Cathepsin and elastase

Cathepsins and elastases are distinct families of proteolytic enzymes that are often studied together due to their synergistic roles in tissue remodeling and inflammation. Cathepsins are primarily lysosomal proteases, categorized into cysteine (e.g., Cathepsin B, L, K), aspartic (e.g., Cathepsin D), and serine (e.g., Cathepsin G) proteases, involved in protein turnover and immune signaling (UniProt, 2023). Elastases, specifically neutrophil elastase (ELANE), are serine proteases secreted by activated neutrophils to degrade extracellular matrix proteins like elastin (PubMed, 2021). In diseases such as chronic obstructive pulmonary disease (COPD) and cystic fibrosis, an overabundance of these proteases leads to excessive lung tissue destruction and chronic inflammation (NIH, 2022). Additionally, Cathepsin L and elastase-like proteases are critical for the entry of certain viruses, including coronaviruses, by processing viral glycoproteins to facilitate membrane fusion (Nature, 2020). Therapeutic interventions include specific inhibitors like sivelestat for elastase or odanacatib for cathepsin K, though broad-spectrum protease inhibition remains a challenge due to potential off-target effects on normal physiological processes (PubChem, 2023).

Other names

ProteasesLysosomal proteasesNeutrophil elastase and cathepsin familyProteolytic enzymes

Protease inhibition; competitive or non-competitive binding to the enzyme active site to prevent substrate cleavage.