Evidence map›Paper›PMID 17597519›Full record

ArticleBMC genomics2007

Identification and characterisation of the angiotensin converting enzyme-3 (ACE3) gene: a novel mammalian homologue of ACE.

Monika Rella, Joann L Elliot, Timothy J Revett, Jerry Lanfear, Anne Phelan, Richard M Jackson, Anthony J Turner, Nigel M Hooper

Open access · goldAbstract read
In one paragraph

Article in BMC genomics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Angiotensin-converting enzymes play a dominant role in fertility.International journal of molecular sciences · 2013
    Review
  7. Emergence and evolution of the renin-angiotensin-aldosterone system.Journal of molecular medicine (Berlin, Germany) · 2012
    Review
  8. Review
  9. Article
  10. Not just angiotensinases: new roles for the angiotensin-converting enzymes.Cellular and molecular life sciences : CMLS · 2010
    Review
  11. Review
  12. Review
  13. 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

8 authors at 2 institutions in 1 country.

Monika RellaInstitute of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK. monika.rella@qmail.com <monika.rella@qmail.com>
Joann L Elliot
Timothy J Revett
Jerry Lanfear
Anne Phelan
Richard M Jackson
Anthony J Turner
Nigel M Hooper
University of Leeds · GBPfizer (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMammalian angiotensin converting enzyme (ACE) plays a key role in blood pressure regulation. Although multiple ACE-like proteins exist in non-mammalian organisms, to date only one other ACE homologue, ACE2, has been identified in mammals.

resultsHere we report the identification and characterisation of the gene encoding a third homologue of ACE, termed ACE3, in several mammalian genomes. The ACE3 gene is located on the same chromosome downstream of the ACE gene. Multiple sequence alignment and molecular modelling have been employed to characterise the predicted ACE3 protein. In mouse, rat, cow and dog, the predicted protein has mutations in some of the critical residues involved in catalysis, including the catalytic Glu in the HEXXH zinc binding motif which is Gln, and ESTs or reverse-transcription PCR indicate that the gene is expressed. In humans, the predicted ACE3 protein has an intact HEXXH motif, but there are other deletions and insertions in the gene and no ESTs have been identified.

conclusionIn the genomes of several mammalian species there is a gene that encodes a novel, single domain ACE-like protein, ACE3. In mouse, rat, cow and dog ACE3, the catalytic Glu is replaced by Gln in the putative zinc binding motif, indicating that in these species ACE3 would lack catalytic activity as a zinc metalloprotease. In humans, no evidence was found that the ACE3 gene is expressed and the presence of deletions and insertions in the sequence indicate that ACE3 is a pseudogene.

Indexed as

Gene Expression ProfilingAmino Acid SequenceAnimalsCattleDogsExpressed Sequence TagsGenomicsHumansMetalloproteasesMiceMolecular Sequence DataPeptidyl-Dipeptidase ARatsSequence Homology, Amino AcidSpecies SpecificityAce3 protein, mouseMetalloproteasesPeptidyl-Dipeptidase A

Identifiers

PMID17597519
PMCPMC1925091
OpenAlexW2057760724

What OpenQuestion holds

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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.