Expression of Mast Cell Proteases in Rat Lung during Helminth Infection: Mast Cells Express both Rat Mast Cell Protease II and Tryptase in Helminth Infected Lung

1999 ◽  
Vol 120 (4) ◽  
pp. 303-309 ◽  
Author(s):  
Masaki Tomita ◽  
Hiroshi Itoh ◽  
Takahiko Kobayashi ◽  
Toshio Onitsuka ◽  
Yukifumi Nawa
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Helminth Infection ◽  
Rat Lung ◽  
Mast Cell Protease

Phenotypic and Quantitative Changes in Mast Cells after Syngeneic Unilateral Lung Transplantation in the Rat

1996 ◽  
Vol 91 (3) ◽  
pp. 319-327 ◽  
Author(s):  
Annick Buvry ◽  
Monique Garbarg ◽  
Violetta Dimitriadou ◽  
Agnès Rouleau ◽  
George F. J. Newlands ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Lung Transplantation ◽  
Left Lung ◽  
Muscle Layer ◽  
Rat Lung ◽  
Large Airways ◽  
Quantitative Changes ◽  
Cell Phenotypes ◽  
And Control

1. Lung transplantation causes a total interruption of the innervation and vascularization within the transplanted organ, followed by repair processes. This is frequently associated with bronchial hyper-responsiveness. A common feature of tissue repair is an increase in the number of mast cells. Three phenotypically distinct mast cell subsets, with respect to their protease content, have been identified in rat lung, and it is probable that mast cells of differing protease phenotype fulfil different functions. 2. We have compared the number, protease phenotype and distribution of mast cells in left lung from transplanted and control Lewis rats 1 month after syngeneic unilateral left lung transplantation, without interference of inflammation, graft rejection or of any treatment. Connective and mucosal-type mast cell phenotypes were characterized using antibodies directed against their specific rat mast cell proteases, RMCPI and RMCPII, respectively. 3. After transplantation, RMCPI and RMCPII tissue concentrations increased by 172% and 239%, respectively, compared with controls (13.1 ± 1.2 and 5.6±1.0 μg/g). 4. Localization of mast cell phenotypes was studied by immunohistochemistry after double immunostaining. The number of mast cells increased after transplantation: the increase in the number of RMCPI-immunoreactive mast cells (RMCPI+) was significant around bronchioles and arterioles, around large vessels and in the pleura. The number of RMCPII+ mast cells also significantly increased around bronchioles and arterioles, as well as in the smooth muscle layer of large airways. Some mast cells stained for the presence of both RMCPI and RMCPII, supporting the existence of co-expressing phenotype in rat lung. The number of mast cells of the RMCPI+ /H+ phenotype significantly increased around bronchioles and arterioles and in the pleura. Moreover, the distribution of the mast cell phenotypes was modified in the different areas after transplantation. 5. This indicates a local differentiation/maturation of mast cells after transplantation.

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 Granzyme D Is a Novel Murine Mast Cell Protease That Is Highly Induced by Multiple Pathways of Mast Cell Activation

2013 ◽  
Vol 81 (6) ◽  
pp. 2085-2094 ◽  
Author(s):  
Elin Rönnberg ◽  
Gabriela Calounova ◽  
Bengt Guss ◽  
Anders Lundequist ◽  
Gunnar Pejler
Keyword(s):  
T Cells ◽  
Mast Cell ◽  
Mast Cells ◽  
Serine Proteases ◽  
Cell Activation ◽  
Calcium Ionophore ◽  
Mast Cell Activation ◽  
Activated T Cells ◽  
Mast Cell Protease ◽  
Murine Mast Cell

ABSTRACTGranzymes are serine proteases known mostly for their role in the induction of apoptosis. Granzymes A and B have been extensively studied, but relatively little is known about granzymes C to G and K to M. T cells, lymphohematopoietic stromal cells, and granulated metrial gland cells express granzyme D, but the function of granzyme D is unknown. Here we show that granzyme D is expressed by murine mast cells and that its level of expression correlates positively with the extent of mast cell maturation. Coculture of mast cells with live, Gram-positive bacteria caused a profound, Toll-like receptor 2 (TLR2)-dependent induction of granzyme D expression. Granzyme D expression was also induced by isolated bacterial cell wall components, including lipopolysaccharide (LPS) and peptidoglycan, and by stem cell factor, IgE receptor cross-linking, and calcium ionophore stimulation. Granzyme D was released into the medium in response to mast cell activation. Granzyme D induction was dependent on protein kinase C and nuclear factor of activated T cells (NFAT). Together, these findings identify granzyme D as a novel murine mast cell protease and implicate granzyme D in settings where mast cells are activated, such as bacterial infection and allergy.

The effect of IL-3 and SCF mixture on cell proliferation and rat mast cell protease-???? synthesis of rat bone marrow derived mast cells

2007 ◽  
Vol &NA; ◽  
pp. S187
Author(s):  
Haneul Nari Lee ◽  
Ju Hyeon Lee ◽  
Chul Hwan Kim ◽  
Yoon Gyu Kang ◽  
Kyung-Whan Joo ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Cell Proliferation ◽  
Mast Cell ◽  
Mast Cells ◽  
Mast Cell Protease ◽  
Rat Bone

scholarly journals Innervation of enteric mast cells by primary spinal afferents in guinea pig and human small intestine

2014 ◽  
Vol 307 (7) ◽  
pp. G719-G731 ◽  
Author(s):  
Guo-Du Wang ◽  
Xi-Yu Wang ◽  
Sumei Liu ◽  
Meihua Qu ◽  
Yun Xia ◽  
...  
Keyword(s):  
Nervous System ◽  
Mast Cell ◽  
Small Intestine ◽  
Electrical Stimulation ◽  
Mast Cells ◽  
Guinea Pig ◽  
Mast Cell Protease ◽  
Human Small Intestine ◽  
Neurokinin 1 ◽  
Stimulation Of

Mast cells express the substance P (SP) neurokinin 1 receptor and the calcitonin gene-related peptide (CGRP) receptor in guinea pig and human small intestine. Enzyme-linked immunoassay showed that activation of intramural afferents by antidromic electrical stimulation or by capsaicin released SP and CGRP from human and guinea pig intestinal segments. Electrical stimulation of the afferents evoked slow excitatory postsynaptic potentials (EPSPs) in the enteric nervous system. The slow EPSPs were mediated by tachykinin neurokinin 1 and CGRP receptors. Capsaicin evoked slow EPSP-like responses that were suppressed by antagonists for protease-activated receptor 2. Afferent stimulation evoked slow EPSP-like excitation that was suppressed by mast cell-stabilizing drugs. Histamine and mast cell protease II were released by 1) exposure to SP or CGRP, 2) capsaicin, 3) compound 48/80, 4) elevation of mast cell Ca2+ by ionophore A23187, and 5) antidromic electrical stimulation of afferents. The mast cell stabilizers cromolyn and doxantrazole suppressed release of protease II and histamine when evoked by SP, CGRP, capsaicin, A23187, electrical stimulation of afferents, or compound 48/80. Neural blockade by tetrodotoxin prevented mast cell protease II release in response to antidromic electrical stimulation of mesenteric afferents. The results support a hypothesis that afferent innervation of enteric mast cells releases histamine and mast cell protease II, both of which are known to act in a diffuse paracrine manner to influence the behavior of enteric nervous system neurons and to elevate the sensitivity of spinal afferent terminals.

scholarly journals Inactivation of thrombin by a complex between rat mast-cell protease 1 and heparin proteoglycan

1994 ◽  
Vol 299 (2) ◽  
pp. 507-513 ◽  
Author(s):  
G Pejler ◽  
K Söderström ◽  
A Karlström
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Binding Sites ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Macromolecular Complex ◽  
Mast Cell Protease ◽  
Peritoneal Mast Cells ◽  
Terminal Amino

Rat peritoneal mast cells were shown to inactivate thrombin rapidly. The thrombin-inactivating activity was purified to homogeneity by a combination of anion-exchange chromatography and h.p.l.c. on a Superdex 75 column. The purified thrombin inactivator had an apparent molecular mass of 29 kDa and an N-terminal amino acid sequence identical to rat mast-cell protease 1 (RMCP-1). After labelling of the mast cells in vivo with 35SO4(2-), RMCP-1 was recovered in a macromolecular complex with [35S]heparin proteoglycans. Dissociation of RMCP-1 from the heparin proteoglycans by Superdex 75 chromatography in the presence of 2 M NaCl resulted in a marked loss of the thrombin-inactivating activity displayed by the enzyme. When RMCP-1 was reconstituted with either endogenous [35S]heparin proteoglycans or standard pig mucosal heparin, the enzyme regained its thrombin-inactivating properties. Affinity chromatography of endogenous [35S]heparin on matrix-linked RMCP-1 demonstrated that all of the heparin molecules contained high-affinity binding sites for the mast-cell protease. In contrast, the endogenous mast-cell heparin showed low affinity for antithrombin, a protease inhibitor involved in the regulation of coagulation enzymes.

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

Pavlovian conditioning of rat mucosal mast cells to secrete rat mast cell protease II

Science ◽  
1989 ◽  
Vol 243 (4887) ◽  
pp. 83-85 ◽  
Author(s):  
G MacQueen ◽  
J Marshall ◽  
M Perdue ◽  
S Siegel ◽  
J Bienenstock
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Pavlovian Conditioning ◽  
Mast Cell Protease ◽  
Mucosal Mast Cells

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
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