Evidence map›Paper›PMID 22842724›Full record

ArticleNaunyn-Schmiedeberg's archives of pharmacology2012

Evaluation of antibodies directed against human protease-activated receptor-2.

Mark N Adams, Charles N Pagel, Eleanor J Mackie, John D Hooper

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Naunyn-Schmiedeberg's archives of pharmacology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

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

  1. Pooled it
  2. Review
  3. Review
  4. PAR-2-activated secretion by airway gland serous cells: role for CFTR and inhibition byAmerican journal of physiology. Lung cellular and molecular physiology · 2021
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  15. Lack of specificity shown by P2Y6 receptor antibodies.Naunyn-Schmiedeberg's archives of pharmacology · 2013
    Article
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  17. 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.

Mark N AdamsMater Medical Research Institute, Aubigny Place, Raymond Terrace, South Brisbane, QLD, 4101, Australia.
Charles N Pagel
Eleanor J Mackie
John D Hooper
Mater Research · AUUniversity of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protease-activated receptor 2 (PAR2) is a G protein-coupled receptor activated by intramolecular docking of a tethered ligand that is released by the actions of proteases, mainly of the serine protease family. Here, we evaluate four commercially available anti-PAR2 antibodies, SAM11, C17, N19 and H99, demonstrating marked differences in the ability of these reagents to detect the target receptor in Western blot, immunocytochemical and flow cytometry applications. In Western blot analysis, we evaluated antibody reactivity against both ectopic and endogenous receptors. Against material from transfected cells, we show that SAM11 and N19, and to a lesser extent C17, but not H99, are able to detect ectopic PAR2. Interestingly, these Western blot analyses indicate that N19 and C17 detect conformations of ectopic PAR2 distinct to those recognised by SAM11. Significantly, our data also indicate that Western blot signal detected by SAM11 and C17, and much of the signal detected by N19, against cells endogenously expressing PAR2 is non-specific. Despite confounding non-specific signals, we were able to discern N19 reactivity against endogenous PAR2 as a broad smear that we also observed in ectopically expressing human and mouse cells and that is sensitive to loss of N-glycosylation. In immunocytochemistry analysis, each antibody is able to detect ectopic PAR2 although it appears that H99 detects only a subset of the ectopically expressed receptor. In addition, SAM11 and N19 are able to detect both ectopic and endogenous cell surface PAR2 by flow cytometry. In summary: (1) each antibody can detect ectopic PAR2 by immunocytochemical analysis with SAM11 and N19 suitable for cell surface detection of both ectopic and endogenous receptor by flow cytometry; (2) in Western blot analysis, N19, SAM11 and C17 can detect ectopically expressed PAR2, with only N19 able to detect the endogenous receptor by this technique and (3) in each of these approaches, appropriate controls are essential to ensure that non-specific reactivity is identified.

Indexed as

Antibody SpecificityAnimalsAntibodiesBlotting, WesternCHO CellsCricetinaeCricetulusFlow CytometryHumansImmunohistochemistryMiceMice, KnockoutReceptor, PAR-2TransfectionAntibodiesReceptor, PAR-2

Identifiers

PMID22842724
OpenAlexW2074870493

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.