1(+/+)/AQP0(-/-) lenses showed improvement in transparency and lateral interdigitations in the outer cortex while inner cortex and nuclear fibers were severely disintegrated. Transmission electron micrographs exhibited tightly packed fiber cells in WT whereas AQP0(-/-) and TgAQP1(+/+)/AQP0(-/-) lenses had wide extracellular spaces. Fibers were easily separable by teasing in AQP0(-/-) and TgAQP1(+/+)/AQP0(-/-) lenses compared to WT. Our data suggest that the increased water permeability through AQP1 does not compensate for loss of AQP0 expression in TgAQP1(+/+)/AQP0(-/-) mice. Fiber cell AQP0 expression is required to maintain their organization, which is a requisite for lens transparency. AQP0 appears necessary for cell-to-cell adhesion and thereby to minimize light scattering since in the AQP0(-/-) and TgAQP1(+/+)/AQP0(-/-) lenses, fiber cell disorganization was evident.

Indexed as

AnimalsAquaporin 1AquaporinsCataractEye ProteinsLens, CrystallineMiceMice, KnockoutMicroscopy, Electron, ScanningModels, Molecularaquaporin 0Aquaporin 1AquaporinsEye Proteins

Identifiers

PMID21511033
PMCPMC3143309
OpenAlexW2118817090

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.