Search results for CTSG

Showing 11 results out of 11

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Protein (4 results from a total of 4)

Identifier: R-HSA-9635429
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: CTSG: P08311
After secretion Cathepsin G is extracellular and associated with the plasma membrane.
Identifier: R-HSA-538738
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: CTSG: P08311
After secretion Cathepsin G is extracellular and associated with the plasma membrane.
Identifier: R-HSA-2228716
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: CTSG: P08311
After secretion Cathepsin G is extracellular and associated with the plasma membrane.
Identifier: R-HSA-6799137
Species: Homo sapiens
Compartment: azurophil granule lumen
Primary external reference: UniProt: CTSG: P08311

Reaction (4 results from a total of 4)

Identifier: R-HSA-3785684
Species: Homo sapiens
Compartment: plasma membrane
Plasma fibronectin (FN1) is degraded by cathepsin G (CTSG) into a characteristic pattern of gelatin-binding peptides of M, = 64000, 40000, and 30000 (Vartio et al. 1981, Vartio 1982). CTSG is activated by UV exposure and can activate matrix metalloproteinases MMP1 and MMP2, but increased levels of MMP activity did not correlate with increased FN degradation in normal human fibroblasts (NHFs) following exposure to UVB (50 mJ/cm2) irradiation, while addtion of CTSG inhibitor decreased FN degradation, suggesting that CTSG is directly responsible for FN1 degradation (Son et al. 2009).
Identifier: R-HSA-448678
Species: Homo sapiens
Compartment: cytosol
Caspase 1 is expressed as a precursor that is cleaved to generate the p10 and p20 subunits that subsequently form the active tetramer.
Identifier: R-HSA-6813659
Species: Homo sapiens
Compartment: extracellular region, plasma membrane
Polymorphonuclear neutrophils (PMNs) are the most abundant circulating blood leukocytes that are rapidly recruited to sites of infection by host- and/or pathogen-derived components. PMNs provide the first-line defense against infection killing invading pathogens and resolving the inflammation they cause (Kobayashi SD et al. 2005). Activated neutrophils are known to release a variety of molecules, including the neutrophil serine proteases such as neutrophil elastase (ELINE), proteinase 3 (PRTN3) and cathepsin G (CTSG) (Garwicz D et al. 2005). Neutrophil serine proteases contribute to antimicrobial defense by
  • attacking membrane-associated (E. coli) or capsule proteins (S.pneumonia), which leads to loss of membrane integrity (Belaaouaj A et al. 2000; Standish AJ & Weiser JN 2009)
  • processing host immune proteins to generate antimicrobial peptides that can directly kill bacteria (Sorensen OE et al. 2001)
  • targeting and inactivating bacterial virulence factors to attenuate bacteria (Weinrauch Y et al. 2002; Lopez-Boado YS et al. 2004)
Identifier: R-HSA-9635424
Species: Homo sapiens
Compartment: cytosol
Mtb secretes serine protease inhibitor Rv3364c (Rv3364c) protein into the phagocyte's cytosol which blocks the serine protease activity of human cathepsin G (CTSG), inhibiting the cleavage of caspase-1 (Danelishvili et al. 2011).

Set (1 results from a total of 1)

Identifier: R-HSA-6813639
Species: Homo sapiens
Compartment: extracellular region

Complex (1 results from a total of 1)

Identifier: R-HSA-6813664
Species: Homo sapiens
Compartment: extracellular region

Pathway (1 results from a total of 1)

Identifier: R-HSA-9014843
Species: Homo sapiens
Interleukin-33 (IL33) cytokine is a member of the Interleukin-1 family. It can be classified as an alarmin because it is released into the extracellular space during cell damage. It acts as an endogenous danger signal (Liew et al. 2010).] The gene product is biologically active (full-length IL33). Its potency has been reported to increase significantly (up to 30x) after cleavage at the N-terminus by inflammatory proteases such as Cathepsin G (CTSG) and Neutrophil elastase (ELANE) (Lefrançais et al. 2012, Lefrançais et al. 2014) but others have suggested that processing inactivates IL33 (Cayrol & Girard 2009). IL33 can act as an extracellular ligand and an intracellular signaling molecule (Martin et al. 2013, 2016). Full-length IL33 has a nuclear localization sequence and can translocate to the nucleus, where it binds heterochromatin (Moussion et al. 2008, Carriere et al. 2007, Roussel et al. 2008, Kuchler et al. 2008, Sundlisaeter et al. 2012, Baekkevold et al. 2003). IL33 that has undergone proteolytic processing is unable to translocate to the nucleus (Martin et al. 2013, Ali et al. 2010). Binding of extracellular IL33 to its receptor Interleukin-1 receptor-like 1 (IL1RL1, suppression of tumorigenicity 2, ST2) initiates several cellular signaling pathways. Cell injury or death are the dominant mechanisms by which IL33 reaches the extracellular environment, IL33 is not actively secreted by cells (Martin et al. 2016, Kaczmarek et al. 2013, Vancamelbeke et al. 2017). Because IL33 is expressed constitutively by endothelial and epithelial cells it is immediately available to the extracellular microenvironment after cell injury and necrosis (Lefrançais et al. 2012). Increases in extracellular ATP or mechanical stress correlate with increased IL33 secretion by mast cells or cardiomyocytes, respectively (Shimokawa et al. 2017, Kakkar et al. 2012, Zhao et al. 2012, Sanada et al. 2007, Chen et al. 2015). Soluble IL1RL1 (IL1RL1 Isoform C, ST2V) (Iwahana et al. 2005, Tominaga et al. 1999) shares the extracellular components of IL1RL1, including the ligand binding domain, but lacks the transmembrane and intracellular components of IL1RL1 (Kakkar et al. 2008, Iwahana et al. 1999). The IL33-IL1RL1 complex recruits a co-receptor, most commonly IL1 receptor accessory protein (IL1RAP, IL-1RAcP) (Schmitz et al. 2005, Lingel et al. 2009, Palmer et al. 2008, Liu et al. 2013).
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