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Cited by 112Mast cells and histamineGastrointestinal motility and disordersBarrier Structure and Function Studies

The rat mucosal mast cell chymase, RMCP-11, alters epithelial cell monolayer permeability in association with altered distribution of the tight junction proteins ZO-1 and occludin

Scudamore, Cheryl L., Jepson, Mark A., Hirst, Barry H., Hugh, R., Miller, P.·1998·European Journal of Cell Biology
DOI 10.1016/s0171-9335(98)80065-4
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Abstract

Mucosal mast cells undergo hyperplasia in a variety of inflammatory bowel diseases including nematode infection in man and animals. The intra-epithelial localization of these cells make their soluble mediators prime candidates for modulators of epithelial function. In particular previous in vivo and ex vivo studies have established a link between the release of the highly soluble mast cell granule chymases and increased mucosal permeability. The hypothesis that the rat mast cell protease, RMCP-II, directly increases permeability to macromolecules via the paracellular route is tested in this study. Monolayers of epithelial cells (Madin-Darby canine kidney cell line) were exposed to varying concentrations of RMCP-II in vitro, in the absence of other cell types or mediators, and the effect on permeability and tight junction associated proteins was investigated. Basolateral, but not apical, exposure of polarized MDCK monolayers on porous supports to RMCP-II led to concentration- (> 100 microg/ml) and time-dependent increases in electrical conductance and permeability to mannitol (MW182) and inulin (MW5000), which was accompanied by decreases in the immunostaining of the tight junction-associated proteins occludin and ZO-1. Furthermore, prolonged exposure to RMCP-II (> 12 hours) resulted in the formation of identifiable gaps separating adjacent epithelial cells, in the absence of evidence of cytotoxicity. Inhibition of RMCP-II with Soya bean trypsin inhibitor completely abrogated the response, demonstrating that proteolysis was required. These data provide direct evidence that the rat mast cell chymase RMCP-II can, in the absence of other inflammatory mediators, increase epithelial permeability via an effect on the paracellular route.

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  • Host proteases such as chymase or ELA2A are able to cleave tight and adherens junction proteins including zonula occludens-1 or E-cadherin.

    “Host proteases such as chymase or ELA2A are able to cleave tight and adherens junction proteins including zonula occludens-1 or E-cadherin.22,29,130”

    From The emerging roles of bacterial proteases in intestinal diseases (2023) · cites this paper as [130]

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Authors
Scudamore, C. L., Jepson, M. A., Hirst, B. H., Hugh, R., & Miller, P.
Affiliations
  • University of Edinburgh (GB)
  • University of Bristol (GB)
  • Newcastle University (GB)
ORCID
Venue
European Journal of Cell Biology
Publisher
Elsevier BV
Published
1998-04
Volume
75
Issue
4
Pages
321-330
ISSN
0171-9335 (ISSN-L)
DOI
10.1016/s0171-9335(98)80065-4
OpenAlex
W2003511889
Cited by
112
References
47
Citations by year
2026: 2 · 2025: 2 · 2024: 2 · 2023: 6 · 2022: 6 · 2021: 3 · 2020: 4 · 2019: 5 · 2017: 4 · 2016: 4 · 2015: 4 · 2014: 8 · 2013: 2 · 2012: 4
FWCI
1.11
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • European Journal of Cell Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Wellcome Trust
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (N01 HD-23144)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Mast cells and histamine
  • Health Sciences › Medicine › Gastroenterology › Gastrointestinal motility and disorders
  • Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Keywords
chymase, epithelial permeability, tight junction proteins, ZO-1, occludin, paracellular permeability, mannitol permeability, inulin permeability, electrical conductance, proteolysis, inflammatory bowel disease, nematode infection, mucosal mast cells
MeSH terms
Animals, Cell Line, Cell Membrane Permeability, Dogs, Epithelial Cells, Kidney, Mast Cells, Membrane Proteins, Phosphoproteins, Serine Endopeptidases, Tight Junctions, Rats, Chymases, Occludin, Zonula Occludens-1 Protein

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