Cathepsin D

Cathepsin D

Target · Lysosomal protease

Cathepsin D Cathepsin D · lysosomal aspartyl protease

Cathepsin D (CTSD) is an acid protease of the peptidase A1 family that is active in intracellular protein breakdown. It is also known as CLN10 and CPSD, and was previously named cathepsin D (lysosomal aspartyl protease). Browse Assay Genie's current range of Cathepsin D research reagents below, or read on for the biology behind the target.

Lysosomal and secretedPepsin-like aspartyl proteaseLinked to CLN10 disease
412 aa
Protein length
~45 kDa
Molecular weight
11p15.5
Gene locus
EC 3.4.23.5
Enzyme class
Target information

What is Cathepsin D (cathepsin D)?

Cathepsin D is an acid protease that functions in intracellular protein breakdown. The enzyme shows pepsin-like activity and contributes to protein turnover and to the proteolytic activation of hormones and growth factors. It also has a role in amyloid precursor protein (APP) processing: following cleavage and activation by ADAM30, cathepsin D leads to APP degradation.

The CTSD gene encodes a member of the A1 family of peptidases. The encoded preproprotein is proteolytically processed into several products, including the cathepsin D light and heavy chains, which heterodimerise to form the mature enzyme. UniProt lists the protein in the lysosome, the melanosome and the extracellular space, where it is found in secreted form. The mouse and rat orthologs are both named Ctsd, which allows comparative work in rodent models.

Cathepsin D belongs to the HGNC gene groups Cathepsins and Peptidase family A1. Mutations in the cathepsin D gene play a causal role in neuronal ceroid lipofuscinosis-10, which accounts for the alias CLN10. The protein is also involved in the pathogenesis of several other diseases, including breast cancer and possibly Alzheimer disease, and so is studied in both neurodegeneration and cancer biology.

Lysosomal protein turnover

Cathepsin D is an acid protease active in intracellular protein breakdown, making it a central enzyme for studying lysosomal degradation and protein turnover.

Neuronal ceroid lipofuscinosis

Mutations in the cathepsin D gene play a causal role in neuronal ceroid lipofuscinosis-10 (CLN10), linking the enzyme to lysosomal storage disease research.

Alzheimer disease and APP

Following activation by ADAM30, cathepsin D contributes to APP degradation and is possibly involved in Alzheimer disease pathogenesis.

Breast cancer biology

Cathepsin D is involved in the pathogenesis of breast cancer, and its role in activating hormones and growth factors is of interest in tumour research.

Background

Cathepsin D frequently asked questions

What does Cathepsin D do?

Cathepsin D is an acid protease active in intracellular protein breakdown. It has pepsin-like activity and contributes to protein turnover and the proteolytic activation of hormones and growth factors. After cleavage and activation by ADAM30, it also participates in APP processing, leading to APP degradation.

What are the other names and forms of Cathepsin D?

The gene symbol is CTSD, with aliases CLN10 and CPSD. An earlier name was cathepsin D (lysosomal aspartyl protease). The preproprotein is processed into several products, including light and heavy chains that heterodimerise to form the mature enzyme.

Is Cathepsin D linked to disease, and is it conserved in rodents?

Mutations in the gene cause neuronal ceroid lipofuscinosis-10, and the protein is involved in breast cancer and possibly Alzheimer disease. Mouse and rat both have a Ctsd ortholog; check the datasheet of any product for its validated reactivity.

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Related targets

Other cathepsins, APP-processing partners and lysosomal protease targets with products at Assay Genie.

Gene and protein annotations from HGNC, NCBI Gene and UniProt P07339; product specifications from Assay Genie datasheets.

Cathepsin D Product listing