Requirement of c-jun transcription factor on the mouse mast cell protease-6 expression in the mast cells

2004 ◽  
Vol 431 (1) ◽  
pp. 71-78 ◽  
Author(s):  
Dae-Ki Kim ◽  
Young-Mi Lee
Keyword(s):  
Transcription Factor ◽  
Mast Cell ◽  
Mast Cells ◽  
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.

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 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 Synergy of PEBP2/CBF with mi transcription factor (MITF) for transactivation of mouse mast cell protease 6 gene

Oncogene ◽  
1999 ◽  
Vol 18 (32) ◽  
pp. 4632-4639 ◽  
Author(s):  
Hideki Ogihara ◽  
Tomohiko Kanno ◽  
Eiichi Morii ◽  
Dae-Ki Kim ◽  
Young-Mi Lee ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Mast Cell ◽  
Mast Cell Protease ◽  
Mouse Mast Cell

Inhibitory effect of the transcription factor encoded by the mutant mi microphthalmia allele on transactivation of mouse mast cell protease 7 gene

Blood ◽  
2001 ◽  
Vol 97 (3) ◽  
pp. 645-651 ◽  
Author(s):  
Hideki Ogihara ◽  
Eiichi Morii ◽  
Dae-Ki Kim ◽  
Keisuke Oboki ◽  
Yukihiko Kitamura
Keyword(s):  
Transcription Factor ◽  
Mast Cell ◽  
Inhibitory Effect ◽  
Chromosome 17 ◽  
Binding Motif ◽  
Mast Cell Protease ◽  
Coding Regions ◽  
Helix Loop Helix ◽  
Negative Effect ◽  
Mouse Mast Cell

Abstract The transcription factor encoded by the mi locus (MITF) is a transcription factor of the basic-helix-loop-helix zipper protein family. Mice of mi/mi genotype express a normal amount of abnormal MITF, whereas mice oftg/tg genotype do not express any MITFs due to the transgene insertional mutation. The effect of normal (+) and mutant (mi) MITFs on the expression of mouse mast cell protease (MMCP) 6 and 7 was examined. Both MMCP-6 and MMCP-7 are tryptases, and their coding regions with high homology are closely located on chromosome 17. Both MMCP-6 and MMCP-7 genes are expressed in normal cultured mast cells (+/+ CMCs). Although the transcription of MMCP-6 gene was severely suppressed in bothmi/mi and tg/tg CMCs, that of MMCP-7 gene was severely suppressed only in mi/mi CMCs. The study identified the most significant segment for the transcription in the 5′ flanking region of MMCP-7 gene. Unexpectedly, no CANNTG motifs were found that are recognized and bound by +-MITF in this segment. Instead, there was an AP-1 binding motif, and binding of c-Jun to the AP-1 motif significantly enhanced the transcription of MMCP-7 gene. The complex formation of c-Jun with either +-MITF ormi-MITF was demonstrated. The binding of +-MITF to c-Jun enhanced the transactivation of MMCP-7 gene, and that ofmi-MITF suppressed the transactivation. Although the former complex was located only in the nucleus, the latter complex was predominantly found in the cytoplasm. The negative effect ofmi-MITF on the transcription of MMCP-7 gene appeared to be executed through the interaction with c-Jun.

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.

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
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