Evidence map›Paper›PMID 25968123›Full record

ArticleAmerican journal of hypertension2015

Plasma and Kidney Angiotensin Peptides: Importance of the Aminopeptidase A/Angiotensin III Axis.

Jan Wysocki, Minghao Ye, Daniel Batlle

Abstract read
In one paragraph

Article in American journal of hypertension, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–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

19 citing papers in PubMed.

  1. Article
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  5. Review
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  8. A pressor dose of angiotensin II has no influence on the angiotensin-converting enzyme 2 and other molecules associated with SARS-CoV-2 infection in mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  9. Article
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  11. Article
  12. Review
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  15. Article
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  17. Article
  18. Reply to "Letter to the editor: Angiotensin quantification by mass spectrometry".American journal of physiology. Heart and circulatory physiology · 2016
    Article
  19. Biochemical evaluation of the renin-angiotensin system: the good, bad, and absolute?American journal of physiology. Heart and circulatory physiology · 2016
    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

3 authors.

Jan WysockiDivision of Nephrology & Hypertension, Department of Medicine, The Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.
Minghao YeDivision of Nephrology & Hypertension, Department of Medicine, The Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.
Daniel BatlleDivision of Nephrology & Hypertension, Department of Medicine, The Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA. d-batlle@northwestern.edu.

Funding

Strategies for ACE2 Amplification to Treat Diabetic Kidney DiseaseR01DK080089 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BATLLE, DANIEL · 2009 to 2012
$1.3M
NIDDK NIH HHS 1R01DK080089-01A2NIDDK NIH HHS R01 DK080089
6 · The paper itself

Abstract

backgroundThe renin-angiotensin system is a complex regulatory hormonal network with a main biological peptide and therapeutic target, angiotensin (Ang) II (1-8). There are other potentially important Ang peptides that have not been well evaluated.

methodsLiquid chromatography-tandem mass spectrometry (LC-MS/MS) was used for concurrent evaluation of multiple Angs downstream of Ang I (1-10) and Ang II (1-8) in kidney and plasma from wild-type (WT) mice. Angiotensin converting enzyme 2 knockout (ACE2KO) was also used as a way to examine the Angs profile in the absence of ACE2, an enzyme that cleaves both Ang I (1-10) and Ang II (1-8).

resultsIn plasma from both WT and ACE2KO, levels of Ang I (1-10), Ang III (2-8), and Ang (2-10) were the highest of all the renin-angiotensin system (RAS) peptides. The latter two peptides are products of aminopeptidase A cleavage of Ang II (1-8) and Ang I (1-10), respectively. In contrast, plasma levels of Ang II (1-8), and Ang (1-7), the product of Ang II (1-8) cleavage by ACE2, were low. In kidney from both WT and ACE2KO, Ang II (1-8) levels were high as compared to plasma levels. In the ACE2KO mice, a significant increase in either Ang II (1-8) or a decrease in Ang (1-7) was not observed in plasma or in the kidney.

conclusionRAS-focused peptidomic approach revealed major differences in Ang peptides between mouse plasma and kidney. These Ang peptide profiles show the dominance of the aminopeptidase A/Ang (2-10) and aminopeptidase A/Ang III (2-8) pathways in the metabolism of Ang I (1-10) and Ang II (1-8) over the ACE2/Ang (1-7) axis. Ang III (2-8) and other peptides formed from aminopeptidase A cleavage may be important therapeutic RAS targets.

Indexed as

Renin-Angiotensin SystemAngiotensin-Converting Enzyme 2AngiotensinsAnimalsFemaleGlutamyl AminopeptidaseKidneyMaleMice, Inbred C57BLMice, KnockoutPeptidyl-Dipeptidase AAce2 protein, mouseAngiotensin-Converting Enzyme 2AngiotensinsGlutamyl AminopeptidasePeptidyl-Dipeptidase AACE2aminopeptidase Aangiotensin (1–7); blood pressure; hypertension.angiotensin IIangiotensin III

Identifiers

PMID25968123
PMCPMC4757941

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Registered trials

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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.