
Cathepsin D is a lysosomal aspartic protease of the pepsin family. Mouse Cathepsin D is synthesized as a precursor protein, consisting of a signal peptide (residues 120), a propeptide (residues 21-64), and a mature chain (residues 65-410). It is expressed in most cells and overexpressed in breast cancer cells. It is a major enzyme in protein degradation in lysosomes, and also involved in the presentation of antigenic peptides. Mice deficient in this enzyme showed a progressive atrophy of the intestinal mucosa, a massive destruction of lymphoid organs, and a profound neuronal ceroid lipofucinosis, indicating that Cathepsin D is essential for proteolysis of proteins regulating cell growth and tissue homeostasis. Cathepsin D secreted from human prostate carcinoma cells is responsible for the generation of angiostatin, a potent endogeneous inhibitor of angiogenesis.
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