The Presence in Blood of Both Glycosaminoglycan and Mucosal Mast Cell Protease following Systemic Anaphylaxis in the Rat

King, Stephen J.; Reilly, K. M.; Dawes, J.; Miller, H. R. P.

doi:10.1159/000233707

Cited by 10 publications

(6 citation statements)

References 10 publications

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“…32,35,36 It is tempting to suggest that both of these chymases are sufficiently concentrated in the granules to form crystals, and that crystal formation could be facilitated by the loss of other granule matrix constituents such as chondroitin sulfate. We have shown previously, for example, that the release of glycosaminoglycans into rat plasma is significantly correlated with levels of rMCP-II during systemic anaphylactic shock, 37 and the diminishing levels of chloroacetate and proteoglycan staining in rat IMMCs in the jejunum were Figure 8). The data show the intensity of each PCR product recorded as a proportion of the corresponding ␤-actin control PCR product from the same sample, to eliminate variations in the heparinase/RT reactions that could affect the efficiency of subsequent PCR reactions.…”

Section: Discussionmentioning

confidence: 72%

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Histochemical and Ultrastructural Modification of Mucosal Mast Cell Granules in Parasitized Mice Lacking the β-Chymase, Mouse Mast Cell Protease-1

Wastling

Knight

Ure

et al. 1998

The American Journal of Pathology

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The soluble beta-chymases mouse mast cell protease-1 (mMCP-1) and rat mast cell protease-II are predominantly expressed by intestinal mucosal mast cells (IMMCs) and may promote mucosal epithelial permeability when released during intestinal allergic hypersensitivity responses. To study the function of these chymases, we generated mice with a homozygous null mutation of the mMCP-1 gene and investigated their response to infection with the intestinal nematode Nippostrongylus brasiliensis. Whereas mMCP-2, -4, and -5 were transcribed normally, there was no transcription of the mMCP-1 gene in null (-/-) mice, nor was mature mMCP-1 protein detected in (-/-) jejunal mucosa. In contrast, levels of mMCP-1 in wild-type (+/+) jejunal mucosa increased 200- to 350-fold from 0.66 microg mMCP-1/g wet weight in uninfected mice to 129 and 229 microg/g wet weight on days 8 and 10 of infection, respectively. The kinetics of IMMC recruitment differed in -/- mice compared with +/+ controls on days 8 (P < 0.05) and 10 (P < 0.03) of infection. The IMMCs in infected -/- mice stained poorly, if at all, for esterase with naphthol AS-D chloroacetate compared with the intense staining observed in +/+ controls. Ultrastructurally, the prominent crystal intragranular structures that are found in intraepithelial +/+ IMMCs were absent from -/- IMMCs. These data show that disruption of the mMCP-1 gene leads to profound histochemical and ultrastructural changes in IMMC granules.

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Section: Discussionmentioning

confidence: 72%

“…Initial dilutions of the RNA template before RT are indicated (1, 0.1, and 0.01 g/20 l reaction volume). also highly correlated, 37 indicating that IMMCs were being substantially depleted. This suggests that both proteoglycan and protease diffuse rapidly out of, and away from, the cell, unlike heparin/rMCP-I or heparin/tryptase complexes.…”

Section: Discussionmentioning

confidence: 98%

Histochemical and Ultrastructural Modification of Mucosal Mast Cell Granules in Parasitized Mice Lacking the β-Chymase, Mouse Mast Cell Protease-1

Wastling

Knight

Ure

et al. 1998

The American Journal of Pathology

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“…Macrophages do not stain with the CAER when sec tions are embedded in paraffin [11], as in the present study, and neutrophils can be distinguished from mast cells by their characteristic nuclear morpholo gy. Further support for the use of this stain is pro vided by the observation that CAER stained equal numbers of mast cells when compared with alcian blue-safranine 0 in human nasal mucosa [12], and when compared with toluidine blue in rat intestine [13,14].…”

Section: Discussionmentioning

confidence: 98%

Time Course of Cellular Infiltration in the Nasal Mucosa during the Immediate Allergic Reaction

Lozewicz

Gomez

Chalstrey

et al. 1991

Int Arch Allergy Immunol

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In 23 patients with allergic rhinitis, biopsies of the nasal mucous membrane were taken at one of the following times after challenge of one nostril with allergen: 0 (baseline) (n = 7), ½ h (n = 6), 1 h (n = 5), and 2 h (n = 5). In the nostril stimulated by allergen there was a transient early phase influx of eosinophils while the numbers of stainable mast cells decreased, probably due to their degranulation. In the contralateral unstimulated nostril, there was no change in numbers of eosinophils but the numbers of stainable mast cells decreased. These results support the proposed role in allergic rhinitis of the mast cell and eosinophil, and suggest that the eosinophil may be a rapidly mobilized effector cell.

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“…In contrast, the tryptase, mMCP‐7, that lacked this positively charged domain, was released from the cells and was found in the bloodstream 95 . The lack of heparin in rodent MMC may also account for the high solubility of mMCP‐1 and rMCP‐2 and for the rapid, concomitant release of rMCP‐2 and GAGs into peripheral blood during systemic anaphylaxis 96 . The heterogeneity of the GAGs of mast cells at sites of inflammation, 97 as well as the strong net positive charge of most chymases (Table 1) and the positively charged domains on tryptases, indicate therefore that patterns of storage and release of these proteolytic enzymes will differ from tissue to tissue.…”

Section: Variant Expression Of Granule Proteinases and Proteoglycans mentioning

confidence: 99%

Tissue‐specific expression of mast cell granule serine proteinases and their role in inflammation in the lung and gut

2002

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SUMMARYSerine proteinases with trypsin-like (tryptase) and chymotrypsin-like (chymase) properties are major constituents of mast cell granules. Several tetrameric tryptases with differing specificities have been characterized in humans, but only a single chymase. In other species there are larger families of chymases with distinct and narrow proteolytic specificities. Expression of chymases and tryptases varies between tissues. Human pulmonary and gastrointestinal mast cells express chymase at lower levels than tryptase, whereas rodent and ruminant gastrointestinal mast cells express uniquely mucosa-specific chymases. Local and systemic release of chymases and tryptases can be quantified by immunoassay, providing highly specific markers of mast cell activation. The expression and constitutive extracellular secretion of the mucosa-specific chymase, mouse mast cell proteinase-1 (mMCP-1), is regulated by transforming growth factor-b 1 (TGF-b 1 ) in vitro, but it is not clear how the differential expression of chymases and tryptases is regulated in other species. Few native inhibitors have been identified for tryptases but the tetramers dissociate into inactive subunits in the absence of heparin. Chymases are variably inhibited by plasma proteinase inhibitors and by secretory leucocyte protease inhibitor (SLPI) that is expressed in the airways. Tryptases and chymases promote vascular permeability via indirect and possibly direct mechanisms. They contribute to tissue remodelling through selective proteolysis of matrix proteins and through activation of proteinase-activated receptors and of matrix metalloproteinases. Chymase may modulate vascular tissues through its ability to process angiotensin-I to angiotensin-II. Mucosa-specific chymases promote epithelial permeability and are involved in the immune expulsion of intestinal nematodes. Importantly, granule proteinases released extracellularly contribute to the recruitment of inflammatory cells and may thus be involved in innate responses to infection.

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The Presence in Blood of Both Glycosaminoglycan and Mucosal Mast Cell Protease following Systemic Anaphylaxis in the Rat

Cited by 10 publications

References 10 publications

Histochemical and Ultrastructural Modification of Mucosal Mast Cell Granules in Parasitized Mice Lacking the β-Chymase, Mouse Mast Cell Protease-1

Histochemical and Ultrastructural Modification of Mucosal Mast Cell Granules in Parasitized Mice Lacking the β-Chymase, Mouse Mast Cell Protease-1

Time Course of Cellular Infiltration in the Nasal Mucosa during the Immediate Allergic Reaction

Tissue‐specific expression of mast cell granule serine proteinases and their role in inflammation in the lung and gut

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