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Article: Sputum sol neutrophil elastase activity in bronchiectasis: Differential modulation by syndecan-1

TitleSputum sol neutrophil elastase activity in bronchiectasis: Differential modulation by syndecan-1
Authors
Keywordsα1-antitrypsin
Heparan sulfate proteoglycans
Proteinase
Secretory leukoproteinase inhibitor
Issue Date2003
PublisherAmerican Thoracic Society. The Journal's web site is located at http://ajrccm.atsjournals.org
Citation
American Journal Of Respiratory And Critical Care Medicine, 2003, v. 168 n. 2, p. 192-198 How to Cite?
AbstractThe persistently dominant activity of neutrophil elastase in bronchial secretions replete with antielastases is crucial to the pathogenesis of bronchiectasis. We hypothesize that components in the bronchial secretions bind neutrophil elastase and compromise the inhibitory efficiency of prevailing antielastases. Zymographic analysis of sputum sols from patients with bronchiectasis found elastase activity in a polydisperse, alcian blue-stained zone of high molecular mass. This suggested that neutrophil elastase was complexed with polyanionic partners. Western blot analysis found not only the polyanionic partner, heparan sulfate/syndecan-1, but also the physiological antielastases, secretory leukoproteinase inhibitor and α1-antitrypsin, in the complex. Both dissociative density gradient ultracentrifugation and heparin displacement revealed that elastase dissociated from heparan sulfate/syndecan-1 was fully inhibited by the endogenous antielastases. This contrasts with the effects of exogenous antielastases on sputum neutrophil elastase activity - that of α1-antitrypsin was limited, but that of secretory leukoproteinase inhibitor was facilitated. Similarly, complexed elastase on blots of sputum sol zymographs was bound and inhibited by exogenous secretory leukoproteinase inhibitor but not by exogenous α1-antitrypsin. Taken together, the results bring a new focus to heparan sulfate/syndecan-1 complexed with neutrophil elastase in inflamed bronchial secretions as a target for modulating elastase susceptibility to physiological antielastases.
Persistent Identifierhttp://hdl.handle.net/10722/68227
ISSN
2015 Impact Factor: 13.118
2015 SCImago Journal Rankings: 5.832
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, SCHen_HK
dc.contributor.authorShum, DKYen_HK
dc.contributor.authorIp, MSMen_HK
dc.date.accessioned2010-09-06T06:02:34Z-
dc.date.available2010-09-06T06:02:34Z-
dc.date.issued2003en_HK
dc.identifier.citationAmerican Journal Of Respiratory And Critical Care Medicine, 2003, v. 168 n. 2, p. 192-198en_HK
dc.identifier.issn1073-449Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/68227-
dc.description.abstractThe persistently dominant activity of neutrophil elastase in bronchial secretions replete with antielastases is crucial to the pathogenesis of bronchiectasis. We hypothesize that components in the bronchial secretions bind neutrophil elastase and compromise the inhibitory efficiency of prevailing antielastases. Zymographic analysis of sputum sols from patients with bronchiectasis found elastase activity in a polydisperse, alcian blue-stained zone of high molecular mass. This suggested that neutrophil elastase was complexed with polyanionic partners. Western blot analysis found not only the polyanionic partner, heparan sulfate/syndecan-1, but also the physiological antielastases, secretory leukoproteinase inhibitor and α1-antitrypsin, in the complex. Both dissociative density gradient ultracentrifugation and heparin displacement revealed that elastase dissociated from heparan sulfate/syndecan-1 was fully inhibited by the endogenous antielastases. This contrasts with the effects of exogenous antielastases on sputum neutrophil elastase activity - that of α1-antitrypsin was limited, but that of secretory leukoproteinase inhibitor was facilitated. Similarly, complexed elastase on blots of sputum sol zymographs was bound and inhibited by exogenous secretory leukoproteinase inhibitor but not by exogenous α1-antitrypsin. Taken together, the results bring a new focus to heparan sulfate/syndecan-1 complexed with neutrophil elastase in inflamed bronchial secretions as a target for modulating elastase susceptibility to physiological antielastases.en_HK
dc.languageengen_HK
dc.publisherAmerican Thoracic Society. The Journal's web site is located at http://ajrccm.atsjournals.orgen_HK
dc.relation.ispartofAmerican Journal of Respiratory and Critical Care Medicineen_HK
dc.subjectα1-antitrypsinen_HK
dc.subjectHeparan sulfate proteoglycansen_HK
dc.subjectProteinaseen_HK
dc.subjectSecretory leukoproteinase inhibitoren_HK
dc.subject.meshBlotting, Westernen_HK
dc.subject.meshBronchiectasis - enzymologyen_HK
dc.subject.meshFemaleen_HK
dc.subject.meshHeparitin Sulfate - metabolismen_HK
dc.subject.meshHumansen_HK
dc.subject.meshLeukocyte Elastase - metabolismen_HK
dc.subject.meshMaleen_HK
dc.subject.meshMembrane Glycoproteins - metabolismen_HK
dc.subject.meshMiddle Ageden_HK
dc.subject.meshProteinase Inhibitory Proteins, Secretoryen_HK
dc.subject.meshProteins - metabolismen_HK
dc.subject.meshProteoglycans - metabolismen_HK
dc.subject.meshSerine Proteinase Inhibitors - metabolismen_HK
dc.subject.meshSputum - enzymologyen_HK
dc.subject.meshSyndecan-1en_HK
dc.subject.meshSyndecansen_HK
dc.subject.meshalpha 1-Antitrypsin - metabolismen_HK
dc.titleSputum sol neutrophil elastase activity in bronchiectasis: Differential modulation by syndecan-1en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1073-449X&volume=168&issue=2&spage=192&epage=198&date=2003&atitle=Sputum+sol+neutrophil+elastase+activity+in+bronchiectasis:+differential+modulation+by+syndecan-1+en_HK
dc.identifier.emailShum, DKY:shumdkhk@hkucc.hku.hken_HK
dc.identifier.emailIp, MSM:msmip@hku.hken_HK
dc.identifier.authorityShum, DKY=rp00321en_HK
dc.identifier.authorityIp, MSM=rp00347en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1164/rccm.200208-829OCen_HK
dc.identifier.pmid12702549-
dc.identifier.scopuseid_2-s2.0-0043033174en_HK
dc.identifier.hkuros95193en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0043033174&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume168en_HK
dc.identifier.issue2en_HK
dc.identifier.spage192en_HK
dc.identifier.epage198en_HK
dc.identifier.isiWOS:000184082000012-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChan, SCH=35261745200en_HK
dc.identifier.scopusauthoridShum, DKY=7004824447en_HK
dc.identifier.scopusauthoridIp, MSM=7102423259en_HK

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