Abstract
An outline is given of the properties and substrate specificities of three lysosomal peptidases, and of efforts to elucidate their potential role in the intracellular degradation of collagen. Use of specific fluorogenic substrates such as Gly-Phe-NNap*, Lys-Ala-NNap and Gly-Pro-Met-NMec allows direct assay of DPP I, DPP II and TPP I respectively. They may hydrolyze macromolecules as exemplified by insulin A and B chains and by poly(Gly-Pro-Ala) as a model collagen α-chain. These are extensively hydrolyzed at acidic pH by the coupled action of the three exopeptidases, which could explain the degradation of proline-rich, collagen-derived polypeptides within lysosomes lacking any known endopeptidases active at prolyl bonds.
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McDonald, J.K., Schwabe, C., Owers, N.O. (1987). Peptidases in Connective Tissue Degradation and Remodelling in Reproductive and Invasive Tissues. In: Reid, E., Cook, G.M.W., Luzio, J.P. (eds) Cells, Membranes, and Disease, Including Renal. Methodological Surveys in Biochemistry and Analysis, vol 17. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1283-3_35
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