Smooth muscle cell (SMC) migration from the tunica media to the intima, a key event in
neointimal formation, requires proteolytic degradation of elastin-rich extracellular matrix …

Cathepsin K has emerged as a promising target for the treatment of osteoporosis in recent
years. Initially identified as a papain-like cysteine peptidase expressed in high levels in …

During chronic kidney disease (CKD) there is a dysregulation of extracellular matrix (ECM)
homeostasis leading to renal fibrosis. Lysosomal proteases such as cathepsins (Cts) …

Cysteine cathepsins are lysosomal proteases with housekeeping as well as highly
specialized functions. Although their activities are optimal at lysosomal acidic and reducing …

The lysosomal cysteine peptidase cathepsin L (CTSL) is an important lysosomal proteinase
involved in a variety of cellular functions including intracellular protein turnover, epidermal …

Human cysteine proteases of the papain family have been recognized as potential drug
targets for musculoskeletal diseases. Most of the interest is focused on cathepsins S and K …

Proteolysis of extracellular matrix components and the production of cryptic bioactive factors
play key roles in vascular remodeling. We showed previously that extracellular matrix …

Objective—The development of abdominal aortic aneurysms (AAA) requires extensive aortic
wall matrix degradation. Human AAA lesions express high levels of cathepsin L (CatL), one …

During atherogenesis, low density lipoprotein (LDL) particles in the arterial intima become
modified and fuse to form extracellular lipid droplets. Proteolytic modification of …

Background—Lysosomal carboxypeptidase, cathepsin A (protective protein, CathA), is a
component of the lysosomal multienzyme complex along with β-galactosidase (GAL) and …