Activation of cathepsin D by glycosaminoglycans

Cysteine Cathepsin Activity Regulation by Glycosaminoglycans

Cysteine cathepsins are a group of enzymes normally found in the endolysosomes where they are primarily involved in intracellular protein turnover but also have a critical role in MHC II-mediated antigen processing and presentation. However, in a number of pathologies cysteine cathepsins were found to be heavily upregulated and secreted into extracellular milieu, where they were found to degrad...

Regulation of Cathepsin D Activity and Activation

Inhibition of cathepsin D by synthetic oligopeptides.

A number of synthetic oligopeptides with the COOH terminus D-amino acid situated third from the potentially cleavable phenylalanyl-phenylalanyl bond, typified by < Glu-D-Phe-Pro-Phe-Phe-Val-D-Trp (Peptide VI) were shown to be potent competitive inhibitors of cathepsin D and pepsin. Peptide VI, which forms an equimolar nonproductive enzyme l inhibitor complex, inhibited the hydrolysis of methyl[...

Cathepsin D Processing Differently Affected by Cathepsin B and Chemokine/CC Chemokine Ligand 20 Is Function of Liver Activation-Regulated

ATP activation of parathyroid hormone cleavage catalyzed by cathepsin D from bovine kidney.

The acid protease which is activated by ATP and which catalyzes production of fragments of parathyroid hormone similar to those produced in vivo was shown to be cathepsin D. Purified cathepsin D from bovine kidney and spleen is activated by ATP and other nucleoside triphosphates, and to a much lesser extent by nucleoside diphosphates and pyrophosphate. These findings suggest that cathepsin D ma...