Evidence map›Paper›PMID 26852705›Full record

ReviewBiological reviews of the Cambridge Philosophical Society2017

The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1.

Laura C D Pomatto, Rachel Raynes, Kelvin J A Davies

Open access · greenAbstract readReview
In one paragraph

Review in Biological reviews of the Cambridge Philosophical Society, 2017. 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
3.3field-weighted citation impact, top 8% 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, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Molecular mechanisms of mitochondrial AAA+ proteases.The Journal of biological chemistry · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Organelle abnormalities in Alzheimer's disease.Organelle (Tucson, Ariz.) · 2025
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  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

3 authors at 1 institution in 1 country.

Laura C D PomattoEthel Percy Andrus Gerontology Center of the Davis School of Gerontology and Division of Molecular & Computational Biology, Department of Biological Sciences of the College of Letters, Arts & Sciences, University of Southern California, 3715 McClintock Avenue, Los Angeles, CA, 90089-0191, U.S.A.
Rachel RaynesEthel Percy Andrus Gerontology Center of the Davis School of Gerontology and Division of Molecular & Computational Biology, Department of Biological Sciences of the College of Letters, Arts & Sciences, University of Southern California, 3715 McClintock Avenue, Los Angeles, CA, 90089-0191, U.S.A.
Kelvin J A DaviesEthel Percy Andrus Gerontology Center of the Davis School of Gerontology and Division of Molecular & Computational Biology, Department of Biological Sciences of the College of Letters, Arts & Sciences, University of Southern California, 3715 McClintock Avenue, Los Angeles, CA, 90089-0191, U.S.A.
University of Southern California · US

Funding

OXYGEN RADICAL TOXICITY AND RED CELL PROTEIN DEGRADATIONR01ES003598 · NIEHS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI DAVIES, KELVIN J. A. · 1988 to 2017
$5.7M
USC Geroscience Training in the Biology of AgingT32AG052374 · NIA · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Sean P CURRAN · 2016 to 2026
$5.3M
NIA NIH HHS T32 AG052374NIEHS NIH HHS R01 ES003598
6 · The paper itself

Abstract

Peroxisomes are ubiquitous eukaryotic organelles with the primary role of breaking down very long- and branched-chain fatty acids for subsequent β-oxidation in the mitochondrion. Like mitochondria, peroxisomes are major sites for oxygen utilization and potential contributors to cellular oxidative stress. The accumulation of oxidatively damaged proteins, which often develop into inclusion bodies (of oxidized, aggregated, and cross-linked proteins) within both mitochondria and peroxisomes, results in loss of organelle function that may contribute to the aging process. Both organelles possess an isoform of the Lon protease that is responsible for degrading proteins damaged by oxidation. While the importance of mitochondrial Lon (LonP1) in relation to oxidative stress and aging has been established, little is known regarding the role of LonP2 and aging-related changes in the peroxisome. Recently, peroxisome dysfunction has been associated with aging-related diseases indicating that peroxisome maintenance is a critical component of 'healthy aging'. Although mitochondria and peroxisomes are both needed for fatty acid metabolism, little work has focused on understanding the relationship between these two organelles including how age-dependent changes in one organelle may be detrimental for the other. Herein, we summarize findings that establish proteolytic degradation of damaged proteins by the Lon protease as a vital mechanism to maintain protein homeostasis within the peroxisome. Due to the metabolic coordination between peroxisomes and mitochondria, understanding the role of Lon in the aging peroxisome may help to elucidate cellular causes for both peroxisome and mitochondrial dysfunction.

Indexed as

AgingDiseaseHumansMitochondriaOxidative StressPeroxisomesProtease LaProtease LaagingchaperonehormesisLon proteasemitochondriamitochondrial DNAoxidative stressperoxisomereactive oxygen species

Identifiers

PMID26852705
PMCPMC5159316
OpenAlexW2254819329

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.