Mast cells protect from post‐traumatic brain inflammation by the mast cell‐specific chymase mouse mast cell protease‐4

2012 ◽  
Vol 27 (3) ◽  
pp. 920-929 ◽  
Author(s):  
Sven Hendrix ◽  
Peter Kramer ◽  
Debora Pehl ◽  
Katharina Warnke ◽  
Francesco Boato ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Brain Inflammation ◽  
Mast Cell Protease ◽  
Post Traumatic ◽  
Mouse Mast Cell

scholarly journals Mast cells protect from post-traumatic spinal cord damage in mice by degrading inflammation-associated cytokines via mouse mast cell protease 4

2014 ◽  
Vol 62 ◽  
pp. 260-272 ◽  
Author(s):  
Sofie Nelissen ◽  
Tim Vangansewinkel ◽  
Nathalie Geurts ◽  
Lies Geboes ◽  
Evi Lemmens ◽  
...  
Keyword(s):  
Spinal Cord ◽  
Mast Cell ◽  
Mast Cells ◽  
Mast Cell Protease ◽  
Spinal Cord Damage ◽  
Post Traumatic ◽  
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.

scholarly journals Basophils preferentially express mouse mast cell protease 11 among the mast cell tryptase family in contrast to mast cells

2009 ◽  
Vol 86 (6) ◽  
pp. 1417-1425 ◽  
Author(s):  
Tsukasa Ugajin ◽  
Toshiyuki Kojima ◽  
Kaori Mukai ◽  
Kazushige Obata ◽  
Yohei Kawano ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Mast Cell Tryptase ◽  
Mast Cell Protease ◽  
Mouse Mast Cell

scholarly journals Mouse bone marrow-derived mast cells (mBMMC) obtained in vitro from mice that are mast cell-deficient in vivo express the same panel of granule proteases as mBMMC and serosal mast cells from their normal littermates.

1994 ◽  
Vol 180 (1) ◽  
pp. 67-73 ◽  
Author(s):  
K K Eklund ◽  
N Ghildyal ◽  
K F Austen ◽  
D S Friend ◽  
V Schiller ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Mast Cell ◽  
Steady State ◽  
Mast Cells ◽  
Induced Expression ◽  
Mast Cell Protease ◽  
Steady State Levels ◽  
Mouse Mast Cell

The ear, skin, and purified serosal mast cells of WBB6F1/J-(+/+) (WB-(+/+)) and WCB6F1/J-(+/+) (WC-(+/+)) mice contain high steady-state levels of the transcripts that encode mouse mast cell protease (mMCP) 2, mMCP-4, mMCP-5, mMCP-6, and mouse mast cell carboxypeptidase A (mMC-CPA). In contrast, no mast cell protease transcripts are present in abundance in the ear and skin of WBB6F1/J-W/Wv (W/Wv) and WCB6F1/J-Sl/Sld (Sl/Sld) mice which are mast cell-deficient in vivo due to defects in their c-kit and c-kit ligand genes, respectively. We now report that the immature bone marrow-derived mast cells (mBMMC) obtained in vitro with recombinant interleukin 3 (rIL-3) or WEHI-3 cell conditioned medium from WB-(+/+), WC-(+/+), W/Wv, and Sl/Sld mice all contain high steady-state levels of the mMCP-2, mMCP-4, mMCP-5, mMCP-6, and mMC-CPA transcripts. As assessed immunohistochemically, mMCP-2 protein and mMCP-5 protein are also present in the granules of mBMMC from WB-(+/+), WC-(+/+), and W/Wv mice. That Sl/Sld and W/Wv mBMMC contain high steady-state levels of five granule protease transcripts expressed by the mature serosal, ear, and skin mast cells of their normal +/+ littermates suggests that c-kit-mediated signal transduction is not essential for inducing transcription of these protease genes. Because rIL-4 inhibits the rIL-10-induced expression of mMCP-1 and mMCP-2 in BALB/cJ mBMMC, the ability of rIL-4 to influence protease mRNA levels in WC-(+/+) mBMMC and W/Wv mBMMC was investigated. Although rIL-10 induced expression of the mMCP-1 transcript in WC-(+/+) and W/Wv mBMMC, rIL-4 was not able to suppress the steady-state levels of the mMCP-1 transcript or any other protease transcript in these cultured mast cells. Thus, not only do BALB/cJ mBMMC express fewer granule proteases than mBMMC from mast cell-deficient strains and their normal littermates but the subsequent induction of late-expressed proteases in BALB/cJ mBMMC is more tightly regulated by IL-3 and IL-4.

scholarly journals Abnormal Expression of Mouse Mast Cell Protease 5 Gene in Cultured Mast Cells Derived From Mutant mi/mi Mice

Blood ◽  
1997 ◽  
Vol 90 (8) ◽  
pp. 3057-3066 ◽  
Author(s):  
Eiichi Morii ◽  
Tomoko Jippo ◽  
Tohru Tsujimura ◽  
Koji Hashimoto ◽  
Dae-Ki Kim ◽  
...  
Keyword(s):  
Mast Cell ◽  
Transcription Factors ◽  
Mast Cells ◽  
Promoter Region ◽  
Leucine Zipper ◽  
Consensus Sequence ◽  
Mast Cell Protease ◽  
Helix Loop Helix ◽  
Regulation Mechanisms ◽  
Mouse Mast Cell

Abstract Mast cells contain a lot of mast cell-specific proteases. We have reported that the expression of mouse mast cell protease 6 (MMCP-6) is remarkably reduced in both cultured mast cells (CMCs) and skin mast cells of mi/mi mutant mice. In the present study, we found that the expression of MMCP-5 was reduced in CMCs but not in skin mast cells of mi/mi mice, and we compared the regulation mechanisms of MMCP-5 with those of MMCP-6. The mi locus encodes a member of the basic-helix-loop-helix-leucine zipper (bHLH-Zip) protein family of transcription factors (hereafter called MITF ). The consensus sequence recognized and bound by bHLH-Zip transcription factors is CANNTG. The overexpression of the normal (+) MITF but not of mi-MITF normalized the poor expression of the MMCP-5 gene in mi/mi CMCs, indicating the involvement of +-MITF in transactivation of the MMCP-5 gene. Although +-MITF directly bound CANNTG motifs in the promoter region of the MMCP-6 gene and transactivated it, the binding of +-MITF to the CAGTTG motif in the promoter region of the MMCP-5 gene was not detectable. The +-MITF appeared to regulate the transactivation of the MMCP-5 gene indirectly. Moreover, addition of stem cell factor to the medium normalized the expression of the MMCP-5 but not of the MMCP-6 gene in mi/mi CMCs. Despite the significant reduction of both MMCP-5 and MMCP-6 expressions in mi/mi CMCs, their regulation mechanisms appeared to be different.

scholarly journals Trichinella spiralis Secreted Enzymes Regulate Nucleotide-Induced Mast Cell Activation and Release of Mouse Mast Cell Protease 1

2012 ◽  
Vol 80 (11) ◽  
pp. 3761-3767 ◽  
Author(s):  
Holly C. Afferson ◽  
Emily Eleftheriou ◽  
Murray E. Selkirk ◽  
Kleoniki Gounaris
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Cell Activation ◽  
Trichinella Spiralis ◽  
Critical Role ◽  
Extracellular Nucleotides ◽  
Mast Cell Activation ◽  
Content Type ◽  
Mast Cell Protease ◽  
Mouse Mast Cell

ABSTRACTExtracellular nucleotides are important triggers of innate immunity, acting on a wide variety of cells via signaling through purinergic receptors. Mucosal mast cells contribute to expulsion of a number of gastrointestinal nematode parasites, and mouse mast cell protease 1 has been shown to have a critical role in clearance ofTrichinella spiralisfrom the intestinal tract. We show here that adenosine, ADP, ATP, UDP, and UTP all stimulate calcium mobilization in bone marrow-derived mast cells with a mucosal phenotype. Secreted proteins fromT. spiralisinfective larvae inhibit nucleotide-induced mast cell activation, and that induced by ADP and UDP is specifically blocked by parasite secretory 5′-nucleotidase. Release of mouse mast cell protease 1 is stimulated by ADP and ATP. Both parasite secreted products and the 5′-nucleotidase inhibit ADP-induced release of mast cell protease, whereas that stimulated by ATP is partially inhibited by secreted products alone. This indicates that the 5′-nucleotidase contributes to but is not solely responsible for inhibition of nucleotide-mediated effects on mast cell function. Secretion of nucleotide-metabolizing enzymes by parasitic nematodes most likely evolved as a strategy for suppression of innate immune responses and is discussed in this context.

scholarly journals Mouse Mast Cell Protease 9, a Novel Member of the Chromosome 14 Family of Serine Proteases that is Selectively Expressed in Uterine Mast Cells

1997 ◽  
Vol 272 (46) ◽  
pp. 29158-29166 ◽  
Author(s):  
John E. Hunt ◽  
Daniel S. Friend ◽  
Michael F. Gurish ◽  
Eric Feyfant ◽  
Andrej Šali ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Serine Proteases ◽  
Chromosome 14 ◽  
Mast Cell Protease ◽  
Mouse Mast Cell
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