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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2005-9-16
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1431-6730
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
386
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
941-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16164419-Amino Acid Sequence,
pubmed-meshheading:16164419-Cathepsin H,
pubmed-meshheading:16164419-Cathepsins,
pubmed-meshheading:16164419-Circular Dichroism,
pubmed-meshheading:16164419-Cysteine Endopeptidases,
pubmed-meshheading:16164419-Enzyme Activation,
pubmed-meshheading:16164419-Enzyme Precursors,
pubmed-meshheading:16164419-Models, Molecular,
pubmed-meshheading:16164419-Molecular Sequence Data,
pubmed-meshheading:16164419-Peptides,
pubmed-meshheading:16164419-Protein Structure, Tertiary
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pubmed:year |
2005
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pubmed:articleTitle |
Activation processing of cathepsin H impairs recognition by its propeptide.
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pubmed:affiliation |
Department of Protein Biochemistry, Institute of Organic Chemistry and Biochemistry, Flemingovo nam. 2, CZ-16610 Praha, Czech Republic.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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