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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Cathepsin E

cathepsin E, Cate
The protein encoded by this gene is a gastric aspartyl protease that functions as a disulfide-linked homodimer. This protease, which is a member of the peptidase C1 family, has a specificity similar to that of pepsin A and cathepsin D. It is an intracellular proteinase that does not appear to be involved in the digestion of dietary protein and is found in highest concentration in the surface of epithelial mucus-producing cells of the stomach. It is the first aspartic proteinase expressed in the fetal stomach and is found in more than half of gastric cancers. It appears, therefore, to be an oncofetal antigen. Transcript variants utilizing alternative polyadenylation signals and two transcript variants encoding different isoforms exist for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, Cathepsins, CAN, HAD, V1a
Papers using cathepsin E antibodies
Physical and computational analysis of the yeast Kluyveromyces lactis secreted proteome
Chong Shaorong et al., In Nucleic Acids Research, 2007
... CateJHInsights into protein biosynthesis from structures of bacterial ...
Papers on cathepsin E
Purification and molecular cloning of aspartic proteinases from the stomach of adult Japanese fire belly newts, Cynops pyrrhogaster.
Inokuchi et al., Tokyo, Japan. In J Biochem, Jan 2016
UNASSIGNED: Six aspartic proteinase precursors, a pro-cathepsin E (ProCatE) and five pepsinogens (Pgs), were purified from the stomach of adult newts (Cynops pyrrhogaster).
Genome-wide identification and transcript profile of the whole cathepsin superfamily in the intertidal copepod Tigriopus japonicus.
Rhee et al., Suwŏn, South Korea. In Dev Comp Immunol, Nov 2015
However, Tj-aspartyl cathepsin E-like and a novel cysteine cathepsin were slightly reduced in response to LPS exposure.
High Expression of Cathepsin E is Associated with the Severity 
of Airflow Limitation in Patients with COPD.
Xu et al., Shanghai, China. In Copd, Nov 2015
BACKGROUND: It was reported that Cathepsin E (Cat E) plays a critical role in antigen processing and in the development of pulmonary emphysema.
Unstable Foxp3+ regulatory T cells and altered dendritic cells are associated with lipopolysaccharide-induced fetal loss in pregnant interleukin 10-deficient mice.
Robertson et al., Groningen, Netherlands. In Biol Reprod, Oct 2015
Affymetrix microarray revealed an altered transcriptional profile in Treg cells from pregnant Il10(-/-) mice, with elevated expression of Ctse (cathepsin E), Il1r1, Il12rb2, and Ifng.
Aspartic cathepsin D degrades the cytosolic cysteine cathepsin inhibitor stefin B in the cells.
Dolenc et al., Ljubljana, Slovenia. In Biochem Biophys Res Commun, Oct 2015
In contrast, cathepsin E silencing had no effect on stefin B degradation.
The Critical Role of Proteolytic Relay through Cathepsins B and E in the Phenotypic Change of Microglia/Macrophage.
Nakanishi et al., Freiburg, Germany. In J Neurosci, Oct 2015
We herein show the critical role of proteolytic relay through microglial CatB and CatE in the polarization of microglia/macrophages in the neurotoxic phenotype, leading to hypoxia/ischemia (HI)-induced hippocampal neuronal damage in neonatal mice.
High Expression of Cathepsin E in Tissues but Not Blood of Patients with Barrett's Esophagus and Adenocarcinoma.
Lord et al., Sydney, Australia. In Ann Surg Oncol, Jul 2015
BACKGROUND: Cathepsin E (CTSE), an aspartic proteinase, is differentially expressed in the metaplasia-dysplasia-neoplasia sequence of gastric and colon cancer.
Expression, purification and auto-activation of cathepsin E from insect cells.
Dolenc et al., Ljubljana, Slovenia. In Protein Pept Lett, 2014
Cathepsin E is an aspartic protease that belongs to the pepsin family.
Autophagic digestion of Leishmania major by host macrophages is associated with differential expression of BNIP3, CTSE, and the miRNAs miR-101c, miR-129, and miR-210.
Schurigt et al., Würzburg, Germany. In Parasit Vectors, 2014
The protein expression levels of autophagy related 5 (ATG5), BCL2/adenovirus E1B 19 kDa protein-interacting protein 3 (BNIP3), cathepsin E (CTSE), mechanistic target of rapamycin (MTOR), microtubule-associated proteins 1A/1B light chain 3B (LC3B), and ubiquitin (UB) were investigated through western blot analyses.
Detection of pancreatic cancer tumours and precursor lesions by cathepsin E activity in mouse models.
Logsdon et al., Houston, United States. In Gut, 2012
Cath E activity is useful as a potential molecular target for Pancreatic ductal adenocarcinoma and early detection imaging.
Biochemical characterization and structural modeling of human cathepsin E variant 2 in comparison to the wild-type protein.
Turk et al., Ljubljana, Slovenia. In Biol Chem, 2012
A comparative structure model of splice variant 2 was computed based on its alignment to the known structure of cathepsin E intermediate (Protein Data Bank code 1TZS) and used to rationalize its conformational properties and loss of activity.
Emerging roles of cathepsin E in host defense mechanisms.
Tsukuba et al., Fukuoka, Japan. In Biochim Biophys Acta, 2012
Emerging roles of cathepsin E in immune system cells and skin keratinocytes, and in host defense against cancer cells.
Cathepsin E (EC review.
Lapiński et al., Białystok, Poland. In Folia Histochem Cytobiol, 2010
Cathepsin E belongs to the third class of enzymes - hydrolases, a subclass of peptide bond hydrolases and a sub-subclass of endopeptidases with aspartic catalytic sites.
What makes Aspergillus fumigatus a successful pathogen? Genes and molecules involved in invasive aspergillosis.
Rementeria et al., Leioa, Spain. In Rev Iberoam Micol, 2010
These sections include β-glucan, α-glucan, chitin, galactomannan, galactomannoproteins (afmp1/asp f 17 and afmp2), hydrophobins (rodA/hyp1 and rodB), DHN-melanin, their respective synthases (fks1, rho1-4, ags1-3, chsA-G, och1-4, mnn9, van1, anp1, glfA, pksP/alb1, arp1, arp2, abr1, abr2, and ayg1), and modifying enzymes (gel1-7, bgt1, eng1, ecm33, afpigA, afpmt1-2, afpmt4, kre2/afmnt1, afmnt2-3, afcwh41 and pmi); several enzymes related to oxidative stress protection such as catalases (catA, cat1/catB, cat2/katG, catC, and catE), superoxide dismutases (sod1, sod2, sod3/asp f 6, and sod4), fatty acid oxygenases (ppoA-C), glutathione tranferases (gstA-E), and others (afyap1, skn7, and pes1); and efflux transporters (mdr1-4, atrF, abcA-E, and msfA-E).
Selective detection of Cathepsin E proteolytic activity.
Tung et al., Houston, United States. In Biochim Biophys Acta, 2010
Cath E selectivity was established by having -Leu**Pro- residues at the scissile peptide bond.
Over-expression of cathepsin E and trefoil factor 1 in sessile serrated adenomas of the colorectum identified by gene expression analysis.
Ruszkiewicz et al., Adelaide, Australia. In Virchows Arch, 2009
This study demonstrates the over-expression in CTSE, in particular, and TFF1 in sessile serrated adenomas compared to both hyperplastic polyps and tubular adenomas.
Emerging functional roles of cathepsin E.
Kalbacher et al., Tübingen, Germany. In Biochem Biophys Res Commun, 2009
Cathepsin E is an intracellular aspartic protease of the endolysosomal pathway.
Cathepsin E: a mini review.
Kalbacher et al., Tübingen, Germany. In Biochem Biophys Res Commun, 2008
Cathepsin E is a major intracellular aspartic protease which is predominantly present in the cells of immune system and is frequently implicated in antigen processing via the MHC class II pathway.
Identification of beta-secretase-like activity using a mass spectrometry-based assay system.
Döbeli et al., Basel, Switzerland. In Nat Biotechnol, 2000
Subsequent analysis of the related aspartic protease, cathepsin E, revealed almost identical cleavage specificity.
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