Activation processing of cathepsin H impairs recognition by its propeptide
Language English Country Germany Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
16164419
DOI
10.1515/bc.2005.109
Knihovny.cz E-resources
- MeSH
- Enzyme Activation MeSH
- Circular Dichroism MeSH
- Cysteine Endopeptidases chemistry metabolism MeSH
- Cathepsin H MeSH
- Cathepsins antagonists & inhibitors chemistry metabolism MeSH
- Models, Molecular MeSH
- Molecular Sequence Data MeSH
- Peptides chemistry metabolism MeSH
- Enzyme Precursors chemistry metabolism MeSH
- Amino Acid Sequence MeSH
- Protein Structure, Tertiary MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Cysteine Endopeptidases MeSH
- Cathepsin H MeSH
- Cathepsins MeSH
- Peptides MeSH
- Enzyme Precursors MeSH
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.
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