Evidence map›Paper›PMID 9806967›Full record

ArticleThe Journal of general physiology1998

Mechanism of peptide-induced mast cell degranulation. Translocation and patch-clamp studies.

D Lorenz, B Wiesner, J Zipper, A Winkler, E Krause, M Beyermann, M Lindau, M Bienert

Abstract read
In one paragraph

Article in The Journal of general physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Review
  2. Review
  3. BioMed research international · 2020
    Article
  4. Article
  5. Article
  6. Review
  7. Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes.The journal of physical chemistry letters · 2016
    Article
  8. Article
  9. Article
  10. Review
  11. Substance P in heart failure: the good and the bad.International journal of cardiology · 2014
    Review
  12. Review
  13. Article
  14. Effects of endogenous substance P expression on degranulation in RBL-2H3 cells.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2011
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors.

D LorenzInstitute of Molecular Pharmacology, 10315 Berlin, Germany. lorenz@fmp-berlin.de
B Wiesner
J Zipper
A Winkler
E Krause
M Beyermann
M Lindau
M Bienert

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Substance P and other polycationic peptides are thought to stimulate mast cell degranulation via direct activation of G proteins. We investigated the ability of extracellularly applied substance P to translocate into mast cells and the ability of intracellularly applied substance P to stimulate degranulation. In addition, we studied by reverse transcription--PCR whether substance P-specific receptors are present in the mast cell membrane. To study translocation, a biologically active and enzymatically stable fluorescent analogue of substance P was synthesized. A rapid, substance P receptor- and energy-independent uptake of this peptide into pertussis toxin-treated and -untreated mast cells was demonstrated using confocal laser scanning microscopy. The peptide was shown to localize preferentially on or inside the mast cell granules using electron microscopic autoradiography with 125I-labeled all-D substance P and 3H-labeled substance P. Cell membrane capacitance measurements using the patch-clamp technique demonstrated that intracellularly applied substance P induced calcium transients and activated mast cell exocytosis with a time delay that depended on peptide concentration (delay of 100-500 s at concentrations of substance P from 50 to 5 microM). Degranulation in response to intracellularly applied substance P was inhibited by GDPbetaS and pertussis toxin, suggesting that substance P acts via G protein activation. These results support the recently proposed model of a receptor-independent mechanism of peptide-induced mast cell degranulation, which assumes a direct interaction of peptides with G protein alpha subunits subsequent to their translocation across the plasma membrane.

Indexed as

AnimalsAutoradiographyBiological TransportCalciumCell DegranulationCytoplasmic GranulesElectric ConductivityGene ExpressionGTP-Binding ProteinsHistamine ReleaseMaleMast CellsMicroscopy, ConfocalMicroscopy, ElectronPatch-Clamp TechniquesRatsCalciumGTP-Binding ProteinsRNA, MessengerSubstance P

Identifiers

PMID9806967
PMCPMC2229441

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LicenceCC BY-NC-SA
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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.