Evidence map›Paper›PMID 19968759›Full record

ArticleJournal of neurochemistry2010

Neuropeptidomic analysis establishes a major role for prohormone convertase-2 in neuropeptide biosynthesis.

Xin Zhang, Hui Pan, Bonnie Peng, Donald F Steiner, John E Pintar, Lloyd D Fricker

Open access · bronzeAbstract read
In one paragraph

Article in Journal of neurochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
3.3field-weighted citation impact, top 8% 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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 75 citations in OpenAlex.

  1. Limitations of Mass Spectrometry-Based Peptidomic Approaches.Journal of the American Society for Mass Spectrometry · 2015
    Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Quantitative Peptidomics: General Considerations.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Article
  9. Article
  10. Molecular pharmacology · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
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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

6 authors at 3 institutions in 1 country.

Xin ZhangDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Hui Pan
Bonnie Peng
Donald F Steiner
John E Pintar
Lloyd D Fricker
Albert Einstein College of Medicine · USRutgers, The State University of New Jersey · USUniversity of Chicago · US

Funding

REGULATION OF ENKEPHALIN CONVERTASE--CARBOXYPEPTIDASE ER01DA004494 · NIDA · YESHIVA UNIVERSITY · PI FRICKER, LLOYD D · 1987 to 2015
$5.9M
STUDIES ON PANCREATIC HORMONESR01DK013914 · NIDDK · UNIVERSITY OF CHICAGO · PI STEINER, DONALD F · 1986 to 2011
$5.5M
STRUCTURE/FUNCTION OF CARBOXYPEPTIDASE DR01DK051271 · NIDDK · YESHIVA UNIVERSITY · PI FRICKER, LLOYD D · 1996 to 2008
$2.7M
Gene array analysis of opioid system mutant miceR01DA015237 · NIDA · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI PINTAR, JOHN E · 2002 to 2005
$1.1M
STUDIES ON PANCREATIC HORMONESR37DK013914 · NIDDK · UNIVERSITY OF CHICAGO · PI STEINER, DONALD F · 1990 to 1997
–
NIDA NIH HHS DA015237NIDA NIH HHS DA04494NIDA NIH HHS R01 DA004494NIDA NIH HHS R01 DA015237NIDDK NIH HHS DK13914NIDDK NIH HHS DK51271NIDDK NIH HHS R01 DK013914NIDDK NIH HHS R01 DK051271
6 · The paper itself

Abstract

Prohormone convertase 2 (PC2) functions in the generation of neuropeptides from their precursors. A quantitative peptidomics approach was used to evaluate the role of PC2 in the processing of peptides in a variety of brain regions. Altogether, 115 neuropeptides or other peptides derived from secretory pathway proteins were identified. These peptides arise from 28 distinct secretory pathway proteins, including proenkephalin, proopiomelanocortin, prodynorphin, protachykinin A and B, procholecystokinin, and many others. Forty one of the peptides found in wild-type (WT) mice were not detectable in any of the brain regions of PC2 knockout mice, and another 24 peptides were present at levels ranging from 20% to 79% of WT levels. Most of the other peptides were not substantially affected by the mutation, with levels ranging from 80% to 120% of WT levels, and only three peptides were found to increase in one or more brain regions of PC2 knockout mice. Taken together, these results are consistent with a broad role for PC2 in neuropeptide processing, but with functional redundancy for many of the cleavages. Comparison of the cleavage sites affected by the absence of PC2 confirms previous suggestions that sequences with a Trp, Tyr, and/or Pro in the P1' or P2' position are preferentially cleaved by PC2 and not by other enzymes present in the secretory pathway.

Indexed as

Amino Acid SequenceAnimalsBrainChromatography, High Pressure LiquidMiceMice, KnockoutNeuropeptidesProprotein Convertase 2ProteomicsSpectrometry, Mass, Electrospray IonizationNeuropeptidesProprotein Convertase 2

Identifiers

PMID19968759
PMCPMC2901178
OpenAlexW1990815716

What OpenQuestion holds

Textmetadata
LicenceTDM
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.