cathepsin d การใช้

• Cathepsin D is an aspartic endo-protease that is ubiquitously distributed in lysosomes.
• Nonetheless, these structures contain endocytic markers even small lysosomal proteins such as cathepsin D.
• Cathepsin D is involved in CLN10.
• The optimum pH for cathepsin D in vitro is 4.5-5.0.
• Cathepsin D ( an aspartyl protease ) appears to cleave a variety of substrates such as fibronectin and laminin.
• Cathepsin D "'is a protein that in humans is encoded by the " CTSD " gene.
• The main function of cathepsin D is to degrade proteins and activate precursors of bioactive proteins in pre-lysosomal compartments.
• Similar to other aspartic protainases, cathepsin D accommodates up to 8 amino acid residues in the binding cleft of the active site.
• Cathepsin D enzymatic activity induces hydrolytic modification of apolipoprotein B-100-containing lipoproteins, including LDL, which means it may be involved in atherosclerosis as well.
• Unlike some of the other cathepsins, cathepsin D has some protease activity at neutral pH . High levels of this enzyme in tumor cells seems to be associated with greater invasiveness.
• Along with renin and Cathepsin D, Cathepsin E is one of the only few aspartic proteases known to be made in human tissues other than those of gastrointestinal and reproductive tracts.
• Over the past two decades, accumulating evidences indicates that NCLs are caused by mutations in eight different genes, including genes encoding several soluble proteins ( cathepsin D, PPT1, and TPP1 ).
• Knock-out of " CTSD " gene would cause intestinal necrosis and hemorrhage and increase apoptosis in thymus, indicating that cathepsin D is required incertain epithelial cells for tissue remodeling and renewal.
• F2L is a naturally occurring acylated peptide derived from the N-terminal sequence of heme-binding protein 1 by cathepsin D cleavage that potently stimulates chemotaxis through FPR3 in monocytes and monocyte-derived dendritic cells.
• It is a member of the peptidase A1 family, and therefore observes specificity similar to that of Pepsin A and Cathepsin D . Cathepsin E is an intracellular enzyme and does not appear to be involved in dietary protein digestion.
• 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.
• Cathepsin B may enhance the activity of other protease, including matrix metalloproteinase, urokinase ( serine protease urokinase plasminogen activator ), and cathepsin D, and thus it has an essential position for in the proteolysis of extracellular matrix components, intercellular communication disruption, and reduced protease inhibitor expression.
• This inhibition seems to be independent of the activities of proteinases such as cathepsin D, because the formation of osteoclasts was not suppressed with the concentration that inhibited the activity of cathepsin D . Cell signaling analysis indicated that the phosphorylation of ERK was inhibited in pepstatin A-treated cells, while the phosphorylation of I?B and Akt showed almost no change.
• This inhibition seems to be independent of the activities of proteinases such as cathepsin D, because the formation of osteoclasts was not suppressed with the concentration that inhibited the activity of cathepsin D . Cell signaling analysis indicated that the phosphorylation of ERK was inhibited in pepstatin A-treated cells, while the phosphorylation of I?B and Akt showed almost no change.