All parasitic protozoa contain multiple proteases, some of which are attracting attention as drug targets.
The activated resident cells and the recruited inflammatory (M1) macrophages release toxic ROS that destroy invading pathogens [78,79] and induce the expression of genes encoding various cytokines, inflammatory molecules and multiple proteases including MMPs, serine and cysteine proteases, and elastases.
Multiple proteases of Pseudomonas aeruginosa (AprA, LasA, LasB, and protease IV) also are involved in disease pathogenesis.
We observed differential expression of multiple proteases, and di- and oligopeptide transport systems (Table 6).
The next strategy investigated was the use of multiple proteases.
Recombinant GST-His-tagged PPAD was digested by multiple proteases.
As with other proteases that perform RIP, bioactivation of the substrate is a multi-step process, involving multiple proteases.
Multiple proteases, including the ubiquitin-proteasome system, lysosomal proteases, and calcium-dependent calpains, are involved in skeletal muscle atrophy.
FN can also be degraded by multiple proteases including MMP-9 [ 217].
Multiple proteases, including cathepsins B, E, H, L, and S, and serine-type peptidase, were identified.
