Evidence map›Paper›PMID 30280189›Full record

ArticleMolecular medicine reports2018

MrgX2‑mediated internalization of LL‑37 and degranulation of human LAD2 mast cells.

Taisuke Murakami, Kaori Suzuki, Francois Niyonsaba, Hiroyuki Tada, Johannes Reich, Hiroshi Tamura, Isao Nagaoka

Open access · hybridAbstract read
In one paragraph

Article in Molecular medicine reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Pooled it
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  9. Phytochemicals and Vitamin D for a Healthy Life and Prevention of Diseases.International journal of molecular sciences · 2023
    Review
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  15. Review
  16. 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 2 institutions in 1 country.

Taisuke MurakamiDepartment of Host Defense and Biochemical Research, Juntendo University Graduate School of Medicine, Tokyo 113‑8421, Japan.
Kaori SuzukiDepartment of Host Defense and Biochemical Research, Juntendo University Graduate School of Medicine, Tokyo 113‑8421, Japan.
Francois NiyonsabaAtopy (Allergy) Research Center, Juntendo University Graduate School of Medicine, Tokyo 113‑8421, Japan.
Hiroyuki TadaDivision of Oral Microbiology, Tohoku University Graduate School of Dentistry, Sendai‑shi, Miyagi 980‑8575, Japan.
Johannes ReichEndotoxin Test Service, Microcoat Biotechnologie GmbH, D‑82347 Bernried, Germany.
Hiroshi TamuraDepartment of Host Defense and Biochemical Research, Juntendo University Graduate School of Medicine, Tokyo 113‑8421, Japan.
Isao NagaokaDepartment of Host Defense and Biochemical Research, Juntendo University Graduate School of Medicine, Tokyo 113‑8421, Japan.
Juntendo University · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

LL‑37 is the sole antimicrobial peptide of human cathelicidin comprising 37 amino acids, which is expressed mainly in epithelial cells and neutrophils, and activates mast cells. In the present study, in order to elucidate the mechanism of mast cell activation by LL‑37, the associations between the internalization of LL‑37 and Mas‑related gene X2 (MrgX2)‑mediated mast cell activation (degranulation) was investigated using the human mast cell line, LAD2. LL‑37 was rapidly internalized into the cells, and induced degranulation, as assessed by the extracellular release of β‑hexosaminidase. Pertussis toxin, a G‑protein inhibitor, significantly suppressed the internalization of LL‑37 and the degranulation of LAD2 cells. Furthermore, small interfering (si)‑RNA‑mediated knockdown of MrgX2, a putative G protein‑coupled receptor for LL‑37, inhibited the internalization of LL‑37 and degranulation of LAD2 cells. Notably, LL‑37 internalization was enhanced by the stable expression of MrgX2 in HMC‑1 and 293 cells. In addition, the internalized LL‑37 mainly colocalized with MrgX2 in the perinuclear region of LAD2 cells. Furthermore, neuraminidase treatment, which removes negatively charged sialic acid from the cell surface, markedly reduced the internalization of LL‑37 and degranulation of LAD2 cells, and clathrin‑mediated endocytosis inhibitors (dynasore and chlorpromazine) inhibited the internalization and degranulation of LAD2 cells. Taken together, these observations indicated that LL‑37 may bind the negatively charged cell surface molecules, rapidly internalize into the cells via clathrin‑mediated endocytosis and interact with MrgX2 to activate mast cells (LAD2 cells).

Indexed as

Antimicrobial Cationic PeptidesCathelicidinsCell DegranulationCell LineCells, CulturedEndocytosisGene ExpressionGene Knockdown TechniquesHumansMast CellsNerve Tissue ProteinsReceptors, G-Protein-CoupledReceptors, NeuropeptideAntimicrobial Cationic PeptidesCathelicidinsMRGPRX2 protein, humanNerve Tissue ProteinsReceptors, G-Protein-CoupledReceptors, Neuropeptideantimicrobial peptidedegranulationendocytosisG protein-coupled receptorinternalizationLL-37Mas-related gene X2mast cells

Identifiers

PMID30280189
PMCPMC6236315
OpenAlexW2895726295

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.