Evidence map›Paper›PMID 9990065›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Prototypic G protein-coupled receptor for the intestinotrophic factor glucagon-like peptide 2.

D G Munroe, A K Gupta, F Kooshesh, T B Vyas, G Rizkalla, H Wang, L Demchyshyn, Z J Yang, R K Kamboj, H Chen and 4 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
14.1field-weighted citation impact, top 1% 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

75 citing papers in PubMed, 325 citations in OpenAlex.

  1. Review
  2. Article
  3. Class B1 GPCRs: insights into multireceptor pharmacology for the treatment of metabolic disease.American journal of physiology. Endocrinology and metabolism · 2024
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Glucagon and Its Receptors in the Mammalian Heart.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Proglucagon-Derived Peptides as Therapeutics.Frontiers in endocrinology · 2021
    Review
  19. Review
  20. Article

15 more citing papers are in PubMed but not listed here.

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

14 authors at 1 institution in 1 country.

D G MunroeAllelix Biopharmaceuticals Inc., 6850 Goreway Drive, Mississauga, Ontario L4V 1V7, Canada. dmunroe@allelix.com
A K Gupta
F Kooshesh
T B Vyas
G Rizkalla
H Wang
L Demchyshyn
Z J Yang
R K Kamboj
H Chen
K McCallum
M Sumner-Smith
D J Drucker
A Crivici
University of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucagon-like peptide 2 (GLP-2) is a 33-aa proglucagon-derived peptide produced by intestinal enteroendocrine cells. GLP-2 stimulates intestinal growth and up-regulates villus height in the small intestine, concomitant with increased crypt cell proliferation and decreased enterocyte apoptosis. Moreover, GLP-2 prevents intestinal hypoplasia resulting from total parenteral nutrition. However, the mechanism underlying these actions has remained unclear. Here we report the cloning and characterization of cDNAs encoding rat and human GLP-2 receptors (GLP-2R), a G protein-coupled receptor superfamily member expressed in the gut and closely related to the glucagon and GLP-1 receptors. The human GLP-2R gene maps to chromosome 17p13.3. Cells expressing the GLP-2R responded to GLP-2, but not GLP-1 or related peptides, with increased cAMP production (EC50 = 0.58 nM) and displayed saturable high-affinity radioligand binding (Kd = 0.57 nM), which could be displaced by synthetic rat GLP-2 (Ki = 0.06 nM). GLP-2 analogs that activated GLP-2R signal transduction in vitro displayed intestinotrophic activity in vivo. These results strongly suggest that GLP-2, like glucagon and GLP-1, exerts its actions through a distinct and specific novel receptor expressed in its principal target tissue, the gastrointestinal tract.

Indexed as

Amino Acid SequenceAnimalsBrainCloning, MolecularCOS CellsCyclic AMPGene LibraryGlucagon-Like Peptide 1Glucagon-Like Peptide-1 ReceptorGlucagon-Like Peptide 2GTP-Binding ProteinsHumansIntestinal MucosaKineticsMolecular Sequence DataOrgan SpecificityCyclic AMPGLP1R protein, humanGlp1r protein, ratGlucagon-Like Peptide 1Glucagon-Like Peptide-1 ReceptorGlucagon-Like Peptide 2GTP-Binding ProteinsPeptide FragmentsPeptidesReceptors, Glucagon

Identifiers

PMID9990065
PMCPMC15520
OpenAlexW2138867063

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.