Evidence map›Paper›PMID 18096669›Full record

ArticleEndocrinology2008

The cell-specific pattern of cholecystokinin peptides in endocrine cells versus neurons is governed by the expression of prohormone convertases 1/3, 2, and 5/6.

Jens F Rehfeld, Jens R Bundgaard, Jens Hannibal, Xiaorong Zhu, Christina Norrbom, Donald F Steiner, Lennart Friis-Hansen

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Endocrinology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 31% 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

15 citing papers in PubMed, 48 citations in OpenAlex.

  1. Trial
  2. Review
  3. Cholecystokinin: Clinical aspects of the new biology.Journal of internal medicine · 2025
    Review
  4. Review
  5. Review
  6. Cholecystokinin and the hormone concept.Endocrine connections · 2021
    Review
  7. Premises for Cholecystokinin and Gastrin Peptides in Diabetes Therapy.Clinical medicine insights. Endocrinology and diabetes · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Peptide processing and biology in human disease.Current opinion in endocrinology, diabetes, and obesity · 2009
    Review
  15. Article
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 3 institutions in 2 countries.

Jens F RehfeldDepartment of Clinical Biochemistry, Rigshospitalet, Blegdamsvej 9, Copenhagen, Denmark. jens.f.rehfeld@rh.regionh.dk
Jens R Bundgaard
Jens Hannibal
Xiaorong Zhu
Christina Norrbom
Donald F Steiner
Lennart Friis-Hansen
University of Chicago · USUniversity of Copenhagen · DKRigshospitalet · DK

Funding

TRANSGENIC COREP60DK020595 · NIDDK · UNIVERSITY OF CHICAGO · PI BELL, GRAEME I · 1985 to 2012
$25.5M
Pilot and Feasibility ProgramP30DK020595 · NIDDK · UNIVERSITY OF CHICAGO · PI Matthew J Brady · 2013 to 2026
$20.9M
STUDIES ON PANCREATIC HORMONESR01DK013914 · NIDDK · UNIVERSITY OF CHICAGO · PI STEINER, DONALD F · 1986 to 2011
$5.5M
STUDIES ON PANCREATIC HORMONESR37DK013914 · NIDDK · UNIVERSITY OF CHICAGO · PI STEINER, DONALD F · 1990 to 1997
–
Howard Hughes Medical InstituteNIDDK NIH HHS DK 13914NIDDK NIH HHS DK 20595NIDDK NIH HHS P30 DK020595NIDDK NIH HHS P60 DK020595NIDDK NIH HHS R01 DK013914
6 · The paper itself

Abstract

Most peptide hormone genes are, in addition to endocrine cells, also expressed in neurons. The peptide hormone cholecystokinin (CCK) is expressed in different molecular forms in cerebral neurons and intestinal endocrine cells. To understand this difference, we examined the roles of the neuroendocrine prohormone convertases (PC) 1/3, PC2, and PC5/6 by measurement of proCCK, processing intermediates and bioactive, alpha-amidated, and O-sulfated CCK peptides in cerebral and jejunal extracts of null mice, controls, and in the PC5/6-expressing SK-N-MC cell-line. In PC1/3 null mice, the synthesis of bioactive CCK peptide in the gut was reduced to 3% of the translational product, all of which was in the form of alpha-amidated and tyrosine O-sulfated CCK-22, whereas the neuronal synthesis in the brain was largely unaffected. This is opposite to the PC2 null mice in which only the cerebral synthesis was affected. SK-N-MC cells, which express neither PC1/3 nor PC2, synthesized alone the processing intermediate, glycine-extended CCK-22. Immunocytochemistry confirmed that intestinal endocrine CCK cells in wild-type mice express PC1/3 but not PC2. In contrast, cerebral CCK neurons contain PC2 and only little, if any, PC1/3. Taken together, the data indicate that PC1/3 governs the endocrine and PC2 the neuronal processing of proCCK, whereas PC5/6 contributes only to a modest endocrine synthesis of CCK-22. The results suggest that the different peptide patterns in the brain and the gut are due to different expression of PCs.

Indexed as

AnimalsBrainCell Line, TumorCholecystokininEnteroendocrine CellsHumansMiceNeuronsOrgan SpecificityPeptide FragmentsProprotein Convertase 1Proprotein Convertase 2Proprotein Convertase 5Cholecystokinincholecystokinin 22 C-terminal fragmentPeptide FragmentsProprotein Convertase 1Proprotein Convertase 2Proprotein Convertase 5

Identifiers

PMID18096669
PMCPMC2734493
OpenAlexW2036077009

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.