Evidence map›Paper›PMID 17065399›Full record

ArticleThe Journal of endocrinology2006

Meat hydrolysate and essential amino acid-induced glucagon-like peptide-1 secretion, in the human NCI-H716 enteroendocrine cell line, is regulated by extracellular signal-regulated kinase1/2 and p38 mitogen-activated protein kinases.

Raylene A Reimer

Abstract read
In one paragraph

Article in The Journal of endocrinology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

39 citing papers in PubMed, 110 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Molecular Mechanisms and Antidiabetic Effects of Mango (International journal of molecular sciences · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
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  12. Review
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  14. Article
  15. Glucagon-like peptide 1 (GLP-1).Molecular metabolism · 2019 · on this map
    Review
  16. Article
  17. Article
  18. Article
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  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

1 author at 1 institution in 1 country.

Raylene A ReimerDepartment of Biochemistry and Molecular Biology, Faculties of Kinesiology and Medicine, University of Calgary, 2500 University Drive NW, Calgary, AB T2N 1N4 Canada. reimer@ucalgary.ca
University of Calgary · CA

Funding

CIHR 67027-1
6 · The paper itself

Abstract

Glucagon-like peptide-1 (GLP-1) is a potent insulin secretagogue released from L-cells in the intestine. Meat hydrolysate (MH) is a powerful activator of GLP-1 secretion in the human enteroendocrine NCI-H716 cell line, but the mechanisms involved in nutrient-stimulated GLP-1 secretion are poorly understood. The objective of this study was to characterize the intracellular signalling pathways regulating MH- and amino acid-induced GLP-1 secretion. Individually, the pharmacological inhibitors, SB203580 (inhibitor of p38 mitogen-activated protein kinase (MAPK)), wortmannin (inhibitor of phosphatidyl inositol 3-kinase) and U0126 (inhibitor of mitogen activated or extracellular signal-regulated protein kinase (MEK1/2) upstream of extracellular signal-regulated kinase (ERK)1/2) all inhibited MH-induced GLP-1 secretion. Further examination of the MAPK pathway showed that MH increased the phosphorylation of ERK1/2, but not p38 or c-Jun N-terminal kinase over 2-15 min. Incubation with SB203580 resulted in a decrease in phosphorylated p38 MAPK and a concomitant increase in the phosphorylation of ERK1/2. Phosphorylation of ERK1/2 was augmented by co-incubation of MH with SB203580. Inhibitors of protein kinase A and protein kinase C did not inhibit MH-induced GLP-1 secretion. In contrast to non-essential amino acids, essential amino acids (EAAs) increased GLP-1 secretion and similar to MH, activated ERK1/2. However, they also activated p38-suggesting type of protein may affect GLP-1 secretion. In conclusion, there appears to be a crosstalk between p38 and ERK1/2 MAPK in the human enteroendocrine cell with the activation of ERK1/2 common to both MH and EAA. Understanding the cellular pathways involved in nutrient-stimulated GLP-1 secretion has important implications for the design of new treatments aimed at increasing endogenous GLP-1 release in type-2 diabetes and obesity.

Indexed as

MeatAmino Acids, EssentialAndrostadienesBlotting, WesternButadienesCell LineDepression, ChemicalEnterocytesEnzyme ActivationGlucagon-Like Peptide 1HumansImidazolesMitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesNitrilesp38 Mitogen-Activated Protein KinasesAmino Acids, EssentialAndrostadienesButadienesGlucagon-Like Peptide 1ImidazolesMitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesNitrilesp38 Mitogen-Activated Protein KinasesPhosphoinositide-3 Kinase InhibitorsProtein HydrolysatesPyridinesRNA, MessengerSB 203580U 0126Wortmannin

Identifiers

PMID17065399
PMCPMC3838362
OpenAlexW2151652647

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.