Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization. (1/15)

A novel murine cysteine protease from the family of papain-like cysteine proteinases was identified by dbEST-database search. A 1. 4-kb full-length cDNA encoding a predicted polypeptide of 306 amino acids was characterized. The new protease, tentatively named cathepsin Z, exhibits all features characteristics of a papain-like cysteine protease, including the highly conserved residues of the 'catalytic triad'. Cathepsin Z shares only 26-35% overall homology with previously described mammalian papain-like cysteine peptidases and has an unusually short propeptide, which may indicate that it is a member of a putative new subfamily within the family of papain-like cysteine peptidases. Genomic clones covering the murine and human cathepsin Z genes were isolated. They comprise six exons and five introns spanning a 12-kb region of genomic DNA, respectively. Murine cathepsin Z was mapped to chromosome 2, a region with synteny homology to a region of human chromosome 20 to which human cathepsin Z has been mapped previously. Northern blot analysis revealed ubiquitous expression of murine cathepsin Z. Multiple transcriptional start sites were identified for the murine cathepsin Z gene and together with the absence of a TATA box, a high G+C content, a CpG island and the presence of several Sp1-binding sites in the promoter region, murine cathepsin Z may be classified as a 'housekeeping' gene.  (+info)

Capturing protein interactions in the secretory pathway of living cells. (2/15)

The secretory pathway is composed of membrane compartments specialized in protein folding, modification, transport, and sorting. Numerous transient protein-protein interactions guide the transport-competent proteins through the secretory pathway. Here we have adapted the yellow fluorescent protein (YFP)-based protein fragment complementation assay (PCA) to detect protein-protein interactions in the secretory pathway of living cells. Fragments of YFP were fused to the homooligomeric cargo-receptor lectin endoplasmic reticulum Golgi intermediate compartment (ERGIC)-53, to the ERGIC-53-interacting multi-coagulation factor deficiency protein MCFD2, and to ERGIC-53's cargo glycoprotein cathepsin Z. YFP PCA analysis revealed the oligomerization of ERGIC-53 and its interaction with MCFD2, as well as its lectin-mediated interaction with cathepsin Z. Mutation of the lectin domain of ERGIC-53 selectively decreased YFP complementation with cathepsin Z. Using YFP PCA, we discovered a carbohydrate-mediated interaction between ERGIC-53 and cathepsin C. We conclude that YFP PCA can detect weak and transient protein interactions in the secretory pathway and hence is a powerful approach to study luminal processes involved in protein secretion. The study extends the application of PCA to carbohydrate-mediated protein-protein interactions of low affinity.  (+info)

Mapping of a novel susceptibility locus suggests a role for MC3R and CTSZ in human tuberculosis. (3/15)

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Synergistic antitumor effects of combined cathepsin B and cathepsin Z deficiencies on breast cancer progression and metastasis in mice. (4/15)

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Cathepsin X is secreted by human osteoblasts, digests CXCL-12 and impairs adhesion of hematopoietic stem and progenitor cells to osteoblasts. (5/15)

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Cathepsin X-deficient gastric epithelial cells in co-culture with macrophages: characterization of cytokine response and migration capability after Helicobacter pylori infection. (6/15)

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Cysteine proteases bleomycin hydrolase and cathepsin Z mediate N-terminal proteolysis and toxicity of mutant huntingtin. (7/15)

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Genetic susceptibility to tuberculosis associated with cathepsin Z haplotype in a Ugandan household contact study. (8/15)

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