Cathepsin B Function describes the specific biological roles executed by the lysosomal cysteine protease Cathepsin B, a key enzyme in cellular homeostasis. Its primary function involves the controlled degradation of endogenous and exogenous proteins within the lysosome, essential for cellular waste disposal and nutrient recycling. Furthermore, Cathepsin B participates in critical non-lysosomal processes, including antigen presentation, pro-hormone processing, and the controlled initiation of certain cell death pathways. Proper function is integral to maintaining the delicate balance of protein turnover and overall cellular vitality, particularly in hormone-sensitive tissues.
Origin
The functional understanding of Cathepsin B stems from decades of research in cellular biochemistry and lysosomal biology, establishing it as a fundamental component of the cell’s proteolytic machinery. Its name, derived from the Greek for “to digest,” reflects its core role in catabolism. In endocrinology, its significance is highlighted by its involvement in processing precursor molecules into active peptide hormones, linking cellular digestion to systemic signaling.
Mechanism
Functionally, Cathepsin B cleaves peptide bonds with a preference for certain amino acid sequences, acting as a proteolytic enzyme. Within the cell, it is synthesized as an inactive pro-enzyme and subsequently activated upon transport to the acidic lysosome. Outside the lysosome, under conditions of cellular stress or inflammation, its release can trigger pathways like inflammasome activation, linking lysosomal health directly to the broader immune and metabolic response, profoundly affecting the hormonal milieu.
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