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Martin Horn, Lucie Dole?ková-Mare?ová, Lubomír Rulí?ek, Martin Má?a, Olga Vasiljeva, Boris Turk, Tudeviin Gan-Erdene, Miroslav Baudy?, Michael Mare?

Activation processing of cathepsin H impairs recognition by its propeptide

Keywords: aminopeptidase, cysteine peptidase, inhibition, maturation, mini-chain

Free propeptides are known to function as inhibitors of the parental mature cysteine cathepsins. This general rule, however, does not apply to the aminopeptidase cathepsin H. Screening of propeptide fragments for their inhibitory potency revealed no significant effect on the native mature cathepsin H. On the other hand, inhibitory interaction was established with recombinant cathepsin H that displays endopeptidase activity due to a lack of the mini-chain. This finding suggests that the propeptide-binding region is structurally rearranged during maturation processing and mini-chain formation, which impairs the effective recognition of mature cathepsin H by its own propeptide.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 386, 09/2005
Pages: 941 - 947

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