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Mast cells have the ability to produce and degrade FXIIIA depending on their chymase expression profile: mast cells expressing chymase degrade FXIIIA, whereas mast cells that do not express chymase mainly produce FXIIIA
Fibronectin (show FN1 Proteins) was identified as a target of mMCP-5, and the exocytosis of mMCP-5 from the MCs (show SMCP Proteins) in the mouse's peritoneal cavity resulted in the expression of metalloproteinase protease-9, which has been implicated in arthritis.
Data indicate that a second-degree burn injury can initiate an immediate novel zonal degranulation of mast cell throughout all skin layers and a disruption of the epidermal tight junctions dependent on the nonredundant presence of mMCP4 and mMCP5.
mast cell/chymase-mediated intestinal epithelial barrier function is mediated by proteinase-activated receptor 2 (show F2RL1 Proteins)/MMP (show MMP2 Proteins)-2 (show MMP2 Proteins)-dependent
mMCP-4-deficient mice but not to mMCP-5-deficient mice revealing nonredundant actions for these two MC proteases in a model of innate inflammatory injury with remodeling.
mast cell mMCP-4, -5, and -6 (chymase and tryptase (show TPSAB1 Proteins)) participate in the acute inflammation and remodeling process of viral myocarditis.
The prominent mast cell secretory granule protease MCP-5 is essential for the occurrence of irreversible ischemia-reperfusion injury of skeletal muscle.
mast cell chymase activates ERK (show EPHB2 Proteins) and p38 (show CRK Proteins) probably through G-protein-coupled receptor (show GPR34 Proteins), and the ERK (show EPHB2 Proteins) but not p38 (show CRK Proteins) cascade may have a crucial role in chymase-induced migration of eosinophils
chymase rapidly cleaves recombinant pro-IL-18 (show IL18 Proteins) at 56-phenylalanine and produces a biologically active IL-18 (show IL18 Proteins) fragment that is smaller than any other reported IL-18 (show IL18 Proteins)-derived species
Just after stopping the angiotensin II infusion, aortic ACE (show ACE Proteins) and chymase activities were significantly increased, and were involved in the progression of aortic abdominal aneurysms
Cleavage of the alarmins by Human mast cell chymase and human neutrophil cathepsin G (show CTSG Proteins) suggests a function in regulating excessive inflammation.
activation of endothelial CLP (show CALML3 Proteins)/chymase may directly relate to the increased inflammatory phenotypic changes in the vascular system in women with preeclampsia
Placenta-derived chymotrypsin-like protease contributes to the altered endothelial barrier function in preeclampsia.
Our data demonstrated that mast cell chymase plays an important role in keloid formation through TGF-beta1 (show TGFB1 Proteins)/Smad (show SMAD1 Proteins) signaling pathway.
These data suggest a possible contribution of human chymase activation to LPS (show IRF6 Proteins)-induced mortality
we present data indicating that MC tryptase (show TPSAB1 Proteins) and chymase contribute to the development of OSF (show OSTF1 Proteins) and malignant transformation of the overlying epithelium.
The polymorphisms and haplotypes of the CMA1 locus are associated with cardiac hypertrophy in male patients with symptomatic aortic stenosis.
CMA1 gene single nucleotide polymorphisms is associated with essential hypertension.
Significant association between the AG genotype of CMA1 A polymorphism and Angina Pectoris and Ventricular Extrasystoles was observed.
demonstrate the generation of Pso (show PIPOX Proteins) p27 (show PAK2 Proteins) from SCCA1 with extracts from psoriatic scale and even more remarkably, the generation of Pso (show PIPOX Proteins) p27 (show PAK2 Proteins) from SCCA1 in the presence of mast cell associated chymase
This gene product is a chymotryptic serine proteinase that belongs to the peptidase family S1. It is expressed in mast cells and thought to function in the degradation of the extracellular matrix, the regulation of submucosal gland secretion, and the generation of vasoactive peptides. In the heart and blood vessels, this protein, rather than angiotensin converting enzyme, is largely responsible for converting angiotensin I to the vasoactive peptide angiotensin II. Angiotensin II has been implicated in blood pressure control and in the pathogenesis of hypertension, cardiac hypertrophy, and heart failure. Thus, this gene product is a target for cardiovascular disease therapies. This gene maps to 14q11.2 in a cluster of genes encoding other proteases.
chymase 1, mast cell
, mast cell chymase 1
, mast cell protease 5
, mast cell protease I
, chymase 1 preproprotein transcript E
, chymase 1 preproprotein transcript I
, chymase, heart
, chymase, mast cell
, mast cell protease 3
, mast cell protease III
, mast cell chymase
, serine protease