Disease relevance of Ctse

• Our studies initially demonstrated that catechol estrogen (CE) quinone metabolites are formed in MCF-7 human breast cancer cells in culture [1].
• In the present study, we investigated the role of cathepsin E in immune defense systems against bacterial infection [2].
• Transcriptional profiling of APC(Min/+) mouse intestinal epithelial tissue has revealed that cathepsin E (catE) manifests high relative expression in adenomas and carcinomas relative to normal epithelium [3].
• Cathepsin E-deficient (CatE(-/-)) mice showed dramatically increased susceptibility to infection with both the Gram-positive bacterium Staphyrococcus aureus, and the Gram-negative bacterium Porphyromonas gingivalis when compared with syngeneic wild-type mice, most likely due to impaired regulation of bacterial elimination [2].

High impact information on Ctse

• This relationship led us to postulate that oxidation of the carcinogenic 4-hydroxy catechol estrogens (CE) of estrone (E1) and estradiol (E2) to catechol estrogen-3,4-quinones (CE-3, 4-Q) results in electrophilic intermediates that covalently bind to DNA to form depurinating adducts [4].
• Some of these genes, such as cathepsin E and Igf2, have been previously implicated in tumor cell migration and invasion [5].
• Cathepsin E: a novel target for regulation by class II transactivator [6].
• Further treatment by the air-liquid interface environment modified the differentiated state of the pit cells (pit top cell stage); resulting in the expression of cathepsin E, the disappearance of glycogen granules and the apical accumulation of secretory granules along with an increase in apoptotic cells [7].
• In primary cultured murine microglia, CE was localized mainly in early endosomes and its expression level was markedly increased upon stimulation with interferon-gamma [8].

Biological context of Ctse

• Involvement of cathepsin E in exogenous antigen processing in primary cultured murine microglia [8].
• Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E [9].
• Although CE was not detectable even in the atrophied cortical area of SAMP10, CD contents in the cerebral cortex slightly increased with senescence in all three strains.(ABSTRACT TRUNCATED AT 400 WORDS)[10]
• Germ line genes encoding mouse Ig kappa-chains belonging to the V kappa-1 group have been isolated from BALB/c, NZB, and CE, three inbred strains of differing kappa haplotype [11].
• The analysis of LDL recovered 3 h after injection in mice from different genotypes revealed that LDLs are significantly depleted in CE (reduction from 19% to 50% of the CE/protein ratios) [12].

Anatomical context of Ctse

• In conclusion, CE is required for the generation of an antigenic epitope from OVA but not for the processing of Ii in microglia [8].
• Moreover, mast-cell degranulation resulted in the release of cathepsin E [13].
• Functional studies using a highly specific inhibitor of cathepsin E show that this enzyme is essential for the processing of ovalbumin by this cell line [9].
• At the light-microscopic level, increased immunoreactivities for CE in the brain stem of 2-month-old SAMP8 and P10 were found in reactive microglial cells clustered at the spongy areas but not in microglial cells with resting or ramified morphology and astrocytes [10].
• Characteristic distribution of cathepsin E which immunologically cross-reacts with the 86-kDa acid proteinase from rat gastric mucosa [14].

Associations of Ctse with chemical compounds

• Taken together, our results indicate that cathepsin E is located in mast-cell secretory granules in complex with heparin proteoglycans, and that it has a role in the processing of procarboxypeptidase A into active protease [13].
• The ratio of the soluble/sedimentable cathepsin E content was 1.1, 1.4, 0.9, and 0.7 in cells after 0, 1, 4, and 7 days of DMSO treatment, respectively [15].
• Cathepsin E-type enzymes partially purified from these five tissues were precipitated in the same manner by the specific antiserum, and they had the same molecular weight, electrophoretic mobility, and resistance against denaturation by 4 M urea [14].
• The low pH optimum may distinguish this enzyme from the known rat and mouse aspartic acid proteinases including cathepsin D and cathepsin E [16].
• 4-CE conjugates with glutathione or its hydrolytic products (cysteine and N-acetylcysteine) were detected in picomole amounts in both tumors and hyperplastic mammary tissue, demonstrating the formation of CE-3,4-quinones [17].

Other interactions of Ctse

• We have attempted to elucidate an involvement of cathepsin E (CE) in major histocompatibility complex class II-mediated antigen presentation by microglia [8].
• A role for cathepsin E in the processing of mast-cell carboxypeptidase A [13].
• Here, we show that mast cells from mice lacking the aspartic protease cathepsin E display an accumulation of procarboxypeptidase A, indicating a defect in carboxypeptidase-A processing [13].
• The current study used biochemical and immunohistochemical methods to examine whether cathepsin D (catD) and cathepsin E (catE), candidate aspartic proteases, may be involved in apoE proteolysis [18].
• 6. Activity on human serum albumin is much less and also shows an optimum at pH 3.6; hence, neither enzyme has the properties of cathepsin E [19].

Analytical, diagnostic and therapeutic context of Ctse

• In accordance with this notion, affinity chromatography showed that recombinant cathepsin E bound strongly to heparin under acidic conditions (the conditions prevailing in mast-cell granules) but not at neutral pH [13].
• Immunoblotting analyses revealed that CE in the brain stem of 2-month-old SAMP10 consisted of only the mature form of 42 kDa, whereas CD in this tissue is composed of mainly the mature form of 44 kDa and partially its degradation products [10].

References