cathepsin s造句

• Secreted cathepsin S cleaves some extracellular matrix ( ECM ) proteins.
• In contrast, cortical thymic epithelial cells do not express cathepsin S.
• Cathepsin S is produced as a zymogen and is activated by processing.
• Cathepsin S may be considered the most potent elastase known.
• Cathepsin K is degraded by Cathepsin S, called Controlled Cathepsin Cannibalism.
• Chronologically, action of cathepsin S follows two cleavages performed by aspartyl proteases.
• Cathepsin S has a role in nociception, including itch and gastrointestinal pain.
• Cathepsin S is expressed by some epithelial cells.
• While pH optima of many lysosomal proteases are acidic, cathepsin S is an exception.
• In contrast, cathepsin S remains stable and has a physiological role outside the lysosome.
• In vitro, cathepsin S retains some enzyme activity in the presence of 3M urea.
• The expression of cathepsin S can be triggered by proinflammatory factors secreted by tumor cells.
• The list of proposed cathepsin S substrates includes laminin, fibronectin elastin, osteocalcin and some collagens.
• For instance, cleavage of laminin-5 by cathepsin S leads to generation of proangiogenic peptides.
• Cathepsin S is expressed by antigen presenting cells including macrophages, B-lymphocytes, dendritic cells and microglia.
• Cathepsin S plays an active role in blood vessels permeability and angiogenesis due to its elastolytic and collagenolytic activities.
• Cathepsin S participates in the degradation of the invariant or Ii chain that prevents loading the antigen into the complex.
• Immune cells, including macrophages and microglia, secrete cathepsin S in response to inflammatory mediators including lipopolysaccharides, proinflammatory cytokines and neutrophils.
• The activity of cathepsin S is tightly regulated by its endogenous inhibitor, cystatin C, which also has a role in antigen presentation.
• In a special endosome called the MHC II compartment, cathepsin S cleaves the invariant chain, leaving CLIP bound to the MHC II complex.