Disease relevance of Ctsh

• Cathepsin H and beta-glucuronidase activities were not localized in the plasma membrane fractions of the B16 melanomas [1].
• The mean cathepsin H level was significantly higher for both groups of patients compared to normal sera level, being highest for metastatic melanoma patients [2].

High impact information on Ctsh

• The amino acid sequence of a part of the murine major excreted protein deduced from the DNA sequence reveals substantial and significant homology with the cysteine proteases actinidin, rat cathepsin H, and papain [3].
• In contrast to parental L cells, mutant LX cells harbor defects that interfere with the maturation and activity of cathepsin B and cathepsin L but not cathepsin H [4].
• The first site of hydrolase concentration was the early endosomes, which contained the bulk of the cellular cathepsin H [5].
• Lysosomal enzyme trafficking between phagosomes, endosomes, and lysosomes in J774 macrophages. Enrichment of cathepsin H in early endosomes [5].
• The DNA sequence predicts a protein that is closely related to, but distinct from, the lysosomal enzyme cathepsin H [6].

Anatomical context of Ctsh

• IFN-gamma increases cathepsin H mRNA levels in mouse macrophages [7].
• The level of cathepsin H mRNA increased in mouse peritoneal macrophages following addition of IFN-gamma [7].
• Strong cathepsin H staining was sharply defined in theca externa which also stained for cathepsins K and S [8].
• Using immunohistochemistry on BALB/c Peyer's patches, cathepsin H and clusterin expression was increased in the FAE compared to the VE [9].
• The level of cathepsin H was defined in tissue cytosols of human heart, muscle and kidney and in sera from 30 healthy individuals [2].

Associations of Ctsh with chemical compounds

• We have isolated a cDNA clone for cathepsin H, a lysosomal cysteine proteinase from a cDNA subtraction library of mouse macrophage genes induced by IFN-gamma, and have characterized its expression [7].

Other interactions of Ctsh

• Although the exon-intron organization of the mouse cathepsin B gene showed some similarity to the rat cathepsin H and L genes, significant differences were found [10].
• The activities of the cytoplasmic proteases arginyl aminopeptidase and dipeptidyl aminopeptidase IV, and of lysosomal proteases dipeptidyl aminopeptidase II and cathepsin H were not significantly altered following TOCP administration at this higher dosage [11].

References