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PubMed · 234219

Eosinophil polymorphonuclear leukocyte function in immediate hypersensitivity.

E J Goetzl·S I Wasserman·F Austen
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Abstract

An eosinophil chemotactic factor of anaphylaxis (ECF-A), released along with other chemical mediators of immediate hypersensitivity from sensitized mast cells that have been challenged with specific antigen, is capable of selectively attracting eosinophils. The rate and magnitude of tissue eosinophil influx may be enhanced by ascorbate and inhibited by the neutrophil immobilizing factor (NIF). Eosinophils may then exercise a local regulatory function. Phagocytosis or the action of ECF-A at high concentrations causes eosinophils to release arylsulfatase, which inactivates slow reacting substance of anaphylaxis (SRS-A). Additional possible functions of eosinophils may follow from their content of factors that inhibit histamine release or its mediator function, and the high levels of intracellular plasminogen and phospholipase B. Thus, the unique enzymes and factors released from eosinophils may form the basis of their role in immediate and subacute hypersensitivity reactions.

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AnaphylaxisAnimalsAntibody FormationCell MovementCell NucleusChemotaxisComplement System ProteinsEosinophilsFemaleHumansHypersensitivity, ImmediateImmunityImmunity, CellularLeukocytesMast CellsNeutrophilsPeptidesPhagocytosisSRS-AJournal ArticleReview

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E J Goetzl, S I Wasserman, F Austen. 1975. Eosinophil polymorphonuclear leukocyte function in immediate hypersensitivity.. https://pubmed.ncbi.nlm.nih.gov/234219/

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PubMed1995

Release of the mucosal mast cell granule chymase, rat mast cell protease-II, during anaphylaxis is associated with the rapid development of paracellular permeability to macromolecules in rat jejunum.

The soluble granule chymase, rat mast cell protease-II (RMCP-II), is abundantly expressed in intestinal mucosal mast cells (MMC) but its function is not known. One hypothesis is that RMCP-II degrades the epithelial basement membrane and promotes the loss of enterocytes typically associated with type I hypersensitivity reactions in the rat. To test this hypothesis more directly, ex vivo perfusion of the cranial mesenteric artery and jejunal lumen was used to monitor the anaphylactic release of RMCP-II and its effects on mucosal permeability and epithelial integrity. Within 2 min of intravascular challenge with soluble adult Nippostrongylus brasiliensis worm antigen there was a 1,000-fold (P < 0.02) increase in the concentration of RMCP-II in the vascular perfusate from the jejunum of Nippostrongylus-sensitized rats but not the controls. Similarly, translocation of RMCP-II into the gut lumen increased 10-fold (P < 0.02) after 2 min only in worm antigen-challenged immune rats. Using an identical protocol, but incorporating Evans blue-labeled human serum albumin (EB-HSA) in the vascular perfusate, the timing of the release of RMCP-II into the two compartments was very similar to the first experiment and furthermore the translocation of EB-HSA increased 18-fold (P < 0.05) after 4 min in sensitized rats challenged with worm antigen. To examine the effects of RMCP-II more directly 1 mg of the highly purified chymase was introduced into the cranial mesenteric artery in ex vivo perfused normal rats. A significant (P < 0.05) 70-fold increase in concentration of RMCP-II in jejunal perfusate occurred after 6 min. In a repeat dose-response experiment, infusion of 0.375, 0.75, or 1.5 mg of RMCP-II, together with EB-HSA, established that the cumulative amounts of RMCP-II and EB-HSA translocated from the vasculature to the gut lumen in each perfusion (during the 10-min period of RMCP-II infusion) were significantly correlated. Analysis of intestinal perfusates by SDS-PAGE and by Western blotting using monoclonal anti-RMCP-II antibody confirmed that there was a concomitant translocation of both the protease and EB-HSA into the gut lumen. Histological evaluation of the mucosa failed to reveal any significant morphological change in any of the experiments. The rapid development of macromolecular leak, its association with the translocation of RMCP-II, and the absence of gross epithelial lesions, suggest for the first time that a mast cell granule chymase increases epithelial permeability via a paracellular route and implies that the substrate may be a protein, or proteins, in the epithelial junctional complex.

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