What does cathepsin d do?
What does cathepsin d do?
Cathepsin D is one of a family of cathepsin proteins that act as protease enzymes, which modify proteins by cutting them apart. Cathepsin D is found in many types of cells and is active in lysosomes, which are compartments within cells that digest and recycle different types of molecules.
Is cathepsin a lysosomal enzymes?
Cathepsin D is the main lysosomal enzyme involved in the degradation of α-synuclein and generation of its carboxy-terminally truncated species. To whom correspondence should be addressed: Department of Neuroscience, Mayo Clinic College of Medicine, 4500 San Pablo Road, Jacksonville, FL 32224, USA.
Is cathepsin D an enzyme?
Cathepsin D is a protein that in humans is encoded by the CTSD gene. Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes. The main function of cathepsin D is to degrade proteins and activate precursors of bioactive proteins in pre-lysosomal compartments.
What is the purpose of proteases?
The function of proteases is to catalyze the hydrolysis of proteins, which has been exploited for the production of high-value protein hydrolysates from different sources of proteins such as casein, whey, soy protein and fish meat.
What are the physiological functions of cathepsin D?
The main physiological functions of cathepsin D consist of metabolic degradation of intracellular proteins, activation and degradation of polypeptide hormones and growth factors, activation of enzymatic precursors, processing of enzyme activators and inhibitors, brain antigen processing and regulation of programmed cell death.
What happens to cathepsin D gene in mice?
Although disruption of the cathepsin D gene in mice leads to postnatal lethality, general lysosomal protein degradation appears to be largely unimpaired in fibroblasts from these animals (Saftig et al., 1995 ), indicating that cathepsin D may not be required for general intracellular protein turnover in lysosomes.
What kind of precursors can cathepsin D cleave?
Cathepsin D can cleave endothelin and its precursors, tachykinin and enkephalin precursors, but its function as the normal processing enzyme for these precursors must be evaluated in the light of other proteinases that have been purified and which appear to function in this regard (Chapters 35, 110 and 111 ).
How does over expression of cathepsin D affect breast cancer?
Over-expression of cathepsin D stimulates tumorigenicity and metastasis as well as initiation of tumor apoptosis. This protease has been regarded an independent marker of poor prognosis in breast cancer being correlated with the incidence of clinical metastasis.