Evidence map›Paper›PMID 18227073›Full record

ArticleThe Journal of biological chemistry2008

Significance of interactions of low molecular weight crystallin fragments in lens aging and cataract formation.

Puttur Santhoshkumar, Padmanabha Udupa, Raju Murugesan, K Krishna Sharma

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

51 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
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  6. Article
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  13. Article
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  15. Article
  16. Review
  17. Current Trends in the Pharmacotherapy of Cataracts.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  18. Molecular Processes Implicated in Human Age-Related Nuclear Cataract.Investigative ophthalmology & visual science · 2019
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Puttur SanthoshkumarDepartment of Ophthalmology, University of Missouri-Columbia School of Medicine, Columbia, MO 65212, USA.
Padmanabha Udupa
Raju Murugesan
K Krishna Sharma
University of Missouri · US

Funding

FUNCTIONAL ELEMENTS IN ALPHA CRYSTALLIN CHAPERONER01EY011981 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 1998 to 2010
$2.8M
AMINOPEPTIDASES IN NORMAL AND CATARACT LENSESR01EY009855 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 1999 to 2009
$1.7M
PROTEIN AND HISTOLOGY MINICORE GRANT FOR VISION RESEARCHR24EY014795 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 2003 to 2007
$855k
AMINOPEPTIDASES IN NORMAL AND CATARACT LENSESR29EY009855 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 1993 to 1997
–
NEI NIH HHS EY009855NEI NIH HHS EY 11981NEI NIH HHS EY 14795NEI NIH HHS R01 EY011981NEI NIH HHS R24 EY014795
6 · The paper itself

Abstract

Analysis of aged and cataract lenses shows the presence of increased amounts of crystallin fragments in the high molecular weight aggregates of water-soluble and water-insoluble fractions. However, the significance of accumulation and interaction of low molecular weight crystallin fragments in aging and cataract development is not clearly understood. In this study, 23 low molecular mass (<3.5-kDa) peptides in the urea-soluble fractions of young, aged, and aged cataract human lenses were identified by mass spectroscopy. Two peptides, alphaB-(1-18) (MDIAIHHPWIRRPFFPFH) and betaA3/A1-(59-74) (SD(N)AYHIERLMSFRPIC), present in aged and cataract lens but not young lens, and a third peptide, gammaS-(167-178) (SPAVQSFRRIVE) present in all three lens groups were synthesized to study the effects of interaction of these peptides with intact alpha-, beta-, and gamma-crystallins and alcohol dehydrogenase, a protein used in aggregation studies. Interaction of alphaB-(1-18) and betaA3/A1-(59-74) peptides increased the scattering of light by beta- and gamma-crystallin and alcohol dehydrogenase. The ability of alpha-crystallin subunits to function as molecular chaperones was significantly reduced by interaction with alphaB-(1-18) and betaA3/A1-(59-74) peptides, whereas gammaS peptide had no effect on chaperone-like activity of alpha-crystallin. The betaA3/A1-(59-74 peptide caused a 5.64-fold increase in alphaB-crystallin oligomeric mass and partial precipitation. Replacing hydrophobic residues in alphaB-(1-18) and betaA3/A1-(59-74) peptides abolished their ability to induce crystallin aggregation and light scattering. Our study suggests that interaction of crystallin-derived peptides with intact crystallins could be a key event in age-related protein aggregation in lens and cataractogenesis.

Indexed as

AdolescentAdultAgedAged, 80 and overAgingAmino Acid SequenceAnimalsCataractCattleCrystallinsHumansLens, CrystallineMolecular ChaperonesMolecular Sequence DataMolecular WeightPeptide FragmentsCrystallinsMolecular ChaperonesPeptide Fragments

Identifiers

PMID18227073
PMCPMC2417163
OpenAlexW2044754760

What OpenQuestion holds

Textmetadata
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.