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Cathepsin W

cathepsin W, CTSW
The protein encoded by this gene, a member of the peptidase C1 family, is a cysteine proteinase that may have a specific function in the mechanism or regulation of T-cell cytolytic activity. The encoded protein is found associated with the membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. Expression of this gene is up-regulated by interleukin-2. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Cathepsins, ACID, HAD, CD8, SET
Papers on cathepsin W
CXCR3 expression defines a novel subset of innate CD8+ T cells that enhance immunity against bacterial infection and cancer upon stimulation with IL-15.
Satoskar et al., Columbus, United States. In Faseb J, Mar 2015
In depth analysis of the CXCR3(+) subset showed increased gene expression of Ccl5, Klrc1, CtsW, GP49a, IL-2Rβ, Atp5e, and Ly6c but reduced IFN-γR2 and Art2b.
Cathepsin W Is Required for Escape of Influenza A Virus from Late Endosomes.
Stertz et al., Zürich, Switzerland. In Mbio, 2014
UNLABELLED: Human cathepsin W (CtsW) is a cysteine protease, which was identified in a genome-wide RNA interference (RNAi) screen to be required for influenza A virus (IAV) replication.
Mild Plasmodium falciparum malaria following an episode of severe malaria is associated with induction of the interferon pathway in Malawian children.
Daily et al., New York City, United States. In Infect Immun, 2012
These genes reflect the interferon (IFN) pathway and T cell biology and include IFN-induced protein transcripts 1 to 3, oligoadenylate synthetases 1 and 3, and the T cell markers cathepsin W and perforin.
Expression pattern of cathepsin W isoforms in peripheral blood and gastroesophageal mucosa of patients with gastroesophageal reflux disease.
Wex et al., Magdeburg, Germany. In Biol Chem, 2011
The predominant expression of wildtype form by infiltrating immune cells was confirmed in 116 patients with gastroesophageal reflux disease and 27 reflux-negative individuals demonstrating that cathepsin W expression is not altered in this disease.
Cathepsin W expressed exclusively in CD8+ T cells and NK cells, is secreted during target cell killing but is not essential for cytotoxicity in human CTLs.
Tolosa et al., Tübingen, Germany. In Exp Hematol, 2009
Despite being expressed in the effector subset of CD8(+) and NK cells and of being released during target cell killing, our functional inhibition studies exclude an essential role of CatW in the process of cytotoxicity.
Proteomic analysis of human NK-92 cells after NK cell-mediated cytotoxicity against K562 cells.
Chen et al., Xi'an, China. In Biochemistry (mosc), 2007
Western blotting analysis of heat shock protein 60 (HSP60) and cathepsin W verified their proteome results.
Microarray analysis of gene expression associated with extrapulmonary dissemination of tuberculosis.
Yim et al., Seoul, South Korea. In Respirology, 2006
RESULTS: Compared with the control sample, the expression of 16 genes, including those for tumour necrosis factor (TNF)-alpha and cathepsin W, was increased, and the expression of 45 genes including that for TNF-receptor superfamily member 7 (TNFRSF7), was decreased in the extrapulmonary tuberculosis patients.
Upregulation of cathepsin W-expressing T cells is specific for autoimmune atrophic gastritis compared to other types of chronic gastritis.
Wex et al., Magdeburg, Germany. In World J Gastroenterol, 2005
AIM: To investigate a pathophysiological role of cathepsin W (CatW), a putative thiol-dependent cysteine protease, which is specifically expressed in cytotoxic lymphocytes, in different types of chronic inflammation of the gastric mucosa.
Identification of a novel isoform predominantly expressed in gastric tissue and a triple-base pair polymorphism of the cathepsin W gene.
Wex et al., Magdeburg, Germany. In Biochem Biophys Res Commun, 2004
a genetic variant and a novel isoform of cathepsin W are present in about 14% and 12%, respectively, within the Caucasian population
Characterization of murine cathepsin W and its role in cell-mediated cytotoxicity.
Pham et al., Saint Louis, United States. In J Biol Chem, 2004
Cathepsin W is a member of the papain-like family of cysteine proteases.
Cathepsins K, L, B, X and W are differentially expressed in normal and chronically inflamed gastric mucosa.
Wex et al., Magdeburg, Germany. In Biol Chem, 2004
In contrast, cathepsin W was expressed at very low levels.
Functional involvement of cathepsin W in the cytotoxic activity of NK-92 cells.
Malfertheiner et al., Magdeburg, Germany. In Febs Lett, 2003
Human cathepsin W (lymphopain) is a papain-like cysteine protease of unknown function that is specifically expressed in natural killer (NK) cells and to a lesser extent in cytotoxic T cells (CTL).
Constitutive expression of cytotoxic proteases and down-regulation of protease inhibitors in LGL leukemia.
Loughran et al., Tampa, United States. In Int J Oncol, 2003
The up-regulated genes involved in cytotoxic function were serine proteinases (granzymes A, B, H and K) cysteine proteinases [cathepsin C, cathepsin W (lymphopain)], calpain small subunit and caspase-8.
Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal tract.
Wex et al., Magdeburg, Germany. In Biol Chem, 2002
Cathepsin W-positive cells had a 'lymphocyte phenotype', but the relative portion of cathepsin W-positive cells among the infiltrating leukocytes in gastrointestinal disease differed remarkably.
Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum.
Brömme et al., New York City, United States. In J Immunol, 2001
Endogenous cathepsin W is expressed predominantly in NK cells, is up-regulated by IL-2, and is mainly targeted to the endoplasmic reticulum.
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