Evidence map›Paper›PMID 32607937›Full record

ArticleCell stress & chaperones2020

Increased expression and retention of the secretory chaperone proSAAS following cell stress.

Manita Shakya, Taha Yildirim, Iris Lindberg

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Cell stress & chaperones, 2020. 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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 16 citations in OpenAlex.

  1. Review
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  9. Review
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  11. Article
  12. Secreted Chaperones in Neurodegeneration.Frontiers in aging neuroscience · 2020
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Manita ShakyaDepartment of Anatomy and Neurobiology, University of Maryland School of Medicine, 20 Penn St, HSF2, S267, Baltimore, MD, 21201, USA.
Taha YildirimDepartment of Anatomy and Neurobiology, University of Maryland School of Medicine, 20 Penn St, HSF2, S267, Baltimore, MD, 21201, USA.
Iris LindbergDepartment of Anatomy and Neurobiology, University of Maryland School of Medicine, 20 Penn St, HSF2, S267, Baltimore, MD, 21201, USA. ilindberg@som.umaryland.edu.ORCID http://orcid.org/0000-0002-1188-170X
University of Maryland, Baltimore · US

Funding

ProSAAS-mediated neuroprotective mechanisms in Alzheimer's and Parkinson's diseases: the role of secretory chaperones in neurodegenerationR01AG062222 · NIA · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS, MAIDMENT, NIGEL T · 2019 to 2023
$3.5M
Opioid Peptide Synthesizing EnzymesR01DA042351 · NIDA · UNIVERSITY OF MARYLAND BALTIMORE · PI LINDBERG, IRIS · 2017 to 2021
$2.0M
NIA NIH HHS R01 AG062222NIDA NIH HHS R01 DA042351
6 · The paper itself

Abstract

The secretory pathway of neurons and endocrine cells contains a variety of mechanisms designed to combat cellular stress. These include not only the unfolded protein response pathways but also diverse chaperone proteins that collectively work to ensure proteostatic control of secreted and membrane-bound molecules. One of the least studied of these chaperones is the neural- and endocrine-specific molecule known as proSAAS. This small chaperone protein acts as a potent anti-aggregant both in vitro and in cellulo and also represents a cerebrospinal fluid biomarker in Alzheimer's disease. In the present study, we have examined the idea that proSAAS, like other secretory chaperones, might represent a stress-responsive protein. We find that exposure of neural and endocrine cells to the cell stressors tunicamycin and thapsigargin increases cellular proSAAS mRNA and protein in Neuro2A cells. Paradoxically, proSAAS secretion is inhibited by these same drugs. Exposure of Neuro2A cells to low concentrations of the hypoxic stress inducer cobalt chloride, or to sodium arsenite, an oxidative stressor, also increases cellular proSAAS content and reduces its secretion. We conclude that the cellular levels of the small secretory chaperone proSAAS are positively modulated by cell stress.

Indexed as

Stress, PhysiologicalAnimalsArsenitesCell HypoxiaCell LineCobaltEndoplasmic Reticulum Chaperone BiPEndoplasmic Reticulum StressHeat-Shock ProteinsMiceMolecular ChaperonesNeuropeptidesOxidative StressProtective AgentsRatsRNA, MessengerArsenitesCobaltcobaltous chlorideEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMolecular ChaperonesNeuropeptidesPcsk1n protein, mouseProtective AgentsRNA, Messengersodium arseniteSodium CompoundsThapsigarginTunicamycinCell stressCell viabilityPCSK1NproSAASSecretory chaperones

Identifiers

PMID32607937
PMCPMC7591655
OpenAlexW3040443122

What OpenQuestion holds

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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.