<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Small DM</submitter><funding>Public Health Agency</funding><pagination>24-31</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4426794</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>23(1)</volume><pubmed_abstract>Elafin is a serine protease inhibitor produced by epithelial and immune cells with anti-inflammatory properties. Research has shown that dysregulated protease activity may elicit proteolytic cleavage of elafin, thereby impairing the innate immune function of the protein. The aim of this study was to generate variants of elafin (GG- and QQ-elafin) that exhibit increased protease resistance while retaining the biological properties of wild-type (WT) elafin. Similar to WT-elafin, GG- and QQ-elafin variants retained antiprotease activity and susceptibility to transglutaminase-mediated fibronectin cross-linking. However, in contrast to WT-elafin, GG- and QQ-elafin displayed significantly enhanced resistance to degradation when incubated with bronchoalveolar lavage fluid from patients with cysti</pubmed_abstract><journal>Molecular therapy : the journal of the American Society of Gene Therapy</journal><pubmed_title>A functional variant of elafin with improved anti-inflammatory activity for pulmonary inflammation.</pubmed_title><pmcid>PMC4426794</pmcid><funding_grant_id>CDV/3778/08</funding_grant_id><funding_grant_id>COM/4275/10</funding_grant_id><pubmed_authors>Small DM</pubmed_authors><pubmed_authors>Quinn DJ</pubmed_authors><pubmed_authors>Weldon S</pubmed_authors><pubmed_authors>Glasgow AM</pubmed_authors><pubmed_authors>Zani ML</pubmed_authors><pubmed_authors>Dallet-Choisy S</pubmed_authors><pubmed_authors>McAuley DF</pubmed_authors><pubmed_authors>Taggart CC</pubmed_authors><pubmed_authors>McNally P</pubmed_authors><pubmed_authors>O'Kane C</pubmed_authors><pubmed_authors>Moreau T</pubmed_authors></additional><is_claimable>false</is_claimable><name>A functional variant of elafin with improved anti-inflammatory activity for pulmonary inflammation.</name><description>Elafin is a serine protease inhibitor produced by epithelial and immune cells with anti-inflammatory properties. Research has shown that dysregulated protease activity may elicit proteolytic cleavage of elafin, thereby impairing the innate immune function of the protein. The aim of this study was to generate variants of elafin (GG- and QQ-elafin) that exhibit increased protease resistance while retaining the biological properties of wild-type (WT) elafin. Similar to WT-elafin, GG- and QQ-elafin variants retained antiprotease activity and susceptibility to transglutaminase-mediated fibronectin cross-linking. However, in contrast to WT-elafin, GG- and QQ-elafin displayed significantly enhanced resistance to degradation when incubated with bronchoalveolar lavage fluid from patients with cysti</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Jan</publication><modification>2025-04-04T07:30:30.85Z</modification><creation>2019-03-27T01:51:21Z</creation></dates><accession>S-EPMC4426794</accession><cross_references><pubmed>25189740</pubmed><doi>10.1038/mt.2014.162</doi></cross_references></HashMap>