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Abstract The lysosomal cysteine peptidases cathepsin B and cathepsin L are abundant and ubiquitously expressed members of the papain family, and both enzymes contribute to the terminal degradation of proteins in the lysosome. However, there is accumulating evidence for specific functions of...
Abstract The carboxypeptidase and endopeptidase activities of cathepsins X and B, as well as their inhibition by E 64 derivatives, have been investigated in detail and compared. The results clearly demonstrate that cathepsins X and B do not share similar activity profiles against substrates and...
Abstract The activation of progelatinase A to gelatinase A requires cleavage of an asparaginyl bond to form the Nterminus of the mature enzyme. We have asked whether the activation can be mediated by legumain, the recently discovered lysosomal cysteine proteinase that is specific for hydrolysis...
Abstract Although papainlike enzymes are strongly inhibited by their natural tightbinding inhibitors of the cystatin superfamily, cathepsins B and L may still retain some residual proteolytic activity toward ZPheArgAMC in the presence of an excess of kininogen. This activity is abolished by...
Abstract The proteolytic enzymes that depend upon a cysteine residue for activity have come from at least seven different evolutionary origins, each of which has produced a group of cysteine peptidases with distinctive structures and properties. We show here that the characteristic molecular...
Abstract The rate of autolysis of and mcalpain from bovine skeletal muscle was measured by using densitometry of SDS polyacrylamide gels and determining the rate of disappearance of the 28 and 80 kDa subunits of the native, unautolyzed calpain molecules. Rate of autolysis of both the 28 and 80...
Abstract The properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata. Both peptidases were purified to homogeneity by acetone precipitation followed by...
Abstract Thyroglobulin, the precursor of thyroid hormones, is extracellularly stored in a highly condensed and covalently crosslinked form. Solublization of thyroglobulin is facilitated by cysteine proteinases like cathepsins B and K which are proteolytically active at the surface of thyroid...
Abstract It has been suggested that the lysosomal proteinases cathepsin B, L and D participate in tumour invasion and metastasis. Whereas for cathepsins B and L the role of active enzyme in invasion processes has been confirmed, cathepsin D was suggested to support tumour progression via its...
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