Plant Phenolics Inhibit Neutrophil Elastase
Abstract Human neutrophil elastase (HNE) is a serine protease, which is present in its active form in inflamed tissue as well as in psoriatic lesions. In extension of our research on natural compounds as inhibitors of HNE or of its release, several phenolics of different size were tested. The ellagi...
Gespeichert in:
| Veröffentlicht in: | Planta medica 2006-10, Vol.72 (12), p.1127-1131 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1131 |
|---|---|
| container_issue | 12 |
| container_start_page | 1127 |
| container_title | Planta medica |
| container_volume | 72 |
| creator | Hrenn, A Steinbrecher, T Labahn, A Schwager, J Schempp, C.M Merfort, I |
| description | Abstract
Human neutrophil elastase (HNE) is a serine protease, which is present in its active form in inflamed tissue as well as in psoriatic lesions. In extension of our research on natural compounds as inhibitors of HNE or of its release, several phenolics of different size were tested. The ellagitannins agrimoniin and pedunculagin were the most potent direct HNE inhibitors (IC
50
= 0.9 and 2.8 μM, respectively). Ligand docking calculations provided evidence that inhibition may occur in an unspecific manner. Agrimoniin also showed anti-proliferative effects in the ATP assay (IC
50
= 3.2 μM), suggesting that this type of tannin could have beneficial effects in the treatment of diseases such as psoriasis. Tests with other phenolics combined with ligand docking experiments revealed that, besides the presence of ORTHO-dihydroxy groups, a specific lipophilic shape is necessary for an inhibitory activity. The phenolic genistein deserves special interest as an inhibitor of elastase release because its effect was remarkably potent (IC
50
= 0.6 μM). |
| doi_str_mv | 10.1055/s-2006-946700 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68928544</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>68928544</sourcerecordid><originalsourceid>FETCH-LOGICAL-c382t-c2093ba3148fa96c50a8a201fa1fa41d477dd697cbe04ad5df70253553413b8d3</originalsourceid><addsrcrecordid>eNp10M9LwzAUwPEgipvTo1ftRS9affnVJkcZUwdDB7pzSNPUVrp2Ju3B_96MFnYyBHL58PL4InSJ4QED548-JgBJLFmSAhyhKWZUxkAIPkZTAEpikIxO0Jn33wCYSYBTNMEpEMaFnKK7da2bLlqXtmnryvho2ZRVVnXRm-071-7Kqo4Wtfad9vYcnRS69vZifGdo87z4nL_Gq_eX5fxpFRsqSBcbApJmmmImCi0Tw0ELTQAXOlyGc5ameZ7I1GQWmM55XoRtOOWcMkwzkdMZuh3m7lz701vfqW3lja3DprbtvUqEJIIzFmA8QONa750t1M5VW-1-FQa1r6O82tdRQ53gr8bBfba1-UGPOQK4GYH2RteF042p_MEJLFPC9u5-cF1Z2a1V323vmpDk33-vB17oVukvF0ZuPkIRCjgcmRD6Bz6SgZQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>68928544</pqid></control><display><type>article</type><title>Plant Phenolics Inhibit Neutrophil Elastase</title><source>MEDLINE</source><source>Thieme Connect Journals</source><creator>Hrenn, A ; Steinbrecher, T ; Labahn, A ; Schwager, J ; Schempp, C.M ; Merfort, I</creator><creatorcontrib>Hrenn, A ; Steinbrecher, T ; Labahn, A ; Schwager, J ; Schempp, C.M ; Merfort, I</creatorcontrib><description>Abstract
Human neutrophil elastase (HNE) is a serine protease, which is present in its active form in inflamed tissue as well as in psoriatic lesions. In extension of our research on natural compounds as inhibitors of HNE or of its release, several phenolics of different size were tested. The ellagitannins agrimoniin and pedunculagin were the most potent direct HNE inhibitors (IC
50
= 0.9 and 2.8 μM, respectively). Ligand docking calculations provided evidence that inhibition may occur in an unspecific manner. Agrimoniin also showed anti-proliferative effects in the ATP assay (IC
50
= 3.2 μM), suggesting that this type of tannin could have beneficial effects in the treatment of diseases such as psoriasis. Tests with other phenolics combined with ligand docking experiments revealed that, besides the presence of ORTHO-dihydroxy groups, a specific lipophilic shape is necessary for an inhibitory activity. The phenolic genistein deserves special interest as an inhibitor of elastase release because its effect was remarkably potent (IC
50
= 0.6 μM).</description><identifier>ISSN: 0032-0943</identifier><identifier>EISSN: 1439-0221</identifier><identifier>DOI: 10.1055/s-2006-946700</identifier><identifier>PMID: 17024589</identifier><identifier>CODEN: PLMEAA</identifier><language>eng</language><publisher>Stuttgart: Thieme</publisher><subject>agrimoniin ; Biological and medical sciences ; Catechin - analogs & derivatives ; Catechin - pharmacology ; cultured cells ; elastase ; enzyme inhibition ; enzyme inhibitors ; General pharmacology ; Genistein - pharmacology ; Humans ; Hydrolyzable Tannins - pharmacology ; Leukocyte Elastase - antagonists & inhibitors ; Medical sciences ; neutrophils ; Original Paper ; pedunculagin ; Pharmacognosy. Homeopathy. Health food ; Pharmacology. Drug treatments ; phenolic compounds ; Phenols - pharmacology ; Phenylethyl Alcohol - analogs & derivatives ; Phenylethyl Alcohol - pharmacology ; Plant Extracts - chemistry ; plant products ; Proteinase Inhibitory Proteins, Secretory - analysis ; Stilbenes - pharmacology ; structure-activity relationships</subject><ispartof>Planta medica, 2006-10, Vol.72 (12), p.1127-1131</ispartof><rights>Georg Thieme Verlag KG Stuttgart · New York</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c382t-c2093ba3148fa96c50a8a201fa1fa41d477dd697cbe04ad5df70253553413b8d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.thieme-connect.de/products/ejournals/pdf/10.1055/s-2006-946700.pdf$$EPDF$$P50$$Gthieme$$H</linktopdf><linktohtml>$$Uhttps://www.thieme-connect.de/products/ejournals/html/10.1055/s-2006-946700$$EHTML$$P50$$Gthieme$$H</linktohtml><link.rule.ids>314,776,780,3003,3004,27903,27904,54537,54538</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18197249$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17024589$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hrenn, A</creatorcontrib><creatorcontrib>Steinbrecher, T</creatorcontrib><creatorcontrib>Labahn, A</creatorcontrib><creatorcontrib>Schwager, J</creatorcontrib><creatorcontrib>Schempp, C.M</creatorcontrib><creatorcontrib>Merfort, I</creatorcontrib><title>Plant Phenolics Inhibit Neutrophil Elastase</title><title>Planta medica</title><addtitle>Planta Med</addtitle><description>Abstract
Human neutrophil elastase (HNE) is a serine protease, which is present in its active form in inflamed tissue as well as in psoriatic lesions. In extension of our research on natural compounds as inhibitors of HNE or of its release, several phenolics of different size were tested. The ellagitannins agrimoniin and pedunculagin were the most potent direct HNE inhibitors (IC
50
= 0.9 and 2.8 μM, respectively). Ligand docking calculations provided evidence that inhibition may occur in an unspecific manner. Agrimoniin also showed anti-proliferative effects in the ATP assay (IC
50
= 3.2 μM), suggesting that this type of tannin could have beneficial effects in the treatment of diseases such as psoriasis. Tests with other phenolics combined with ligand docking experiments revealed that, besides the presence of ORTHO-dihydroxy groups, a specific lipophilic shape is necessary for an inhibitory activity. The phenolic genistein deserves special interest as an inhibitor of elastase release because its effect was remarkably potent (IC
50
= 0.6 μM).</description><subject>agrimoniin</subject><subject>Biological and medical sciences</subject><subject>Catechin - analogs & derivatives</subject><subject>Catechin - pharmacology</subject><subject>cultured cells</subject><subject>elastase</subject><subject>enzyme inhibition</subject><subject>enzyme inhibitors</subject><subject>General pharmacology</subject><subject>Genistein - pharmacology</subject><subject>Humans</subject><subject>Hydrolyzable Tannins - pharmacology</subject><subject>Leukocyte Elastase - antagonists & inhibitors</subject><subject>Medical sciences</subject><subject>neutrophils</subject><subject>Original Paper</subject><subject>pedunculagin</subject><subject>Pharmacognosy. Homeopathy. Health food</subject><subject>Pharmacology. Drug treatments</subject><subject>phenolic compounds</subject><subject>Phenols - pharmacology</subject><subject>Phenylethyl Alcohol - analogs & derivatives</subject><subject>Phenylethyl Alcohol - pharmacology</subject><subject>Plant Extracts - chemistry</subject><subject>plant products</subject><subject>Proteinase Inhibitory Proteins, Secretory - analysis</subject><subject>Stilbenes - pharmacology</subject><subject>structure-activity relationships</subject><issn>0032-0943</issn><issn>1439-0221</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10M9LwzAUwPEgipvTo1ftRS9affnVJkcZUwdDB7pzSNPUVrp2Ju3B_96MFnYyBHL58PL4InSJ4QED548-JgBJLFmSAhyhKWZUxkAIPkZTAEpikIxO0Jn33wCYSYBTNMEpEMaFnKK7da2bLlqXtmnryvho2ZRVVnXRm-071-7Kqo4Wtfad9vYcnRS69vZifGdo87z4nL_Gq_eX5fxpFRsqSBcbApJmmmImCi0Tw0ELTQAXOlyGc5ameZ7I1GQWmM55XoRtOOWcMkwzkdMZuh3m7lz701vfqW3lja3DprbtvUqEJIIzFmA8QONa750t1M5VW-1-FQa1r6O82tdRQ53gr8bBfba1-UGPOQK4GYH2RteF042p_MEJLFPC9u5-cF1Z2a1V323vmpDk33-vB17oVukvF0ZuPkIRCjgcmRD6Bz6SgZQ</recordid><startdate>20061001</startdate><enddate>20061001</enddate><creator>Hrenn, A</creator><creator>Steinbrecher, T</creator><creator>Labahn, A</creator><creator>Schwager, J</creator><creator>Schempp, C.M</creator><creator>Merfort, I</creator><general>Thieme</general><scope>FBQ</scope><scope>IQODW</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>20061001</creationdate><title>Plant Phenolics Inhibit Neutrophil Elastase</title><author>Hrenn, A ; Steinbrecher, T ; Labahn, A ; Schwager, J ; Schempp, C.M ; Merfort, I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c382t-c2093ba3148fa96c50a8a201fa1fa41d477dd697cbe04ad5df70253553413b8d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>agrimoniin</topic><topic>Biological and medical sciences</topic><topic>Catechin - analogs & derivatives</topic><topic>Catechin - pharmacology</topic><topic>cultured cells</topic><topic>elastase</topic><topic>enzyme inhibition</topic><topic>enzyme inhibitors</topic><topic>General pharmacology</topic><topic>Genistein - pharmacology</topic><topic>Humans</topic><topic>Hydrolyzable Tannins - pharmacology</topic><topic>Leukocyte Elastase - antagonists & inhibitors</topic><topic>Medical sciences</topic><topic>neutrophils</topic><topic>Original Paper</topic><topic>pedunculagin</topic><topic>Pharmacognosy. Homeopathy. Health food</topic><topic>Pharmacology. Drug treatments</topic><topic>phenolic compounds</topic><topic>Phenols - pharmacology</topic><topic>Phenylethyl Alcohol - analogs & derivatives</topic><topic>Phenylethyl Alcohol - pharmacology</topic><topic>Plant Extracts - chemistry</topic><topic>plant products</topic><topic>Proteinase Inhibitory Proteins, Secretory - analysis</topic><topic>Stilbenes - pharmacology</topic><topic>structure-activity relationships</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hrenn, A</creatorcontrib><creatorcontrib>Steinbrecher, T</creatorcontrib><creatorcontrib>Labahn, A</creatorcontrib><creatorcontrib>Schwager, J</creatorcontrib><creatorcontrib>Schempp, C.M</creatorcontrib><creatorcontrib>Merfort, I</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</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>Planta medica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hrenn, A</au><au>Steinbrecher, T</au><au>Labahn, A</au><au>Schwager, J</au><au>Schempp, C.M</au><au>Merfort, I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Plant Phenolics Inhibit Neutrophil Elastase</atitle><jtitle>Planta medica</jtitle><addtitle>Planta Med</addtitle><date>2006-10-01</date><risdate>2006</risdate><volume>72</volume><issue>12</issue><spage>1127</spage><epage>1131</epage><pages>1127-1131</pages><issn>0032-0943</issn><eissn>1439-0221</eissn><coden>PLMEAA</coden><abstract>Abstract
Human neutrophil elastase (HNE) is a serine protease, which is present in its active form in inflamed tissue as well as in psoriatic lesions. In extension of our research on natural compounds as inhibitors of HNE or of its release, several phenolics of different size were tested. The ellagitannins agrimoniin and pedunculagin were the most potent direct HNE inhibitors (IC
50
= 0.9 and 2.8 μM, respectively). Ligand docking calculations provided evidence that inhibition may occur in an unspecific manner. Agrimoniin also showed anti-proliferative effects in the ATP assay (IC
50
= 3.2 μM), suggesting that this type of tannin could have beneficial effects in the treatment of diseases such as psoriasis. Tests with other phenolics combined with ligand docking experiments revealed that, besides the presence of ORTHO-dihydroxy groups, a specific lipophilic shape is necessary for an inhibitory activity. The phenolic genistein deserves special interest as an inhibitor of elastase release because its effect was remarkably potent (IC
50
= 0.6 μM).</abstract><cop>Stuttgart</cop><cop>New York, NY</cop><pub>Thieme</pub><pmid>17024589</pmid><doi>10.1055/s-2006-946700</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0032-0943 |
| ispartof | Planta medica, 2006-10, Vol.72 (12), p.1127-1131 |
| issn | 0032-0943 1439-0221 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68928544 |
| source | MEDLINE; Thieme Connect Journals |
| subjects | agrimoniin Biological and medical sciences Catechin - analogs & derivatives Catechin - pharmacology cultured cells elastase enzyme inhibition enzyme inhibitors General pharmacology Genistein - pharmacology Humans Hydrolyzable Tannins - pharmacology Leukocyte Elastase - antagonists & inhibitors Medical sciences neutrophils Original Paper pedunculagin Pharmacognosy. Homeopathy. Health food Pharmacology. Drug treatments phenolic compounds Phenols - pharmacology Phenylethyl Alcohol - analogs & derivatives Phenylethyl Alcohol - pharmacology Plant Extracts - chemistry plant products Proteinase Inhibitory Proteins, Secretory - analysis Stilbenes - pharmacology structure-activity relationships |
| title | Plant Phenolics Inhibit Neutrophil Elastase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-25T09%3A29%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Plant%20Phenolics%20Inhibit%20Neutrophil%20Elastase&rft.jtitle=Planta%20medica&rft.au=Hrenn,%20A&rft.date=2006-10-01&rft.volume=72&rft.issue=12&rft.spage=1127&rft.epage=1131&rft.pages=1127-1131&rft.issn=0032-0943&rft.eissn=1439-0221&rft.coden=PLMEAA&rft_id=info:doi/10.1055/s-2006-946700&rft_dat=%3Cproquest_cross%3E68928544%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=68928544&rft_id=info:pmid/17024589&rfr_iscdi=true |