Evidence map›Paper›PMID 25592215›Full record

ReviewNeuropharmacology2015

ASICs and neuropeptides.

Jonathan S Vick, Candice C Askwith

Abstract readReview
In one paragraph

Review in Neuropharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.

  1. A review of the kappa opioid receptor system in opioid use.Neuroscience and biobehavioral reviews · 2024
    Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Acid-Sensing Ion Channels and Mechanosensation.International journal of molecular sciences · 2021
    Review
  8. Changes in HFrontiers in cellular neuroscience · 2021
    Article
  9. Article
  10. Monoclonal antibody as an emerging therapy for acute ischemic stroke.International journal of physiology, pathophysiology and pharmacology · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Selection of an ASIC1a-blocking combinatorial antibody that protects cells from ischemic death.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Article
  18. Review
  19. The NovelJDR clinical and translational research · 2016
    Article
  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

2 authors at 1 institution in 1 country.

Jonathan S VickThe Department of Neuroscience, The Ohio State University Wexner Medical Center, United States.
Candice C AskwithThe Department of Neuroscience, The Ohio State University Wexner Medical Center, United States. Electronic address: askwith.1@osu.edu.
The Ohio State University Wexner Medical Center · US

Funding

Ohio State Neuroscience Centr CoreP30NS045758 · NINDS · OHIO STATE UNIVERSITY · PI MCTIGUE, DANA M · 2004 to 2015
$7.7M
Neuropeptide Modulation of ASICsR01NS062967 · NINDS · OHIO STATE UNIVERSITY · PI ASKWITH, CANDICE C · 2008 to 2012
$1.3M
NINDS NIH HHS P30 NS045758NINDS NIH HHS R01 NS062967
6 · The paper itself

Abstract

The acid sensing ion channels (ASICs) are proton-gated cation channels expressed throughout the nervous system. ASICs are activated during acidic pH fluctuations, and recent work suggests that they are involved in excitatory synaptic transmission. ASICs can also induce neuronal degeneration and death during pathological extracellular acidosis caused by ischemia, autoimmune inflammation, and traumatic injury. Many endogenous neuromodulators target ASICs to affect their biophysical characteristics and contributions to neuronal activity. One of the most unconventional types of modulation occurs with the interaction of ASICs and neuropeptides. Collectively, FMRFamide-related peptides and dynorphins potentiate ASIC activity by decreasing the proton-sensitivity of steady state desensitization independent of G protein-coupled receptor activation. By decreasing the proton-sensitivity of steady state desensitization, the FMRFamide-related peptides and dynorphins permit ASICs to remain active at more acidic basal pH. Unlike the dynorphins, some FMRFamide-related peptides also potentiate ASIC activity by slowing inactivation and increasing the sustained current. Through mechanistic studies, the modulation of ASICs by FMRFamide-related peptides and dynorphins appears to be through distinct interactions with the extracellular domain of ASICs. Dynorphins are expressed throughout the nervous system and can increase neuronal death during prolonged extracellular acidosis, suggesting that the interaction between dynorphins and ASICs may have important consequences for the prevention of neurological injury. The overlap in expression of FMRFamide-related peptides with ASICs in the dorsal horn of the spinal cord suggests that their interaction may have important consequences for the treatment of pain during injury and inflammation. This article is part of the Special Issue entitled 'Acid-Sensing Ion Channels in the Nervous System'.

Indexed as

Acid Sensing Ion ChannelsAnimalsHumansNeurodegenerative DiseasesNeuronsNeuropeptidesAcid Sensing Ion ChannelsNeuropeptidesAcid sensing ion channelASICDynorphinFMRFamideNeuropeptideSteady state desensitization

Identifiers

PMID25592215
PMCPMC4458394
OpenAlexW2078428052

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.