scholarly journals Systemic Release of Mucosal Mast-cell Protease in Primed Brown Norway Rats after Feeding withβ-Lactoglobulin

1995 ◽  
Vol 59 (5) ◽  
pp. 771-775 ◽  
Author(s):  
Hyang Ran Ju ◽  
Izumi Matsuura ◽  
Koji Yamada ◽  
Michihiro Sugano ◽  
Katsumi Imaizumi
Keyword(s):  
Mast Cell ◽  
Brown Norway ◽  
Mucosal Mast Cell ◽  
Mast Cell Protease ◽  
Norway Rats

scholarly journals Attenuating Effect of Peruvian Cocoa Populations on the Acute Asthmatic Response in Brown Norway Rats

Nutrients ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2301
Author(s):  
Marta Périz ◽  
Francisco J. Pérez-Cano ◽  
Trinitat Cambras ◽  
Àngels Franch ◽  
Ivan Best ◽  
...  
Keyword(s):  
Mast Cell ◽  
Allergic Asthma ◽  
Immunoglobulin E ◽  
In Vivo Study ◽  
Brown Norway ◽  
Mast Cell Protease ◽  
Norway Rats ◽  
Anaphylactic Response

Cocoa contains bioactive components, which vary according to genetic and environmental factors. The present study aimed to ascertain the anti-allergic properties of native Peruvian cocoa populations (“Blanco de Piura” or BPC, “Amazonas Peru” or APC, “Criollo de Montaña” or CMC, “Chuncho” or CCC, and an ordinary cocoa or OC). To do so, after an initial in vitro approach, an in vivo study focused on the induction of an anaphylactic response associated with allergic asthma in Brown Norway rats was carried out. Based on their polyphenol content, antioxidant activity and in vitro effects, the APC and CMC were selected to be included in the in vivo study. Cocoa diets were tested in a model of allergic asthma in which anaphylactic response was assessed by changes in body temperature, motor activity and body weight. The concentration of specific immunoglobulin E (IgE), mast cell protease and leukotrienes was also quantified in serum and/or bronchoalveolar lavage fluid. CMC and OC populations exhibited a protective effect on the allergic asthma rat model as evidenced by means of a partial protection against anaphylactic response and, above all, in the synthesis of IgE and the release of mast cell protease.

scholarly journals Motor activity as an unbiased variable to assess anaphylaxis in allergic rats

2015 ◽  
Vol 240 (10) ◽  
pp. 1373-1377 ◽  
Author(s):  
Mar Abril-Gil ◽  
Alba Garcia-Just ◽  
Trinitat Cambras ◽  
Francisco J Pérez-Cano ◽  
Cristina Castellote ◽  
...  
Keyword(s):  
Mast Cell ◽  
Body Temperature ◽  
Motor Activity ◽  
Anaphylactic Shock ◽  
Brown Norway ◽  
Mast Cell Protease ◽  
Specific Immunoglobulin ◽  
Norway Rats ◽  
Anaphylactic Response ◽  
Physiological Systems

The release of mediators by mast cells triggers allergic symptoms involving various physiological systems and, in the most severe cases, the development of anaphylactic shock compromising mainly the nervous and cardiovascular systems. We aimed to establish variables to objectively study the anaphylactic response (AR) after an oral challenge in an allergy model. Brown Norway rats were immunized by intraperitoneal injection of ovalbumin with alum and toxin from Bordetella pertussis. Specific immunoglobulin (Ig) E antibodies were developed in immunized animals. Forty days after immunization, the rats were orally challenged with the allergen, and motor activity, body temperature and serum mast cell protease concentration were determined. The anaphylaxis induced a reduction in body temperature and a decrease in the number of animal movements, which was inversely correlated with serum mast cell protease release. In summary, motor activity is a reliable tool for assessing AR and also an unbiased method for screening new anti-allergic drugs.

scholarly journals Dietary wheat germ agglutinin modulates ovalbumin-induced immune responses in Brown Norway rats

2001 ◽  
Vol 85 (4) ◽  
pp. 483-490 ◽  
Author(s):  
Bernhard Watzl ◽  
Christian Neudecker ◽  
Gertrud M. Hänsch ◽  
Gerhard Rechkemmer ◽  
Beatrice L. Pool-Zobel
Keyword(s):  
Mast Cell ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Immunoglobulin E ◽  
Interferon Γ ◽  
Food Allergies ◽  
Brown Norway ◽  
Mast Cell Protease ◽  
Norway Rats

The trend towards an increased consumption of minimally processed plant food results in a higher intake of non-nutritive compounds such as lectins. Lectins are typically globular proteins that are resistant to digestion in the gastrointestinal tract. They affect the integrity of the intestinal epithelium and the absorption of dietary antigens, and induce the release of allergic mediators from mast cellsin vitro. Based on this information we have studied whether dietary wheat germ agglutinin (WGA) could be involved in triggering food allergies. Brown Norway rats were immunized intraperitoneally using ovalbumin (OVA; 10 μg/rat) and 10 d later treated for five consecutive days with WGA (10 mg/rat per d) administered intragastrically. Rats were then orally challenged with OVA (100 μg/rat) 1 h after the last WGA application, and blood was collected 4 h later. Immunological responses (anti-OVA immunoglobulins E and G, rat mast cell protease II, interferon-γ and lymphocyte proliferation) were measured and lymphocyte subpopulations were determined. In immunized rats WGA treatment resulted in increased serum rat mast cell protease II concentrations (pre-challenge 0.26 (SE 0.08) ΜG/ML, POST-CHALLENGE 0.49 (se 0.09) μg/ml; P<0.01) 4 h after the OVA challenge. After 5 d serum concentrations of anti-OVA immunoglobulin E were significantly increased only in the immunized controls (absorbance at 405 nm on days 14 and 19 was 0.09 (se 0.008) and 0.24 (se 0.046) respectively; P=0.02), while in WGA-treated rats no significant increase was seen (0.08 (se 0.004) and 0.15 (se 0.037 respectively; P=0.14). CD4+: CD8+T lymphocytes in the spleen was significantly increased at this time (OVA 1.1 (sd 0.2), OVA+WGA 1.4 (sd 0.1), P<0.05). The treatment did not impair the proliferation and interferon-γ production of mesenteric lymphocytes. In conclusion, these data suggest that high dietary intake of lectins such as WGA may affect the allergic response towards oral antigens in the gut-associated lymphoid tissue.

Constitutive secretion of the granule chymase mouse mast cell protease-1 and the chemokine, CCL2, by mucosal mast cell homologues

2003 ◽  
Vol 33 (1) ◽  
pp. 132-146 ◽  
Author(s):  
J. K. Brown ◽  
P. A. Knight ◽  
S. H. Wright ◽  
E. M. Thornton ◽  
H. R. P. Miller
Keyword(s):  
Mast Cell ◽  
Mucosal Mast Cell ◽  
Mast Cell Protease ◽  
Constitutive Secretion ◽  
Mouse Mast Cell

scholarly journals Mucosal Defense against Gastrointestinal Nematodes: Responses of Mucosal Mast Cells and Mouse Mast Cell Protease 1 during PrimaryStrongyloides venezuelensis Infection in FcRγ-Knockout Mice

2000 ◽  
Vol 68 (9) ◽  
pp. 4968-4971 ◽  
Author(s):  
Denis N. Onah ◽  
Fukumi Uchiyama ◽  
Yuuko Nagakui ◽  
Masao Ono ◽  
Toshiyuki Takai ◽  
...  
Keyword(s):  
Mast Cell ◽  
Gastrointestinal Nematodes ◽  
Enzyme Linked Immunosorbent Assay ◽  
Mucosal Mast Cell ◽  
Mast Cell Protease ◽  
Intestinal Nematode ◽  
Nematode Parasites ◽  
Cell Counts ◽  
Strongyloides Venezuelensis ◽  
Mouse Mast Cell

ABSTRACT A possible role for the γ subunit of immunoglobulin Fc receptors (FcR) in mucosal defenses against intestinal nematode parasites was studied using age-matched FcRγ-knockout (FcRγ−/−) and wild-type (FcRγ+/+) C57BL/6 mice. Mice were infected subcutaneously with 3,000 infective larvae of Strongyloides venezuelensis, and the degree of infection was monitored by daily fecal egg counts and adult worm recovery on days 8 and 13 postinfection. Mucosal mast cell (MMC) responses were assayed by in situ intestinal mast cell counts in stained histological sections of the jejunum and by measuring mouse mast cell protease 1 (MMCP-1) release in serum using sandwich enzyme-linked immunosorbent assay. FcRγ−/− mice had significantly higher egg counts (P < 0.01) and numbers of adult worms (P < 0.05) than FcRγ+/+mice, but mastocytosis and serum MMCP-1 release were comparable. It was concluded that MMCP-1 release may be spontaneous, does not depend on mast cell degranulation via the FcRγ signaling system, and appears to play no role in the expulsion of S. venezuelensis. The delay in worm expulsion in the FcRγ−/− mice might be related to inability of the MMC to degranulate and release effector molecules other than MMCP-1, since FcRγ deletion abrogates mast cell degranulative responses.

Mucosal mast cell protease-1 (MMCP-1) as a marker of intestinal immunopathology in food allergy model

2005 ◽  
Vol 115 (2) ◽  
pp. S240 ◽  
Author(s):  
K. Vaali ◽  
T. Puumalainen ◽  
H. Wolff ◽  
H. Alenius ◽  
T. Palosuo
Keyword(s):  
Mast Cell ◽  
Food Allergy ◽  
Mucosal Mast Cell ◽  
Mast Cell Protease

Selectivity of IgE Responses, Mast Cell Sensitization, and Cytokine Expression in the Immune Response of Brown Norway Rats to Chemical Allergens

1996 ◽  
Vol 172 (2) ◽  
pp. 246-253 ◽  
Author(s):  
K.L. Vento ◽  
R.J. Dearman ◽  
I. Kimber ◽  
D.A. Basketter ◽  
J.W. Coleman
Keyword(s):  
Immune Response ◽  
Mast Cell ◽  
Cytokine Expression ◽  
Brown Norway ◽  
Norway Rats

scholarly journals Mast Cell Inhibition Attenuates Cardiac Remodeling and Diastolic Dysfunction in Middle-aged, Ovariectomized Fischer 344 × Brown Norway Rats

2016 ◽  
Vol 68 (1) ◽  
pp. 49-57 ◽  
Author(s):  
Hao Wang ◽  
Jaqueline da Silva ◽  
Allan Alencar ◽  
Gisele Zapata-Sudo ◽  
Marina R. Lin ◽  
...  
Keyword(s):  
Mast Cell ◽  
Diastolic Dysfunction ◽  
Cardiac Remodeling ◽  
Brown Norway ◽  
Middle Aged ◽  
Fischer 344 ◽  
Cell Inhibition ◽  
Norway Rats

scholarly journals Delayed Expulsion of the Nematode Trichinella spiralisIn Mice Lacking the Mucosal Mast Cell–Specific Granule Chymase, Mouse Mast Cell Protease-1

2000 ◽  
Vol 192 (12) ◽  
pp. 1849-1856 ◽  
Author(s):  
Pamela A. Knight ◽  
Steven H. Wright ◽  
Catherine E. Lawrence ◽  
Yvonne Y.W. Paterson ◽  
Hugh R.P. Miller
Keyword(s):  
Mast Cell ◽  
Serine Proteases ◽  
Trichinella Spiralis ◽  
Gastrointestinal Nematodes ◽  
Intestinal Lumen ◽  
Mucosal Mast Cell ◽  
Mast Cell Protease ◽  
Muscle Larvae ◽  
Mouse Mast Cell

Expulsion of gastrointestinal nematodes is associated with pronounced mucosal mast cell (MMC) hyperplasia, differentiation, and activation, accompanied by the systemic release of MMC granule chymases (chymotrypsin-like serine proteases). The β-chymase mouse mast cell protease-1 (mMCP-1) is expressed predominantly by intraepithelial MMCs, and levels in the bloodstream and intestinal lumen are maximal at the time of worm expulsion in parasitized mice. To address the in vivo functions of MMC-specific β-chymases, we have generated transgenic mice that lack the mMCP-1 gene. They were backcrossed onto a congenic BALB/c background to investigate the response to nematode infection. The deletion of the mMCP-1 gene is associated with significantly delayed expulsion of Trichinella spiralis and increased deposition of muscle larvae in BALB/c mice despite the presence of normal and sometimes increased numbers of MMCs. Neither worm fecundity nor worm burdens were altered in Nippostrongylus-infected mMCP-1−/− BALB/c mice. These data demonstrate, for the first time, that the ablation of an MMC-derived effector molecule compromises the expulsion process.

scholarly journals 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.

1995 ◽  
Vol 182 (6) ◽  
pp. 1871-1881 ◽  
Author(s):  
C L Scudamore ◽  
E M Thornton ◽  
L McMillan ◽  
G F Newlands ◽  
H R Miller
Keyword(s):  
Mast Cell ◽  
Mesenteric Artery ◽  
Ex Vivo ◽  
Rapid Development ◽  
Cell Granule ◽  
Histological Evaluation ◽  
Mucosal Mast Cell ◽  
Type I ◽  
Mast Cell Protease ◽  
Mast Cell Granule

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 &lt; 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 &lt; 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 &lt; 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 &lt; 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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