Cathepsin and matrix metalloproteinase (None (commonly: Cathepsin—various abbreviations like CTSB; Matrix metalloproteinase—MMP))

Cathepsins and matrix metalloproteinases are two distinct families of proteolytic enzymes involved in the degradation of cellular and extracellular proteins, respectively. Cathepsins are primarily lysosomal proteases (mainly cysteine proteases, but can also be aspartic or serine proteases) that function in protein turnover, antigen processing, apoptosis, metabolic and immune processes, and under some pathologic conditions are secreted to act extracellularly[3][2]. Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that locally degrade extracellular matrix components and participate in tissue remodeling, cell migration, and the regulation of growth factors and cytokines[1][5][6]. Both enzyme families play key roles in physiological processes such as wound healing and immune regulation, as well as pathologic processes including cancer progression, atherosclerosis, aneurysm formation, arthritis, and neurodegeneration[2][4][5]. Due to their central roles in disease mechanisms, both cathepsins and MMPs are widely studied as therapeutic targets and disease biomarkers, but therapeutic inhibition is complicated by challenges in selectivity and the risk of adverse effects due to their roles in normal physiological tissue remodeling and immune response[2][3][5].

Other names

Cathepsins (e.g. Cathepsin B, Cathepsin S, etc.)MMPsMatrix metallopeptidasesMatrixins

Inhibition of protease activity to prevent extracellular matrix degradation or pathological tissue remodeling; Inhibition of proenzyme activation; Modulation of immune response by interfering with antigen processing (cathepsins)