Evidence map›Paper›PMID 19620246›Full record

ArticleThe Journal of biological chemistry2009

Kinetic study of neuropeptide Y (NPY) proteolysis in blood and identification of NPY3-35: a new peptide generated by plasma kallikrein.

Karim Abid, Bertrand Rochat, Paul-Gerhard Lassahn, Reto Stöcklin, Sophie Michalet, Noureddine Brakch, Jean-Francois Aubert, Bilgin Vatansever, Patricia Tella, Ingrid De Meester and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

28 citing papers in PubMed, 65 citations in OpenAlex.

  1. In vivo and in vitro degradation of peptide YY3-36 to inactive peptide YY3-34 in humans.American journal of physiology. Regulatory, integrative and comparative physiology · 2016
    Trial
  2. Review
  3. Article
  4. Article
  5. Topical Neuropeptide Y for Ischemic Skin Wounds.International journal of molecular sciences · 2024
    Article
  6. Article
  7. Article
  8. The identification of two M20B family peptidases required for full virulence inFrontiers in cellular and infection microbiology · 2023
    Article
  9. Article
  10. Biomarkers and Detection Platforms for Human Health and Performance Monitoring: A Review.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. NPY and Gene Therapy for Epilepsy: How, When,... and Y.Frontiers in molecular neuroscience · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

11 authors at 4 institutions in 2 countries.

Karim AbidDivision of Clinical Pharmacology and Toxicology, Centre Hospitalier Universitaire Vaudois (CHUV), 1011 Lausanne, Switzerland.
Bertrand Rochat
Paul-Gerhard Lassahn
Reto Stöcklin
Sophie Michalet
Noureddine Brakch
Jean-Francois Aubert
Bilgin Vatansever
Patricia Tella
Ingrid De Meester
Eric Grouzmann
University Hospital of Lausanne · CHAtheris Laboratories (Switzerland) · CHThermo Fisher Scientific (Switzerland) · CHUniversity of Antwerp · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is little information on how neuropeptide Y (NPY) proteolysis by peptidases occurs in serum, in part because reliable techniques are lacking to distinguish different NPY immunoreactive forms and also because the factors affecting the expression of these enzymes have been poorly studied. In the present study, LC-MS/MS was used to identify and quantify NPY fragments resulting from peptidolytic cleavage of NPY(1-36) upon incubation with human serum. Kinetic studies indicated that NPY(1-36) is rapidly cleaved in serum into 3 main fragments with the following order of efficacy: NPY(3-36) >> NPY(3-35) > NPY(2-36). Trace amounts of additional NPY forms were identified by accurate mass spectrometry. Specific inhibitors of dipeptidyl peptidase IV, kallikrein, and aminopeptidase P prevented the production of NPY(3-36), NPY(3-35), and NPY(2-36), respectively. Plasma kallikrein at physiological concentrations converted NPY(3-36) into NPY(3-35). Receptor binding assays revealed that NPY(3-35) is unable to bind to NPY Y1, Y2, and Y5 receptors; thus NPY(3-35) may represent the major metabolic clearance product of the Y2/Y5 agonist, NPY(3-36).

Indexed as

AdamantaneAdultChromatography, LiquidFemaleHumansKineticsMaleMass SpectrometryNeuropeptide YNitrilesPeptide FragmentsPeptidesPlasma KallikreinProtease InhibitorsProtein Structure, TertiaryPyrrolidinesAdamantaneapstatinNeuropeptide Yneuropeptide Y (3-35)NitrilesPeptide FragmentsPeptidesPlasma KallikreinProtease InhibitorsPyrrolidinesVildagliptin

Identifiers

PMID19620246
PMCPMC2757175
OpenAlexW2100790556

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.