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  Processing and Maturation of Cathepsin C Zymogen: A Biochemical and Molecular Modeling Analysis

Lamort, A.-S., Hamon, Y., Czaplewski, C., Gieldon, A., Seren, S., Coquet, L., et al. (2019). Processing and Maturation of Cathepsin C Zymogen: A Biochemical and Molecular Modeling Analysis. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 20(19): 4747. doi:10.3390/ijms20194747.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-5AC6-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-5AC7-6
Genre: Journal Article

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 Creators:
Lamort, Anne-Sophie1, Author
Hamon, Yveline1, Author
Czaplewski, Cezary1, Author
Gieldon, Artur1, Author
Seren, Seda1, Author
Coquet, Laurent1, Author
Lecaille, Fabien1, Author
Lesner, Adam1, Author
Lalmanach, Gilles1, Author
Gauthier, Francis1, Author
Jenne, Dieter E.2, Author              
Korkmaz, Brice1, Author
Affiliations:
1external, ou_persistent22              
2Research Group: Enzymes and Inhibitors in Chronic Lung Disease / Jenne, MPI of Neurobiology, Max Planck Society, ou_1950284              

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Free keywords: PAPILLON-LEFEVRE-SYNDROME; CRYSTAL-STRUCTURE; MUTATIONS; GENE; PROTEINASE-3; INHIBITORS; PROTEASES; DYNAMICS; REVEALS; TARGETSBiochemistry & Molecular Biology; Chemistry; Cathepsin C; cysteine cathepsin; zymogen; zymogen processing;
 Abstract: 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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Language(s): eng - English
 Dates: 2019
 Publication Status: Published online
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000494798300088
DOI: 10.3390/ijms20194747
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Title: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Source Genre: Journal
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Publ. Info: ST ALBAN-ANLAGE 66, CH-4052 BASEL, SWITZERLAND : MDPI
Pages: - Volume / Issue: 20 (19) Sequence Number: 4747 Start / End Page: - Identifier: -