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Cathepsin D is a ubiquitously expressed lysosomal aspartyl protease involved in the normal degradation of proteins. It is synthesized as an inactive 43kDa preprocathepsin D that is cleaved and glycosylated to form a 46kDa procathepsin D and then further cleaved to produce 28kDa and 15kDa subunits (heavy and light chains, respectively). Cathepsin D exhibits pepsin-like activity and plays a role in protein turnover and in the proteolytic activation of hormones and growth factors. Mutations in this gene play a causal role in neuronal ceroid lipofuscinosis-10 and may be involved in the pathogenesis of several other diseases, including breast cancer and possibly Alzheimer's disease.
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