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PubMed · 6181244

Antigen-induced decrease of salicylic acid absorption from the small intestine in actively immunized rats.

J Nakamura·A Yamamoto·S Takada·T Kimura·H Sezaki
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Abstract

Rats were intraperitoneally immunized with bovine gamma-globulin (BGG) emulsified in incomplete Freund's adjuvant. Intestinal absorption of salicylic acid from the rat small intestine was examined by means of in situ recirculation technique. The disappearance of salicylic acid from the luminal solution was significantly decreased in rats challenged intravenously with BGG compared to saline as control. A significant decrease in absorption of salicylic acid was noted in rats immunized twice and three times, but not in rats immunized only once. The effect was maintained for at least 5 weeks after the third immunization, whereas it disappeared within 10 weeks. In normal rats, the decreased absorption of salicylic acid by the intravenous challenge with BGG was hardly observed at all. These findings suggest that the intestinal absorption of salicylic acid may be affected by systemic anaphylaxis in actively immunized rats.

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AnaphylaxisAnimalsImmunizationIntestinal AbsorptionMaleRatsSalicylatesgamma-GlobulinsJournal Article

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J Nakamura, A Yamamoto, S Takada, T Kimura, H Sezaki. 1982. Antigen-induced decrease of salicylic acid absorption from the small intestine in actively immunized rats.. https://doi.org/10.1248/bpb1978.5.278

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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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