2008
DOI: 10.1016/j.biochi.2007.09.007
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Multifaceted roles of human elafin and secretory leukocyte proteinase inhibitor (SLPI), two serine protease inhibitors of the chelonianin family

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Cited by 169 publications
(192 citation statements)
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“…By contrast to all other epitopes we identified, the CLB12.8 epitope is unique in that it is occluded or altered by a1-PI binding and is very close to the active site region. Elafin, another physiological peptide inhibitor of PR3, binds noncovalently in a canonical manner to PR3 (34). As it consists only of 57 residues, the anticipated substrate-like contacts between elafin and PR3 are fewer and are restricted to the S5 to S29 pockets.…”
Section: Discussionmentioning
confidence: 99%
“…By contrast to all other epitopes we identified, the CLB12.8 epitope is unique in that it is occluded or altered by a1-PI binding and is very close to the active site region. Elafin, another physiological peptide inhibitor of PR3, binds noncovalently in a canonical manner to PR3 (34). As it consists only of 57 residues, the anticipated substrate-like contacts between elafin and PR3 are fewer and are restricted to the S5 to S29 pockets.…”
Section: Discussionmentioning
confidence: 99%
“…The HE4 gene resides on human chromosome 20q12-13.1, a region that harbors a locus of 14 genes encoding protein domains that have homology with whey acidic protein (WAP) (3). Two functions attributed to this family of proteins are the regulation of proinflammatory mediators and anti-bacterial or anti-fungal activity (4,5). There is a growing body of evidence demonstrating the tumorpromoting roles of WAP domain family members (6,7).…”
Section: Introductionmentioning
confidence: 99%
“…The expression of PI3 gene can be induced by proinflammatory cytokines (IL-1b, TNF-a), bacterial lipopolysaccharides, and elastase (5-7), and there is constitutive expression in airways and other mucosal sites where the inflammatory stimuli persist (8). In contrast to other protease inhibitors, such as secretory leukocyte proteinase inhibitor and a 1 -antitrypsin, PI3 has a narrower spectrum of inhibition specifically toward HNE (9). Moreover, PI3 protein has a unique molecular structure comprising two domains, including a carboxy-terminal whey acidic protein (WAP) domain containing the antiprotease active site and an aminoterminal domain (38 residues) containing several transglutaminase substrate motifs characterized by hexapeptide repeats with a consensus sequence GQDPVK (10,11).…”
mentioning
confidence: 99%