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.

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.

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

1998 ◽  
Vol 153 (2) ◽  
pp. 491-504 ◽  
Author(s):  
Jonathan M. Wastling ◽  
Pamela Knight ◽  
Jan Ure ◽  
Steven Wright ◽  
Elisabeth M. Thornton ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mucosal Mast Cell ◽  
Mast Cell Protease ◽  
Mouse Mast Cell ◽  
Ultrastructural Modification

scholarly journals Constitutive expression of mouse mast cell protease‐1 in normal BALB/c mice and its up‐regulation during intestinal nematode infection

Immunology ◽  
1997 ◽  
Vol 90 (2) ◽  
pp. 308-313 ◽  
Author(s):  
J. M. WASTLING ◽  
C. L. SCUDAMORE ◽  
E. M. THORNTON ◽  
G. F. J. NEWLANDS ◽  
H. R. P. MILLER
Keyword(s):  
Mast Cell ◽  
Constitutive Expression ◽  
Nematode Infection ◽  
Mast Cell Protease ◽  
Intestinal Nematode ◽  
Mouse Mast Cell

scholarly journals Mouse Mast Cell Protease-4-dependent production of ET-1 (1-31) and of plaque progression in an/INS; Apolipoprotein E knock-out mouse model of spontaneous atherosclerosis

Life Sciences ◽  
2013 ◽  
Vol 93 (25-26) ◽  
pp. e57
Author(s):  
Martin Houde ◽  
Walid Semaan ◽  
Louisane Desbiens ◽  
Zhipeng You ◽  
Adel G. Schwertani ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mouse Model ◽  
Apolipoprotein E ◽  
Plaque Progression ◽  
Knock Out ◽  
Mast Cell Protease ◽  
Mouse Mast Cell ◽  
Knock Out Mouse

Human mouse mast cell protease 7–like tryptase genes are pseudogenes

2001 ◽  
Vol 107 (2) ◽  
pp. 315-321 ◽  
Author(s):  
Hae-Ki Min ◽  
Naotomo Kambe ◽  
Lawrence B. Schwartz
Keyword(s):  
Mast Cell ◽  
Mast Cell Protease ◽  
Mouse Mast Cell

scholarly journals Biochemical and immunological characterization of multiple glycoforms of mouse mast cell protease 1: comparison with an isolated murine serosal mast cell protease (MMCP-4)

1993 ◽  
Vol 294 (1) ◽  
pp. 127-135 ◽  
Author(s):  
G F J Newlands ◽  
D P Knox ◽  
S R Pirie-Shepherd ◽  
H R P Miller
Keyword(s):  
Mast Cell ◽  
Amino Acid ◽  
Mast Cells ◽  
Western Blotting ◽  
Trichinella Spiralis ◽  
Double Diffusion ◽  
Terminal Amino Acid ◽  
Mast Cell Protease ◽  
Terminal Amino ◽  
Mouse Mast Cell

Five highly soluble, chymotrypsin-like, neutral serine proteases, with molecular masses in the range 30-33 kDa, were isolated from Trichinella spiralis-infected mouse small intestine. These enzymes were closely related antigenically on Western blotting and by Ouchterlony double diffusion using a polyclonal, cross-absorbed, sheep antibody raised against mouse mast cell protease-1 (MMCP-1) and on the basis of N-terminal amino acid sequence analysis, were identified as variant forms of MMCP-1. Substrate and inhibitor analysis confirmed that the five variants (MMCP-1 A-E) had similar characteristics, although highly significant (P = 0.025 to P < 0.0001) variations in Km and kcat, were detected. Against human alpha 1-proteinase inhibitor the Ki for MMCP-1C (45 pM) was significantly (P < 0.0001) greater than those for the other proteases (0.76-2.2 pM). The differences in electrophoretic mobility are probably a result of variable glycosylation, since removal of N-linked carbohydrate produced a polypeptide of approx. 28 kDa in each case which was, like the native enzyme, immunoreactive on Western blotting. A much less soluble 28 kDa enzyme was isolated from serosal mast cells and identified as MMCP-4 by N-terminal amino acid sequencing. Like MMCP-1 it has chymotrypsin-like substrate specificities with activity at neutral pH. However, it was antigenically distinct from MMCP-1 and, using sheep anti-MMCP-1, was not detected on Western blotting or by Ouchterlony double diffusion, e.l.i.s.a. or immunohistochemistry. This last technique established that the MMCP-1 variants were uniquely present in enteric mast cells, thereby providing a highly selective means of distinguishing the mucosal and connective tissue mast cell subsets in the mouse.

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