| pubmed-article:19181662 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19181662 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:19181662 | lifeskim:mentions | umls-concept:C0057256 | lld:lifeskim |
| pubmed-article:19181662 | lifeskim:mentions | umls-concept:C0166059 | lld:lifeskim |
| pubmed-article:19181662 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:19181662 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:19181662 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:19181662 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
| pubmed-article:19181662 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:19181662 | pubmed:dateCreated | 2009-3-23 | lld:pubmed |
| pubmed-article:19181662 | pubmed:abstractText | Proteolytic processing of defensins is a critical mode of posttranslational regulation of peptide activity. Because mouse alpha-defensin precursors are cleaved and activated by matrix metalloproteinase-7 (MMP-7), we determined if additional defensin molecules, namely human neutrophil defensin pro-HNP-1 and beta-defensins, are targets for MMP-7. We found that MMP-7 cleaves within the pro-domain of the HNP-1 precursor, a reaction that does not generate the mature peptide but produces a 59-amino acid intermediate. This intermediate, which retains the carboxyl-terminal end of the pro-domain, had antimicrobial activity, indicating that the residues important for masking defensin activity reside in the amino terminus of this domain. Mature HNP-1 was resistant to processing by MMP-7 unless the peptide was reduced and alkylated, demonstrating that only the pro-domain of alpha-defensins is normally accessible for cleavage by this enzyme. From the 47-residue HBD-1 precursor, MMP-7 catalyzed removal of 6 amino acids from the amino terminus. Neither a 39-residue intermediate form of HBD-1 nor the mature 36-residue form of HBD-1 was cleaved by MMP-7. In addition, both pro-HBD-2, with its shorter amino-terminal extension, and pro-HBD-3 were resistant to MMP-7. However, human and mouse beta-defensin precursors that lack disulfide bonding contain a cryptic MMP-7-sensitive site within the mature peptide moiety. These findings support and extend accumulating evidence that the native three-dimensional structure of both alpha- and beta-defensins protects the mature peptides against proteolytic processing by MMP-7. We also conclude that sites for MMP-7 cleavage are more common at the amino termini of alpha-defensin rather than beta-defensin precursors, and that catalysis at these sites in alpha-defensin pro-domains results in acquisition of defensin activity. | lld:pubmed |
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| pubmed-article:19181662 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19181662 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19181662 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19181662 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19181662 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19181662 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:19181662 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:19181662 | pubmed:author | pubmed-author:WilsonCarole... | lld:pubmed |
| pubmed-article:19181662 | pubmed:author | pubmed-author:GanzTomasT | lld:pubmed |
| pubmed-article:19181662 | pubmed:author | pubmed-author:ParksWilliam... | lld:pubmed |
| pubmed-article:19181662 | pubmed:author | pubmed-author:ValoreErika... | lld:pubmed |
| pubmed-article:19181662 | pubmed:author | pubmed-author:SorsaTimoT | lld:pubmed |
| pubmed-article:19181662 | pubmed:author | pubmed-author:FerriNicolaN | lld:pubmed |
| pubmed-article:19181662 | pubmed:author | pubmed-author:PiriläEmmaE | lld:pubmed |
| pubmed-article:19181662 | pubmed:author | pubmed-author:SchmidtAmy... | lld:pubmed |
| pubmed-article:19181662 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19181662 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:19181662 | pubmed:volume | 284 | lld:pubmed |
