Disease relevance of CTSS

• Cathepsin S was purified from bovine spleen by acid autolysis, (NH4)2SO4 fractionation and chromatography on CM-Sephadex C-50, CM-cellulose and activated-thiol-Sepharose [1].

High impact information on CTSS

• 0. Cathepsin S was found to hydrolyse proteins at a similar rate to cathepsin L below pH 7 [2].
• Cathepsin S was detected in bovine kidney, spleen, lymph nodes and lung by immunochemical methods [2].
• The immunostaining of cathepsin S in kidney was concentrated to the cells of the proximal tubule, where the enzyme was present in cytoplasmic granules [2].
• Kinetics of inhibition of bovine cathepsin S by bovine stefin B [3].
• The complete amino acid sequence of bovine spleen cathepsin S has been determined [4].

Biological context of CTSS

• N-terminal amino acid sequence confirms that cathepsin L and cathepsin S are different enzymes [5].
• The open reading frame in these overlapping clones correctly predicts the determined amino acid sequence of 13 tryptic peptides derived from purified bovine spleen cathepsin S [6].

Anatomical context of CTSS

• Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15) [1].
• CCh decreased total cysteine protease and cathepsin S activities in the isolated lysosome, redistributing them to early endocytic and biosynthetic compartments [7].

Associations of CTSS with chemical compounds

• The purification procedure of cathepsin S includes acid activation of spleen homogenate, incubation at 37 degrees C, precipitation with (NH4)2SO4 in H2O/tert-butanol medium, gel chromatography, chromatofocusing, covalent chromatography and cation chromatography of FPLC system [5].

Enzymatic interactions of CTSS

• A significant characteristic of cathepsin S is that it can hydrolyze insoluble elastin at both acidic and neutral pH; this distinguishes it from all of the other lysosomal proteinases [8].
• They could however be distinguished by the fact that cathepsin S reacted with Z-[125I]Tyr-Ala-CHN2 and hydrolyzed Z-Phe-Arg-NHMec whereas cathepsin H did not [8].

Analytical, diagnostic and therapeutic context of CTSS

• Using polymerase chain reaction (PCR) technology, cDNA clones commencing at amino acid 22 of the mature enzyme and continuing through the 3' untranslated region of bovine cathepsin S mRNA were isolated and sequenced [6].

References