Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA
It has been shown previously that DNA binds and inhibits neutrophil elastase (NE). Here we demonstrate that DNA has a better affinity for neutrophil cathepsin G (cat G) than for NE and is a better inhibitor of cat G than of NE. DNase-generated
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| Veröffentlicht in: | FEBS letters 2000-05, Vol.473 (2), p.154-156 |
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| creator | Duranton, Jérôme Belorgey, Didier Carrère, Jacqueline Donato, Lionel Moritz, Thomas Bieth, Joseph G. |
| description | It has been shown previously that DNA binds and inhibits neutrophil elastase (NE). Here we demonstrate that DNA has a better affinity for neutrophil cathepsin G (cat G) than for NE and is a better inhibitor of cat G than of NE. DNase-generated |
| doi_str_mv | 10.1016/S0014-5793(00)01512-X |
| format | Article |
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Here we demonstrate that DNA has a better affinity for neutrophil cathepsin G (cat G) than for NE and is a better inhibitor of cat G than of NE. DNase-generated <0.5 kb DNA fragments inhibit NE and cat G as potently as full length DNA. This rationalises our observation that administration of DNase to cystic fibrosis patients does not enhance the NE and cat G activity of their lung secretions. Neutrophil proteinase 3 is not inhibited by DNA and might thus be the most harmful proteinase in inflammatory lung diseases.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(00)01512-X</identifier><identifier>PMID: 10812064</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Binding, Competitive ; cat G, neutrophil cathepsin G ; Cathepsin G ; Cathepsins - drug effects ; Cathepsins - metabolism ; Cellulose ; Chromatography, Affinity ; Cystic fibrosis ; Cystic Fibrosis - drug therapy ; Cystic Fibrosis - enzymology ; Deoxyribonucleases - metabolism ; Deoxyribonucleases - pharmacology ; Deoxyribonucleases - therapeutic use ; DNA ; DNA - metabolism ; DNA - pharmacology ; DNase ; Elastase ; Elastin - metabolism ; Humans ; Leukocyte Elastase - drug effects ; Leukocyte Elastase - metabolism ; Lung - drug effects ; Lung - enzymology ; Lung - metabolism ; Myeloblastin ; NE, neutrophil elastase ; Neutrophils - enzymology ; Oligonucleotides - metabolism ; Oligonucleotides - pharmacology ; PR3, neutrophil proteinase 3 ; Proteinase 3 ; Serine Endopeptidases - drug effects ; Serine Endopeptidases - metabolism</subject><ispartof>FEBS letters, 2000-05, Vol.473 (2), p.154-156</ispartof><rights>2000 Federation of European Biochemical Societies</rights><rights>FEBS Letters 473 (2000) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525X-c08ec95e53d86ff65cef2e10fb471838747375ea0a7878f1ed2a26d9ea2d90053</citedby><cites>FETCH-LOGICAL-c525X-c08ec95e53d86ff65cef2e10fb471838747375ea0a7878f1ed2a26d9ea2d90053</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2800%2901512-X$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(00)01512-X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1416,1432,3548,27922,27923,45572,45573,45993,46407,46831</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10812064$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Duranton, Jérôme</creatorcontrib><creatorcontrib>Belorgey, Didier</creatorcontrib><creatorcontrib>Carrère, Jacqueline</creatorcontrib><creatorcontrib>Donato, Lionel</creatorcontrib><creatorcontrib>Moritz, Thomas</creatorcontrib><creatorcontrib>Bieth, Joseph G.</creatorcontrib><title>Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>It has been shown previously that DNA binds and inhibits neutrophil elastase (NE). Here we demonstrate that DNA has a better affinity for neutrophil cathepsin G (cat G) than for NE and is a better inhibitor of cat G than of NE. DNase-generated <0.5 kb DNA fragments inhibit NE and cat G as potently as full length DNA. This rationalises our observation that administration of DNase to cystic fibrosis patients does not enhance the NE and cat G activity of their lung secretions. Neutrophil proteinase 3 is not inhibited by DNA and might thus be the most harmful proteinase in inflammatory lung diseases.</description><subject>Binding, Competitive</subject><subject>cat G, neutrophil cathepsin G</subject><subject>Cathepsin G</subject><subject>Cathepsins - drug effects</subject><subject>Cathepsins - metabolism</subject><subject>Cellulose</subject><subject>Chromatography, Affinity</subject><subject>Cystic fibrosis</subject><subject>Cystic Fibrosis - drug therapy</subject><subject>Cystic Fibrosis - enzymology</subject><subject>Deoxyribonucleases - metabolism</subject><subject>Deoxyribonucleases - pharmacology</subject><subject>Deoxyribonucleases - therapeutic use</subject><subject>DNA</subject><subject>DNA - metabolism</subject><subject>DNA - pharmacology</subject><subject>DNase</subject><subject>Elastase</subject><subject>Elastin - metabolism</subject><subject>Humans</subject><subject>Leukocyte Elastase - drug effects</subject><subject>Leukocyte Elastase - metabolism</subject><subject>Lung - drug effects</subject><subject>Lung - enzymology</subject><subject>Lung - metabolism</subject><subject>Myeloblastin</subject><subject>NE, neutrophil elastase</subject><subject>Neutrophils - enzymology</subject><subject>Oligonucleotides - metabolism</subject><subject>Oligonucleotides - pharmacology</subject><subject>PR3, neutrophil proteinase 3</subject><subject>Proteinase 3</subject><subject>Serine Endopeptidases - drug effects</subject><subject>Serine Endopeptidases - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFu1DAQhi0EotvCI4B8QlQiMBPHsXNCpWxbpAoOgLQ3y3XGqiGbpHa2aN8eZ1MhbnCy7Pn8z-gbxl4gvEXA-t1XAKwKqRrxGuAUUGJZbB6xFWolClHV-jFb_UGO2HFKPyDfNTZP2RGCxhLqasV-rr0nN_HB84-fbSI-9Hy6JW7dFO7DtJ8LPe2mOIy3oePU2TRl7A13NmNjCj2_5LZv-RiHiUI_RwgelpAxUqLe0ZJ-9ow98bZL9PzhPGHfL9bfzq-K6y-Xn87PrgsnS7kpHGhyjSQpWl17X0tHviQEf1Mp1EKrSgklyYJVWmmP1Ja2rNuGbNk2AFKcsFdLbp7pbkdpMtuQHHWd7WnYJaMQUTQaMygX0MUhpUjejDFsbdwbBDNbNgfLZlZoAMzBstnkfy8fGuxuttT-9WvRmoGrBfgVOtr_X6q5WH8oD5W5MO8qP8-93i9RlI3dB4omuTBLbUPMizPtEP4x7W-d8Z-_</recordid><startdate>20000512</startdate><enddate>20000512</enddate><creator>Duranton, Jérôme</creator><creator>Belorgey, Didier</creator><creator>Carrère, Jacqueline</creator><creator>Donato, Lionel</creator><creator>Moritz, Thomas</creator><creator>Bieth, Joseph G.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20000512</creationdate><title>Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA</title><author>Duranton, Jérôme ; Belorgey, Didier ; Carrère, Jacqueline ; Donato, Lionel ; Moritz, Thomas ; Bieth, Joseph G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525X-c08ec95e53d86ff65cef2e10fb471838747375ea0a7878f1ed2a26d9ea2d90053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Binding, Competitive</topic><topic>cat G, neutrophil cathepsin G</topic><topic>Cathepsin G</topic><topic>Cathepsins - drug effects</topic><topic>Cathepsins - metabolism</topic><topic>Cellulose</topic><topic>Chromatography, Affinity</topic><topic>Cystic fibrosis</topic><topic>Cystic Fibrosis - drug therapy</topic><topic>Cystic Fibrosis - enzymology</topic><topic>Deoxyribonucleases - metabolism</topic><topic>Deoxyribonucleases - pharmacology</topic><topic>Deoxyribonucleases - therapeutic use</topic><topic>DNA</topic><topic>DNA - metabolism</topic><topic>DNA - pharmacology</topic><topic>DNase</topic><topic>Elastase</topic><topic>Elastin - metabolism</topic><topic>Humans</topic><topic>Leukocyte Elastase - drug effects</topic><topic>Leukocyte Elastase - metabolism</topic><topic>Lung - drug effects</topic><topic>Lung - enzymology</topic><topic>Lung - metabolism</topic><topic>Myeloblastin</topic><topic>NE, neutrophil elastase</topic><topic>Neutrophils - enzymology</topic><topic>Oligonucleotides - metabolism</topic><topic>Oligonucleotides - pharmacology</topic><topic>PR3, neutrophil proteinase 3</topic><topic>Proteinase 3</topic><topic>Serine Endopeptidases - drug effects</topic><topic>Serine Endopeptidases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Duranton, Jérôme</creatorcontrib><creatorcontrib>Belorgey, Didier</creatorcontrib><creatorcontrib>Carrère, Jacqueline</creatorcontrib><creatorcontrib>Donato, Lionel</creatorcontrib><creatorcontrib>Moritz, Thomas</creatorcontrib><creatorcontrib>Bieth, Joseph G.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Duranton, Jérôme</au><au>Belorgey, Didier</au><au>Carrère, Jacqueline</au><au>Donato, Lionel</au><au>Moritz, Thomas</au><au>Bieth, Joseph G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2000-05-12</date><risdate>2000</risdate><volume>473</volume><issue>2</issue><spage>154</spage><epage>156</epage><pages>154-156</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>It has been shown previously that DNA binds and inhibits neutrophil elastase (NE). Here we demonstrate that DNA has a better affinity for neutrophil cathepsin G (cat G) than for NE and is a better inhibitor of cat G than of NE. DNase-generated <0.5 kb DNA fragments inhibit NE and cat G as potently as full length DNA. This rationalises our observation that administration of DNase to cystic fibrosis patients does not enhance the NE and cat G activity of their lung secretions. Neutrophil proteinase 3 is not inhibited by DNA and might thus be the most harmful proteinase in inflammatory lung diseases.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>10812064</pmid><doi>10.1016/S0014-5793(00)01512-X</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; Alma/SFX Local Collection |
| subjects | Binding, Competitive cat G, neutrophil cathepsin G Cathepsin G Cathepsins - drug effects Cathepsins - metabolism Cellulose Chromatography, Affinity Cystic fibrosis Cystic Fibrosis - drug therapy Cystic Fibrosis - enzymology Deoxyribonucleases - metabolism Deoxyribonucleases - pharmacology Deoxyribonucleases - therapeutic use DNA DNA - metabolism DNA - pharmacology DNase Elastase Elastin - metabolism Humans Leukocyte Elastase - drug effects Leukocyte Elastase - metabolism Lung - drug effects Lung - enzymology Lung - metabolism Myeloblastin NE, neutrophil elastase Neutrophils - enzymology Oligonucleotides - metabolism Oligonucleotides - pharmacology PR3, neutrophil proteinase 3 Proteinase 3 Serine Endopeptidases - drug effects Serine Endopeptidases - metabolism |
| title | Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA |
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