Evidence map›Paper›PMID 18223027›Full record

ArticleExperimental physiology2008

Angiotensin-converting enzyme 2 catalytic activity in human plasma is masked by an endogenous inhibitor.

Rebecca A Lew, Fiona J Warner, Iresha Hanchapola, Michael A Yarski, Jay Ramchand, Jay Manohar, Louise M Burrell, A Ian Smith

Erratum issuedAbstract read
In one paragraph

Article in Experimental physiology, 2008. 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 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

69 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. A pilot study to assess the circulating renin-angiotensin system in COVID-19 acute respiratory failure.American journal of physiology. Lung cellular and molecular physiology · 2021
    Trial
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Observational
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
    Corrigendum.2015 · Manohar, Jay [corrected to Ramchand, Jay]
5 · Who and what money

Authors and funding

8 authors.

Rebecca A LewDepartment of Biochemistry & Molecular Biology, PO Box 13D, Monash University, Clayton, Victoria 3800, Australia.
Fiona J Warner
Iresha Hanchapola
Michael A Yarski
Jay Ramchand
Jay Manohar
Louise M Burrell
A Ian Smith

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiotensin-converting enzyme 2 (ACE2) is thought to act in an opposing manner to its homologue, angiotensin-converting enzyme (ACE), by inactivating the vasoconstrictor peptide angiotensin II and generating the vasodilatory fragment, angiotensin(1-7). Both ACE and ACE2 are membrane-bound ectoenzymes and may circulate in plasma as a consequence of a proteolytic shedding event. In this study, we show that ACE2 circulates in human plasma, but its activity is suppressed by the presence of an endogenous inhibitor. Partial purification of this inhibitor indicated that the inhibitor is small, hydrophilic and cationic, but not a divalent metal cation. These observations led us to develop a method for removal of the inhibitor, thus allowing detection of plasma ACE2 levels using a sensitive quenched fluorescent substrate-based assay. Using this technique, ACE2 activity measured in plasma from healthy volunteers (n = 18) ranged from 1.31 to 8.69 pmol substrate cleaved min-1 ml-1 (mean +/- s.e.m., 4.44 +/- 0.56 pmol min-1 ml-1). Future studies of patients with cardiovascular, renal and liver disease will determine whether plasma ACE2 is elevated in parallel with increased tissue levels observed in these conditions.

Indexed as

AcetonitrilesAdultAngiotensin-Converting Enzyme 2Angiotensin-Converting Enzyme InhibitorsAngiotensin IAngiotensin IIAntiportersBlotting, WesternCations, DivalentChelating AgentsFemaleHumansImmunoprecipitationMaleMiddle AgedPeptide FragmentsACE2 protein, humanacetonitrileAcetonitrilesAngiotensin-Converting Enzyme 2Angiotensin-Converting Enzyme InhibitorsAngiotensin Iangiotensin I (1-7)Angiotensin IIAntiportersCations, DivalentChelating AgentsPeptide FragmentsPeptidyl-Dipeptidase ARecombinant Proteins

Identifiers

PMID18223027
PMCPMC7197901

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.