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Cathepsin D is a lysosomal aspartic protease of the pepsin family (4). Mouse Cathepsin D is synthesized as a precursor protein, consisting of a signal peptide (residues 1‑20), a propeptide (residues 21‑64), and a mature chain (residues 65‑410) (1‑3). It is expressed in most cells and overexpressed in breast cancer cells (5). 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 (6). Cathepsin D secreted from human prostate carcinoma cells is responsible for the generation of angiostatin, a potent endogeneous inhibitor of angiogenesis (6).

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