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Lamort, A.-S. ; Hamon, Y.* ; Czaplewski, C.* ; Gieldon, A.* ; Seren, S.* ; Coquet, L.* ; Lecaille, F.* ; Lesner, A.* ; Lalmanach, G.* ; Gauthier, F.* ; Jenne, D. ; Korkmaz, B.*

Processing and maturation of cathepsin C zymogen: A biochemical and molecular modeling analysis.

Int. J. Mol. Sci. 20:4747 (2019)

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Cysteine cathepsin C (CatC) is a ubiquitously expressed, lysosomal aminopeptidase involved in the activation of zymogens of immune-cell-associated serine proteinases (elastase, cathepsin G, proteinase 3, neutrophil serine proteinase 4, lymphocyte granzymes, and mast cell chymases). CatC is first synthetized as an inactive zymogen containing an intramolecular chain propeptide, the dimeric form of which is processed into the mature tetrameric form by proteolytic cleavages. A molecular modeling analysis of proCatC indicated that its propeptide displayed a similar fold to those of other lysosomal cysteine cathepsins, and could be involved in dimer formation. Our in vitro experiments revealed that human proCatC was processed and activated by CatF, CatK, and CatV in two consecutive steps of maturation, as reported for CatL and CatS previously. The unique positioning of the propeptide domains in the proCatC dimer complex allows this order of cleavages to be understood. The missense mutation Leu172Pro within the propeptide region associated with the Papillon-Lefevre and Haim-Munk syndrome altered the proform stability as well as the maturation of the recombinant Leu172Pro proform.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Cathepsin C ; Cysteine Cathepsin ; Zymogen ; Zymogen Processing; Papillon-lefevre-syndrome; Crystal-structure; Mutations; Gene; Proteinase-3; Inhibitors; Proteases; Dynamics; Reveals; Targets

ISSN (print) / ISBN 1422-0067

e-ISSN 1661-6596

Journal International Journal of Molecular Sciences

Quellenangaben Volume: 20, Issue: 19, Article Number: 4747

Publisher MDPI

Publishing Place Basel

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Lung Health and Immunity (LHI)