High impact information on CTSL

• This finding in turn indicated that the protease for which MAG was a substrate had cathepsin L-like activity [1].
• Cathepsin L-like activity in myelin was confirmed by peptidolysis experiments using known cathepsin L substrates [1].
• 0. Cathepsin S was found to hydrolyse proteins at a similar rate to cathepsin L below pH 7 [2].
• We show that proBac7 is a monocyte-selective chemoattractant, potentially contributing to the recruitment of these cells to infection sites, whereas proBac5 efficiently inhibits the in vitro activity of cathepsin L, a cysteine proteinase thought to contribute to tissue injury in inflammation [3].
• The results strongly suggest the involvement of cathepsin B- and cathepsin L-like proteinases in the histolysis of the silk gland during metamorphosis [4].

Biological context of CTSL

• N-terminal amino acid sequence confirms that cathepsin L and cathepsin S are different enzymes [5].
• Based on pH profiles of activity, inhibition studies using diethylpyrocarbonate and the diazomethylketone Z-phe-ala-CHN2, and characterising the substrate specificity of the enzymes using fluorogenic peptide substrates we have shown that the 60-90-kDa proteinases are cathepsin L-like proteinases [6].
• Although to a varying extent, P1, P2 and P3 inhibited papain, cathepsin B and cathepsin L. Analysis of the peptide mixtures of these inhibitors by RP-HPLC after hydrolysis with CNBr or aspartly endoproteinase N together with their amino acid composition revealed that P1, P2 and P3 cysteine proteinase inhibitors are isoforms of the same protein [7].
• Antibody responses to the 28-30 kDa proteins were not detected in groups B-D until 3 weeks later than those observed in group A. Antibody responses to Fasciola hepatica cathepsin L proteases, which are known to induce protection, were monophasic, of the IgG1 isotype only and were not observed prior to secondary challenge in any of the four groups [8].

Anatomical context of CTSL

• Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15) [9].
• Secondly, we studied whether MPRs transport cathepsin L to autophagic vacuoles directly from the TGN [10].
• Purification and characterization of a new potential in vivo inhibitor of cathepsin L from bovine skeletal muscle [11].

Associations of CTSL with chemical compounds

• The appearance of higher molecular-sized components in the cathepsin L clots suggests that polymerisation involves the formation of molecular interactions that are resistant to boiling in mercaptoethanol and SDS [12].
• Also, PTP does not exhibit dipeptidycarboxylpeptidase activity, a property of cathepsin B; PTP demonstrates no elastinolytic activity, a characteristic of cathepsin L. Importantly, the sensitivity of PTP to active-site-directed peptide diazomethane inhibitors and E-64c differs from that of cathepsins B, L, and H [13].
• Both were rapidly inhibited by low concentrations of E-64 or leupeptin, but were unaffected by cathepsin-L-specific inhibitor Z-Phe-Phe-CHN2 [14].

Other interactions of CTSL

• Human and bovine brain cathepsin L and cathepsin H: purification, physico-chemical properties, and specificity [15].

Analytical, diagnostic and therapeutic context of CTSL

• Cathepsin L was purified from bovine kidney by acid treatment and incubation of 37 degrees C, precipitation by (NH4)2SO4, two ion exchange chromatographies on CM-Sephadex, gel chromatography and ion exchange chromatography on FPLC system [5].
• Induction of protective immunity in cattle against infection with Fasciola hepatica by vaccination with cathepsin L proteinases and with hemoglobin [16].
• The sensitivity of the cathepsin L ELISA for sheep and cattle sera was 99.1 and 100%, respectively [17].
• SDS/PAGE analysis of the cathepsin-L-produced clots revealed that cleavage of the alpha polypeptide (66 kDa) precedes that of the beta (52 kDa) and gamma (46.5 kDa) polypeptides [12].
• Quantitative immunocytochemistry showed that neither of these drugs prevented cathepsin L delivery to autophagic vacuoles [10].

References