Evidence map›Paper›PMID 22215671›Full record

ArticleThe Journal of biological chemistry2012

AMP is an adenosine A1 receptor agonist.

Joseph E Rittiner, Ilia Korboukh, Emily A Hull-Ryde, Jian Jin, William P Janzen, Stephen V Frye, Mark J Zylka

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
13.1field-weighted citation impact, top 1% 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

79 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. AMetabolites · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Extracellular AMP Inhibits Pollen Tube Growth inPlants (Basel, Switzerland) · 2024
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
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  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

19 more citing papers are in PubMed but not listed here.

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

7 authors at 1 institution in 1 country.

Joseph E RittinerDepartment of Cell and Molecular Physiology, University of North Carolina Neuroscience Center, Chapel Hill, North Carolina 27599, USA.
Ilia Korboukh
Emily A Hull-Ryde
Jian Jin
William P Janzen
Stephen V Frye
Mark J Zylka
University of North Carolina at Chapel Hill · US

Funding

Harnessing ectonucleotidases to treat chronic painR01NS067688 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZYLKA, MARK J. · 2009 to 2013
$3.6M
Biochemical Modulation of Nociceptive CircuitsR01NS060725 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZYLKA, MARK J. · 2007 to 2010
$1.3M
NINDS NIH HHS R01 NS060725NINDS NIH HHS R01NS060725NINDS NIH HHS R01 NS067688NINDS NIH HHS R01NS067688
6 · The paper itself

Abstract

Numerous receptors for ATP, ADP, and adenosine exist; however, it is currently unknown whether a receptor for the related nucleotide adenosine 5'-monophosphate (AMP) exists. Using a novel cell-based assay to visualize adenosine receptor activation in real time, we found that AMP and a non-hydrolyzable AMP analog (deoxyadenosine 5'-monophosphonate, ACP) directly activated the adenosine A(1) receptor (A(1)R). In contrast, AMP only activated the adenosine A(2B) receptor (A(2B)R) after hydrolysis to adenosine by ecto-5'-nucleotidase (NT5E, CD73) or prostatic acid phosphatase (PAP, ACPP). Adenosine and AMP were equipotent human A(1)R agonists in our real-time assay and in a cAMP accumulation assay. ACP also depressed cAMP levels in mouse cortical neurons through activation of endogenous A(1)R. Non-selective purinergic receptor antagonists (pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid and suramin) did not block adenosine- or AMP-evoked activation. Moreover, mutation of His-251 in the human A(1)R ligand binding pocket reduced AMP potency without affecting adenosine potency. In contrast, mutation of a different binding pocket residue (His-278) eliminated responses to AMP and to adenosine. Taken together, our study indicates that the physiologically relevant nucleotide AMP is a full agonist of A(1)R. In addition, our study suggests that some of the physiological effects of AMP may be direct, and not indirect through ectonucleotidases that hydrolyze this nucleotide to adenosine.

Indexed as

5'-NucleotidaseAdenosineAdenosine A1 Receptor AgonistsAdenosine MonophosphateAnimalsCerebral CortexColforsinHEK293 CellsHistidineHumansHydrolysisLigandsMiceMolecular ImagingNeuronsReceptor, Adenosine A15'-NucleotidaseAdenosineAdenosine A1 Receptor AgonistsAdenosine MonophosphateColforsinHistidineLigandsReceptor, Adenosine A1Receptor, Adenosine A2BReceptors, Purinergic P2YRecombinant Fusion Proteins

Identifiers

PMID22215671
PMCPMC3285310
OpenAlexW2063272225

What OpenQuestion holds

Textmetadata
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.