Activation processing of cathepsin H impairs recognition by its propeptide
| Autor: | Lucie Dolečková-Marešová, Tudeviin Gan-Erdene, Boris Turk, Olga Vasiljeva, Martin Horn, Miroslav Baudyš, Lubomír Rulíšek, Martin Máša, Michael Mareš |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Cathepsin H Enzyme Precursors Chemistry Circular Dichroism Clinical Biochemistry Molecular Sequence Data Cathepsin E Cathepsin F Biochemistry Cathepsin A Cathepsins Cathepsin B Cathepsin C Protein Structure Tertiary Enzyme Activation Cysteine Endopeptidases Cathepsin O Cathepsin L1 Amino Acid Sequence Peptides Molecular Biology |
| Zdroj: | Biological chemistry. 386(9) |
| ISSN: | 1431-6730 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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