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Human Cathepsin G Protein expressed in Human - ABIN3119673
Towstyka, Shiromizu, Keitelman, Sabbione, Salamone, Geffner, Trevani, Jancic: Modulation of γδ T-cell activation by neutrophil elastase. in Immunology 2017
Show all 3 Pubmed References
The lung extracellular matrix is vulnerable to pathological structural changes upon upregulation of serine proteases, including cathepsin G (CG) and proteinase 3 (PR3).
CTSG was increased in peripheral blood mononuclear cells and muscle tissues of dermatomyositis (DM) patients, and CTSG activity was higher in the serum of DM patients
CatG can be used as a novel marker to distinguish different NK cell subsets and MARS116 is applicable to determine cell surface CatG activity by flow cytometry.
Results provide evidence that cathepsin G (GC) activates IGF-1R by stimulating IGF-1 release from MCF-7 cells, and that IGF-1R activation is required for CG-induced cell aggregation.
Cleavage of the alarmins by Human mast cell chymase and human neutrophil cathepsin G suggests a function in regulating excessive inflammation.
Data show that lactoferrin (LF) increases the catalytic activity of cathepsin G (CatG) at physiological concentration.
CatG is an essential protease for regulating MHC I molecules
Patients with certain polymorphisms in the CTSG gene had lower risk for chronic postsurgical pain compared with wild-types.
These in vivo data provide, for the first time, compelling evidence of the collateral involvement of cathepsin G, NE, and proteinase 3 in cigarette smoke-induced tissue damage and emphysema
expression levels of ELANE and CTSG were determined by quantitative real-time PCR
Elastase and cathepsin G are elevated in the plasma of HD patients, originating from primed PMNLs. In these patients, chronic elevation of these enzymes contributes to cleavage of VE-cadherin and possible disruption of endothelial integrity.
Cathepsin G is an antimicrobial protein with bacteriocidal activity against S. aureus and N. gonorrhoeae.
proteolytic cleavage of PLTP by cathepsin G may enhance the injurious inflammatory responses that occur in COPD
Neutrophil cathepsin G is a physiologic modulator of platelet thrombus formation in vivo and has potential as a target for novel anti-thrombotic therapies.
Increased concentrations of cathepsins B, D and G in the proliferative eutopic endometrium may play a role in the implantation of endometrial tissue outside the uterine cavity.
demonstrate that cathepsin G (CG), neutrophil elastase (NE), and to a lesser extent proteinase 3 (PR3), degrade endocan
A novel HLA-A*0201 restricted peptide derived from cathepsin G is an effective immunotherapeutic target in acute myeloid leukemia.
the targeting and suppression of CTSG by AML1-ETO in t(8;21) AML may provide a mechanism for leukemia cells to escape from the intracellular surveillance system by preventing degradation of foreign proteins.
NE and CG bind to the surface of cancer cells, presumably to a cell surface receptor, and subsequently undergo clathrin pit-mediated endocytosis.
major binding partners of LEKTI were found to be the antimicrobial peptide dermcidin and the serine protease cathepsin G and no kallikreins.
these findings present evidence of an arterial-specific recruitment pattern centered on CatG-instructed adhesion strengthening. The inhibition of this process could provide a novel strategy for treatment of arterial inflammation with limited side effects.
Cathepsin G activity may impair efferocytosis, which could lead to an accumulation of lesion-associated apoptotic cells and the accelerated progression of early atherosclerotic lesions to more complex lesions in Apoe(-/-) mice.
SerpinB1 is critical for maintaining polymorphonuclear neutrophils survival by antagonizing intracellular cathepsin G activity.
Cathepsin G-regulated release of formyl peptide receptor agonists modulate neutrophil effector functions.
NADPH oxidase in antimicrobial host defense against A. fumigatus and B. cepacia, whereas the proteases neutrophil elastase, cathepsin G, and lysosomal cysteine protease cathepsin C/ dipeptidyl peptidase I are dispensable
Cathepsin G and neutrophil elastase contribute to lung-protective immunity against mycobacterial infections in mice.
This is the first study showing a contribution of neutrophil-derived neutral serine proteases CG and NE to lung-protective immunity against focal pneumonia-inducing serotype 19 S. pneumoniae in mice.
In the absence of a pathogen challenge, neutrophil-derived proteases and nucleosomes contribute to large vessels thrombosis, the main trigger of myocardial infarction and stroke.
Inhibition of TGF-beta significantly reduces microvessel density in mammary tumor-induced bone lesions, mediated by decreased expression of both vascular endothelial growth factor (VEGF) and monocyte chemotactic protein (MCP)-1.
neutrophil elastase and cathepsin G are inhibited by PAI-1 mutants
cathepsin G activity at the tumor-bone interface plays an important role in mammary tumor-induced osteolysis through RANKL
both Cat-G and PAR(4) play key roles in generating and/or amplifying relapses in ulcerative colitis
Cathepsin G and MMP9 were identified as proteases involved in enhanced TGF-beta signaling at the tumor-bone interface of mammary tumor-induced osteolytic lesions.
Serine protease required for resistance to microbial infection; contributes to pathogenessis in endotoxic shock
The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. Transcript variants utilizing alternative polyadenylation signals exist for this gene.
, vimentin-specific protease
, cathepsin G
, LOW QUALITY PROTEIN: cathepsin G