Evidence map›Paper›PMID 25461968›Full record

ReviewProgress in retinal and eye research2015

βA3/A1-crystallin: more than a lens protein.

J Samuel Zigler, Debasish Sinha

Open access · greenAbstract readReview
In one paragraph

Review in Progress in retinal and eye research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 19% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Role of glia in optic nerve.Progress in retinal and eye research · 2021
    Review
  11. Article
  12. Involvement of Anoikis in Dissociated Optic Nerve Fiber Layer Appearance.International journal of molecular sciences · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Genetic LAMP2 deficiency accelerates the age-associated formation of basal laminar deposits in the retina.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Review
  18. Article
  19. Article
  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

2 authors at 1 institution in 1 country.

J Samuel ZiglerThe Johns Hopkins University School of Medicine, The Wilmer Eye Institute, 400 North Broadway, Smith Building Room M037, Baltimore, MD 21231, USA. Electronic address: szigler1@jhmi.edu.
Debasish SinhaThe Johns Hopkins University School of Medicine, The Wilmer Eye Institute, 400 North Broadway, Smith Building Room M035, Baltimore, MD 21231, USA. Electronic address: Debasish@jhmi.edu.
Johns Hopkins Medicine · US

Funding

Wilmer Core Grant for Vision ResearchP30EY001765 · NEI · JOHNS HOPKINS UNIVERSITY · PI Jiang Qian · 1985 to 2026
$22.1M
A novel bA3/A1-crystallin gene mutation results in persistent fetal vasculatureR01EY019037 · NEI · JOHNS HOPKINS UNIVERSITY · PI SINHA, DEBASISH · 2008 to 2015
$4.1M
A CRYSTALLIN MUTATION WITH ABNORMAL ASTROCYTES AND RETINAL VESSELSR01EY018636 · NEI · JOHNS HOPKINS UNIVERSITY · PI SINHA, DEBASISH · 2009 to 2010
$820k
Intramural NIH HHSNEI NIH HHS EY01765NEI NIH HHS EY018636NEI NIH HHS EY019037NEI NIH HHS EY019037-SNEI NIH HHS P30 EY001765NEI NIH HHS R01 EY018636NEI NIH HHS R01 EY019037
6 · The paper itself

Abstract

Crystallins, the highly abundant proteins of the ocular lens, are essential determinants of the transparency and refractivity required for lens function. Initially thought to be lens-specific and to have evolved as lens proteins, it is now clear that crystallins were recruited to the lens from proteins that existed before lenses evolved. Crystallins are expressed outside of the lens and most have been shown to have cellular functions distinct from their roles as structural elements in the lens. For one major crystallin group, the β/γ-crystallin superfamily, no such functions have yet been established. We have explored possible functions for the polypeptides (βA3-and βA1-crystallins) encoded by Cryba1, one of the 6 β-crystallin genes, using a spontaneous rat mutant and genetically engineered mouse models. βA3-and βA1-crystallins are expressed in retinal astrocytes and retinal pigment epithelial (RPE) cells. In both cell types, these proteins appear to be required for the proper acidification of the lysosomes. In RPE cells, elevated pH in the lysosomes is shown to impair the critical processes of phagocytosis and autophagy, leading to accumulation of undigested cargo in (auto) phagolysosomes. We postulate that this accumulation may cause pathological changes in the cells resembling some of those characteristic of age-related macular degeneration (AMD). Our studies suggest an important regulatory function of βA3/A1-crystallin in astrocytes. We provide evidence that the cellular function of βA3/A1-crystallin involves its interaction with V-ATPase, the proton pump responsible for acidification of the endolysosomal system.

Indexed as

AnimalsAstrocytesbeta-Crystallin A ChainDisease Models, AnimalHumansLysosomesMiceRatsRetinaRetinal Pigment EpitheliumSignal TransductionVacuolar Proton-Translocating ATPasesbeta-Crystallin A ChainVacuolar Proton-Translocating ATPasesAnimal modelAstrocyteLysosomeRetinal pigment epithelial cellSignalingβA3/A1-crystallin

Identifiers

PMID25461968
PMCPMC4268165
OpenAlexW2038569321

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.