High impact information on Ctss

• A portion of cDNA encoding the predicted mature protein of rat cathepsin S was expressed as a glutathione S-transferase-fusion protein [1].
• Sequence analysis, tissue distribution, and expression of rat cathepsin S [1].
• This sequence encodes an open reading frame of 330 amino acids which is 82% homologous to human cathepsin S, suggesting that this sequence represents rat cathepsin S [1].
• The regulation of expression of rat cathepsin S mRNA in response to thyroid-stimulating hormone was studied in a rat thyroid cell line FRTL-5 [1].
• The most significantly induced transcripts included MHC class II molecules, interferon-gamma inducing factor, apolipoprotein E, and cathepsin S [2].

Biological context of Ctss

• PURPOSE: To investigate the effects of recombinant adenovirus-mediated downregulation of cathepsin S (CatS) on the retinal pigment epithelium and/or neural retina in vivo [3].
• To investigate differences between activities related to phagocytosis in iris pigment epithelial (IPE) and retinal pigment epithelial (RPE) cells, an aspartic protease, cathepsin D (cat D), and a cysteine protease, cathepsin S (cat S), of IPE and RPE were studied [4].
• Cathepsin E and cathepsin S, endosomal/lysosomal proteases, have been shown to play important roles in the major histocompatibility complex (MHC) class II-mediated antigen presentation of microglia by processing of exogenous antigens and degradation of the invariant chain associated with MHC class II molecules, respectively [5].

Associations of Ctss with chemical compounds

• Epoxy succinate peptide derivatives, CLIK-066, 088, 112, 121, 148, 181, 185 and 187, are typical specific inhibitors for cathepsin L. Aldehyde derivatives CLIK-060 and CLIK-164 showed specific inhibition against cathepsin S and cathepsin K, respectively [6].
• To see the physiological role these enzymes play in the brain, we studied the relative abundance and distribution of the messenger RNAs for three lysosomal cysteine proteases, cathepsins B and L and cathepsin S, by in situ hybridization histochemistry in rat brain [7].
• In nephron segments microdissected from lyophilized renal sections, highest cathepsin S activity was found in the proximal convoluted tubules (4.21 mumol/min x g dry weight) followed by 0.83 mumol/min x g dry weight in proximal straight tubules of the superficial cortex [8].
• The stability of cathepsin S at pH 7.5 and the resistance of cathepsin B against inactivation by 0.5 microM Z-Phe-Phe-CHN2 permitted differentiation of these enzyme activities [8].
• New synthetic pyridoxal propionate derivatives, -162, -163, and -164, in which the methyl arm of position 6 of CLIK-071 was additionally modified, strongly inhibited cathepsin K and cathepsin S weakly, but other cathepsins were not inhibited [9].

Regulatory relationships of Ctss

• Results have shown that cathepsin S has been expressed early than the cathepsin H in the nephrogenesis [10].

Other interactions of Ctss

• Unlike cathepsin S activity, the activity of cathepsin B was distributed in parallel to that of cathepsins B + L(+S) [8].

Analytical, diagnostic and therapeutic context of Ctss

• Northern blot analysis for rat cathepsin S revealed tissue-specific expression distinct from the distribution of cathepsin B and L [1].

References