Abstract
Lysosomal proteases belong to the aspartic, cysteine, or serine proteinase families of hydrolytic enzymes. They are expressed ubiquitously, and in a tissue- or cell type-specific manner. Although we still call them lysosomal proteases, the enzymes are usually detected within all vesicles of the endocytic pathway. In specific cell types, they might even become secreted and might fulfill important tasks in the direct pericellular surrounding. Functions of lysosomal proteases comprise bulk protein degradation within lysosomes, antigen processing within early endosomes, proprotein processing at unexpected locations such as secretory vesicles, prohormone processing and degradation of matrix constituents in the extracellular space, and, most recently, lysosomal proteases have been proposed to contribute to the initiation of apoptotic processes within the cytosol. Many of these functions were determined through the use of cathepsin-deficient mice which also demonstrated the redundancy of some cathepsins, i.e., those belonging to the cysteine proteinases. Challenges for future research on lysosomal proteases are to uncover more of their in vivo substrates and to clarify where and which of the many enzymes are essential for the maintenance of vital functions of cells, tissues, or organs.
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Brix, K. (2005). Lysosomal Proteases. In: Lysosomes. Medical Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-28957-7_5
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DOI: https://doi.org/10.1007/0-387-28957-7_5
Publisher Name: Springer, Boston, MA
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