Evidence map›Paper›PMID 23441119›Full record

ArticleMolecular vision2013

Carbon turnover in the water-soluble protein of the adult human lens.

Daniel N Stewart, Jozsef Lango, Krishnan P Nambiar, Miranda J S Falso, Paul G FitzGerald, David M Rocke, Bruce D Hammock, Bruce A Buchholz

Open access · greenAbstract read
In one paragraph

Article in Molecular vision, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Paleoproteomics.Chemical reviews · 2022
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. γ-Crystallin redox-detox in the lens.The Journal of biological chemistry · 2018
    Article
  16. Article
  17. Article
  18. Review
  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

8 authors at 1 institution in 1 country.

Daniel N StewartDepartment of Chemistry, University of California, One Shields Avenue, Davis, CA, USA.
Jozsef Lango
Krishnan P Nambiar
Miranda J S Falso
Paul G FitzGerald
David M Rocke
Bruce D Hammock
Bruce A Buchholz
University of California, Davis · US

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
Workshop on Environmental Technology Transfer and EntrepreneurshipP42ES004699 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI HAMMOCK, BRUCE D · 1987 to 2021
$50.1M
UC DAVIS CLINICAL AND TRANSLATIONAL SCIENCE CENTER: BPCAUL1RR024146 · NCRR · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BERGLUND, LARS F · 2006 to 2011
$27.0M
VITAMIN C (ASCORBATE) METABOLISM IN DROSPHILA MELANOGASTERP41RR013461 · NCRR · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI ALLEN, LINDSAY H · 1999 to 2011
$20.8M
Resource for the Development of Biomedical Accelerator Mass Spectrometry (AMS)P41GM103483 · NIGMS · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI TURTELTAUB, KENNETH W. · 2012 to 2019
$12.0M
MOLECULAR ANALYSIS OF OCULAR LENS BEADED FILAMENTSR01EY008747 · NEI · UNIVERSITY OF CALIFORNIA DAVIS · PI FITZGERALD, PAUL GILLESPIE · 1990 to 2010
$4.5M
HYDROLYTIC ENZYMES IN THE METABOLISM OF TOXINSR01ES002710 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI HAMMOCK, BRUCE D · 1985 to 2018
$4.0M
Methods for Analysis of High Throughput Assay DataR01HG003352 · NHGRI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI ROCKE, DAVID M. · 2006 to 2008
$658k
Quantitation of protein turnover in the human adult lens using the 14C bomb-pulseR21EY018722 · NEI · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI BUCHHOLZ, BRUCE A · 2008 to 2009
$522k
NCI NIH HHS P30 CA093373NCRR NIH HHS 5P41RR013461NCRR NIH HHS P41 RR013461NCRR NIH HHS UL1 RR024146NCRR NIH HHS UL1RR024146NEI NIH HHS R01 EY008747NEI NIH HHS R01EY08747NEI NIH HHS R21 EY018722NEI NIH HHS R21EY018722NHGRI NIH HHS R01 HG003352NHGRI NIH HHS R01HG003352NIEHS NIH HHS P42 ES004699NIEHS NIH HHS P42ES004699NIEHS NIH HHS R01 ES002710NIEHS NIH HHS R01ES002710NIGMS NIH HHS 8P41GM103483NIGMS NIH HHS P41 GM103483
6 · The paper itself

Abstract

purposeHuman eye lenses contain cells that persist from embryonic development. These unique, highly specialized fiber cells located at the core (nucleus) of the lens undergo pseudo-apoptosis to become devoid of cell nuclei and most organelles. Ostensibly lacking in protein transcriptional capabilities, it is currently believed that these nuclear fiber cells owe their extreme longevity to the perseverance of highly stable and densely packed crystallin proteins. Maintaining the structural and functional integrity of lenticular proteins is necessary to sustain cellular transparency and proper vision, yet the means by which the lens actually copes with a lifetime of oxidative stress, seemingly without any capacity for protein turnover and repair, is not completely understood. Although many years of research have been predicated upon the assumption that there is no protein turnover or renewal in nuclear fiber cells, we investigated whether or not different protein fractions possess protein of different ages by using the (14)C bomb pulse.

methodsAdult human lenses were concentrically dissected by gently removing the cell layers in water or shaving to the nucleus with a curved micrometer-controlled blade. The cells were lysed, and the proteins were separated into water-soluble and water-insoluble fractions. The small molecules were removed using 3 kDa spin filters. The (14)C/C was measured in paired protein fractions by accelerator mass spectrometry, and an average age for the material within the sample was assigned using the (14)C bomb pulse.

resultsThe water-insoluble fractions possessed (14)C/C ratios consistent with the age of the cells. In all cases, the water-soluble fractions contained carbon that was younger than the paired water-insoluble fraction.

conclusionsAs the first direct evidence of carbon turnover in protein from adult human nuclear fiber cells, this discovery supports the emerging view of the lens nucleus as a dynamic system capable of maintaining homeostasis in part due to intricate protein transport mechanisms and possibly protein repair. This finding implies that the lens plays an active role in the aversion of age-related nuclear (ARN) cataract.

Indexed as

AdultAgedAged, 80 and overAgingCarbonCarbon RadioisotopesCrystallinsHumansLens Nucleus, CrystallineMiddle AgedProtein TransportSolubilityWaterCarbonCarbon RadioisotopesCrystallinsWater

Identifiers

PMID23441119
PMCPMC3580966
OpenAlexW2142561927

What OpenQuestion holds

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LicenceCC BY
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.