Evidence map›Paper›PMID 34896599›Full record

ReviewProgress in retinal and eye research2022

Clusterin, other extracellular chaperones, and eye disease.

Mark R Wilson, Sandeep Satapathy, Shinwu Jeong, M Elizabeth Fini

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Progress in retinal and eye research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

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  8. Clusterin: structure, function and roles in disease.International journal of medical sciences · 2025
    Review
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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 3 institutions in 3 countries.

Mark R WilsonMolecular Horizons and the School of Chemistry and Molecular Bioscience, University of Wollongong; Illawarra Health and Medical Research Institute, Northfields Avenue, Wollongong, New South Wales, 2522, Australia. Electronic address: mrw@uow.edu.au.
Sandeep SatapathyMolecular Horizons and the School of Chemistry and Molecular Bioscience, University of Wollongong; Illawarra Health and Medical Research Institute, Northfields Avenue, Wollongong, New South Wales, 2522, Australia. Electronic address: ss739@uowmail.edu.au.
Shinwu JeongUSC Roski Eye Institute and Department of Ophthalmology, Keck School of Medicine of USC, University of Southern California, 1333 San Pablo Street., Los Angeles, CA, 90033, USA. Electronic address: shinwuje@med.usc.edu.
M Elizabeth FiniNew England Eye Center, Tufts Medical Center and Department of Ophthalmology, Tufts University School of Medicine; Program in Pharmacology & Drug Development, Graduate School of Biomedical Sciences, Tufts University, 800 Washington St, Boston, MA, 02111, USA. Electronic address: mefini@tuftsmedicalcenter.org.
University of Wollongong · AUTufts University · USUniversity of Southern California · US

Funding

Clusterin at the Ocular Surface Administrative Supplement IIR01EY026479 · NEI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FINI, M ELIZABETH · 2016 to 2020
$2.9M
Discovery Approach to Ocular HypertensionR01EY027315 · NEI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI FINI, M ELIZABETH, GAO, XIAOYI RAYMOND · 2017 to 2020
$2.4M
NEI NIH HHS R01 EY026479NEI NIH HHS R01 EY027315
6 · The paper itself

Abstract

Proteostasis refers to all the processes that maintain the correct expression level, location, folding and turnover of proteins, essential to organismal survival. Both inside cells and in body fluids, molecular chaperones play key roles in maintaining proteostasis. In this article, we focus on clusterin, the first-recognized extracellular mammalian chaperone, and its role in diseases of the eye. Clusterin binds to and inhibits the aggregation of proteins that are misfolded due to mutations or stresses, clears these aggregating proteins from extracellular spaces, and facilitates their degradation. Clusterin exhibits three main homeostatic activities: proteostasis, cytoprotection, and anti-inflammation. The so-called "protein misfolding diseases" are caused by aggregation of misfolded proteins that accumulate pathologically as deposits in tissues; we discuss several such diseases that occur in the eye. Clusterin is typically found in these deposits, which is interpreted to mean that its capacity as a molecular chaperone to maintain proteostasis is overwhelmed in the disease state. Nevertheless, the role of clusterin in diseases involving such deposits needs to be better defined before therapeutic approaches can be entertained. A more straightforward case can be made for therapeutic use of clusterin based on its proteostatic role as a proteinase inhibitor, as well as its cytoprotective and anti-inflammatory properties. It is likely that clusterin works together in this way with other extracellular chaperones to protect the eye from disease, and we discuss several examples. We end this article by predicting future steps that may lead to development of clusterin as a biological drug.

Indexed as

ClusterinEye DiseasesAnimalsHumansMammalsProteostasisClusterinAnti-inflammationClusterinCytoprotectionExtracellular chaperoneEyeProteostasis

Identifiers

PMID34896599
PMCPMC9184305
OpenAlexW4200127624

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.