Evidence map›Paper›PMID 33092174›Full record

ArticleCells2020

In Vivo Remodeling of Altered Autophagy-Lysosomal Pathway by a Phosphopeptide in Lupus.

Fengjuan Wang, Inmaculada Tasset, Ana Maria Cuervo, Sylviane Muller

Open access · goldAbstract read
In one paragraph

Article in Cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Therapeutic effects of peptide P140 in a mouse periodontitis model.Cellular and molecular life sciences : CMLS · 2022
    Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Autophagy in major human diseases.The EMBO journal · 2021
    Review
  16. Article
  17. Review
  18. Review
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 2 institutions in 2 countries.

Fengjuan WangBiotechnology and Cell Signaling, CNRS-University of Strasbourg, Illkirch, France/Laboratory of Excellence Medalis, Institut de Science et d'Ingénierie Supramoléculaire, 67000 Strasbourg, France.
Inmaculada TassetDepartment of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Ana Maria CuervoDepartment of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Sylviane MullerBiotechnology and Cell Signaling, CNRS-University of Strasbourg, Illkirch, France/Laboratory of Excellence Medalis, Institut de Science et d'Ingénierie Supramoléculaire, 67000 Strasbourg, France.ORCID 0000-0002-0481-0620
Albert Einstein College of Medicine · USCentre National de la Recherche Scientifique · FR

Funding

Einstein's Nathan Shock Center of Excellence in Basic Biology of AgingP30AG038072 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI HUFFMAN, DEREK MAJOR · 2010 to 2024
$10.8M
NIA NIH HHS P30 AG038072
6 · The paper itself

Abstract

The phosphopeptide P140/Lupuzor, which improves the course of lupus disease in mice and patients, targets chaperone-mediated autophagy (CMA), a selective form of autophagy that is abnormally upregulated in lupus-prone MRL/lpr mice. Administered intravenously to diseased mice, P140 reduces the expression level of two major protein players of CMA, LAMP2A and HSPA8, and inhibits CMA in vitro in a cell line that stably expresses a CMA reporter. Here, we aimed to demonstrate that P140 also affects CMA in vivo and to unravel the precise cellular mechanism of how P140 interacts with the CMA process. MRL/lpr mice and CBA/J mice used as control received P140 or control peptides intravenously. Lysosome-enriched fractions of spleen or liver were prepared to examine lysosomal function. Highly purified lysosomes were further isolated and left to incubate with the CMA substrate to study at which cellular step P140 interacts with the CMA process. The data show that P140 effectively regulates CMA in vivo in MRL/lpr mice at the step of substrate lysosomal uptake and restores some alterations of defective lysosomes. For the first time, it is demonstrated that by occluding the intralysosome uptake of CMA substrates, a therapeutic molecule can attenuate excessive CMA activity in a pathological pro-inflammatory context and protect against hyperinflammation. This recovery effect of P140 on hyperactivated CMA is not only important for lupus therapy but potentially also for treating other (auto)inflammatory diseases, including neurologic and metabolic disorders, where CMA modulation would be highly beneficial.

Indexed as

AutophagyAnimalsChaperone-Mediated AutophagyLupus Erythematosus, SystemicLysosomal-Associated Membrane Protein 2LysosomesMice, Inbred CBAMice, Inbred MRL lprModels, BiologicalPeptide FragmentsPhosphopeptidesSpleenLysosomal-Associated Membrane Protein 2Peptide FragmentsPhosphopeptidesspliceosomal peptide P140chaperone-mediated autophagylupuslysosomesMRL/lpr miceP140 peptide

Identifiers

PMID33092174
PMCPMC7589999
OpenAlexW3093762832

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.