Evidence map›Paper›PMID 28378780›Full record

ArticleScientific reports2017

A Fluorometric Method of Measuring Carboxypeptidase Activities for Angiotensin II and Apelin-13.

Pan Liu, Jan Wysocki, Peter Serfozo, Minghao Ye, Tomokazu Souma, Daniel Batlle, Jing Jin

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
1.9field-weighted citation impact, top 16% 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, 29 citations in OpenAlex.

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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

7 authors at 2 institutions in 1 country.

Pan LiuDivision of Nephrology and Hypertension; The Center for Kidney Research and Therapeutics at the Feinberg Cardiovascular Research Institute, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Jan WysockiDivision of Nephrology and Hypertension; The Center for Kidney Research and Therapeutics at the Feinberg Cardiovascular Research Institute, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Peter SerfozoDivision of Nephrology and Hypertension; The Center for Kidney Research and Therapeutics at the Feinberg Cardiovascular Research Institute, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Minghao YeDivision of Nephrology and Hypertension; The Center for Kidney Research and Therapeutics at the Feinberg Cardiovascular Research Institute, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Tomokazu SoumaDivision of Nephrology and Hypertension; The Center for Kidney Research and Therapeutics at the Feinberg Cardiovascular Research Institute, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Daniel BatlleDivision of Nephrology and Hypertension; The Center for Kidney Research and Therapeutics at the Feinberg Cardiovascular Research Institute, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Jing JinDivision of Nephrology and Hypertension; The Center for Kidney Research and Therapeutics at the Feinberg Cardiovascular Research Institute, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Northwestern University · USHypertension Institute · US

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 R01 DK080089
6 · The paper itself

Abstract

Degradation of the biologically potent octapeptide angiotensin Ang II-(1-8) is mediated by the activities of several peptidases. The conversion of Ang II to the septapeptide Ang-(1-7) is of particular interest as the latter also confers organ protection. The conversion is catalyzed by angiotensin-converting enzyme 2 and other enzymes that selectively cleave the peptide bond between the proline and the phenylalanine at the carboxyl terminus of Ang II. The contribution of various enzyme activities that collectively lead to the formation of Ang-(1-7) from Ang II, in both normal conditions and in disease states, remains only partially understood. This is largely due to the lack of a reliable and sensitive method to detect these converting activities in complex samples, such as blood and tissues. Here, we report a fluorometric method to measure carboxypeptidase activities that cleave the proline-phenylalanine dipeptide bond in Ang II. This method is also suitable for measuring the conversion of apelin-13. The assay detects the release of phenylalanine amino acid in a reaction with the yeast enzyme of phenylalanine ammonia lyase (PAL). When used in cell and mouse organs, the assay can robustly measure endogenous Ang II and apelin-13-converting activities involved in the renin-angiotensin and the apelinergic systems, respectively.

Indexed as

FluorometryAmino Acid SequenceAngiotensin-Converting Enzyme 2Angiotensin IAngiotensin IIAnimalsCarboxypeptidasesHEK293 CellsHumansImmunoassayIntercellular Signaling Peptides and ProteinsKidneyMicePeptide FragmentsPeptidyl-Dipeptidase APhenylalanineACE2 protein, humanAce2 protein, mouseAngiotensin-Converting Enzyme 2Angiotensin Iangiotensin I (1-7)Angiotensin IIapelin-13 peptideCarboxypeptidasesIntercellular Signaling Peptides and ProteinsPeptide FragmentsPeptidyl-Dipeptidase APhenylalanine

Identifiers

PMID28378780
PMCPMC5381230
OpenAlexW2604152065

What OpenQuestion holds

Textmetadata
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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.