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Cysteine cathepsins: From structure, function and regulation to new frontiers☆
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
There continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes, so it is important to update guidelines for monitoring autophagic activity in different organisms.
Selective Disruption of Lysosomes in HeLa Cells Triggers Apoptosis Mediated by Cleavage of Bid by Multiple Papain-like Lysosomal Cathepsins*
- T. Cirman, Kristina Oresić, B. Turk
- Biology, ChemistryJournal of Biological Chemistry
- 30 January 2004
It is shown that selective lysosome disruption with l-leucyl-l-leucine methyl ester results in apoptosis, characterized by translocation of lysOSomal proteases into the cytosol and by the cleavage of a proapoptotic Bcl-2-family member Bid.
Lysosomal cysteine proteases: more than scavengers.
The refined 2.4 A X‐ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.
A stoichiometric complex of human stefin B and carboxymethylated papain has been crystallized in a trigonal crystal form and inhibition by the cysteine proteinase inhibitors is fundamentally different to that observed for the serineproteinase inhibitors.
The cystatins: Protein inhibitors of cysteine proteinases
Lysosomal Protease Pathways to Apoptosis
Data suggest that Bid represents a sensor that allows cells to initiate apoptosis in response to widespread adventitious proteolysis, supported by the finding that cytosolic extracts from mice ablated in the bid gene are impaired in the ability to release cytochrome c in Response to lysosome extracts.
The refined 2.15 A X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity.
Monoclinic crystals were obtained which contain two molecules per asymmetric unit and the overall folding pattern of cathepsin B and the arrangement of the active site residues are similar to the related cysteine proteinases papain, actinidin and calotropin DI.
The 2.0 A X‐ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.
Docking experiments suggest a unique model for the interaction of cystatin and papain that seems to be fundamentally different from the ‘standard mechanism’ defined for serine proteinases and most of their protein inhibitors.
Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors.
Among the lysosomal cysteine proteinases, cathepsin L was found to be the most active in degradation of protein substrates, such as collagen, elastin and azocasein, and the most abundant (Kirschke and Barrett, 1981).