Evidence map›Paper›PMID 20065150›Full record

ReviewHypertension (Dallas, Tex. : 1979)2010

Angiotensin I-converting enzyme inhibitors are allosteric enhancers of kinin B1 and B2 receptor function.

Ervin G Erdös, Fulong Tan, Randal A Skidgel

Open access · bronzeAbstract readReview
In one paragraph

Review in Hypertension (Dallas, Tex. : 1979), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 131 citations in OpenAlex.

  1. Trial
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  4. Article
  5. Article
  6. Endothelial Function Biomarkers in Hypertension.Current medicinal chemistry · 2025
    Review
  7. Immune and Metabolic Mechanisms of Endothelial Dysfunction.International journal of molecular sciences · 2024
    Review
  8. Review
  9. Review
  10. Article
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  12. Article
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  14. Observational
  15. Review
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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

3 authors at 1 institution in 1 country.

Ervin G ErdösDepartment of Pharmacology, University of Illinois College of Medicine, Chicago, Ill 60612, USA. egerdos@uic.edu
Fulong Tan
Randal A Skidgel
Illinois College · US

Funding

TRPC6 Regulation of Lung Endothelial Barrier FunctionP01HL060678 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI MALIK, ASRAR B. · 2000 to 2020
$40.1M
STRUCTURE/FUNCTION OF CARBOXYPEPTIDASESR01DK041431 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SKIDGEL, RANDAL A · 1995 to 2013
$3.7M
VASOACTIVE PEPTIDES WHICH STIMULATE SMOOTH MUSCLESR01HL036473 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI ERDOS, ERVIN G, SKIDGEL, RANDAL A · 1985 to 2010
$3.4M
Structure and Function of CarboxypeptidasesR56DK041431 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SKIDGEL, RANDAL A · 2010 to 2010
$236k
STRUCTURE AND FUNCTION OF CARBOXYPEPTIDASE MR29DK041431 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SKIDGEL, RANDAL A · 1989 to 1993
–
VASOACTIVE PEPTIDES WHICH STIMULATE SMOOTH MUSCLESR37HL036473 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI ERDOS, ERVIN G · 1988 to 1997
–
NHLBI NIH HHS HL36473NHLBI NIH HHS HL60678NHLBI NIH HHS P01 HL060678NHLBI NIH HHS R01 HL036473NIDDK NIH HHS DK 41431NIDDK NIH HHS R01 DK041431NIDDK NIH HHS R56 DK041431
6 · The paper itself

Abstract

The beneficial effects of angiotensin I-converting enzyme (ACE) inhibitors go beyond the inhibition of ACE to decrease angiotensin (Ang) II or increase kinin levels. ACE inhibitors also affect kinin B1 and B2 receptor (B1R and B2R) signaling, which may underlie some of their therapeutic usefulness. They can indirectly potentiate the actions of bradykinin (BK) and ACE-resistant BK analogs on B2Rs to elevate arachidonic acid and NO release in laboratory experiments. Studies indicate that ACE inhibitors and some Ang metabolites increase B2R functions as allosteric enhancers by inducing a conformational change in ACE. This is transmitted to B2Rs via heterodimerization with ACE on the plasma membrane of cells. ACE inhibitors are also agonists of the B1R, at a Zn-binding sequence on the second extracellular loop that differs from the orthosteric binding site of the des-Arg-kinin peptide ligands. Thus, ACE inhibitors act as direct allosteric B1R agonists. When ACE inhibitors enhance B2R and B1R signaling, they augment NO production. Enhancement of B2R signaling activates endothelial NO synthase, yielding a short burst of NO; activation of B1Rs results in a prolonged high output of NO by inducible NO synthase. These actions, outside inhibiting peptide hydrolysis, may contribute to the pleiotropic therapeutic effects of ACE inhibitors in various cardiovascular disorders.

Indexed as

Allosteric RegulationAngiotensin-Converting Enzyme InhibitorsAnimalsEndothelium, VascularFemaleHumansHypertensionMaleNitric Oxide SynthaseProtein TransportReceptor, Bradykinin B1Receptor, Bradykinin B2Sensitivity and SpecificitySignal TransductionAngiotensin-Converting Enzyme InhibitorsNitric Oxide SynthaseReceptor, Bradykinin B1Receptor, Bradykinin B2

Identifiers

PMID20065150
PMCPMC2814794
OpenAlexW2161832913

What OpenQuestion holds

Textmetadata
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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.