Inhibition by Alkylamines of NADPH Oxidase Through Blocking the Assembly of Enzyme Components
Alkylamines inhibit NADPH oxidase both in intact neutrophils and in a cell-free system. The aim of this study was to examine the mechanism underlying this inhibitory effect. Among alkylamines with different chain lengths, the C12 compound (laurylamine) showed the greatest inhibitory effect on the ce...
Gespeichert in:
| Veröffentlicht in: | Japanese Journal of Pharmacology 1999, Vol.80(3), pp.237-242 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 242 |
|---|---|
| container_issue | 3 |
| container_start_page | 237 |
| container_title | Japanese Journal of Pharmacology |
| container_volume | 80 |
| creator | Sawai, Tohru Asada, Makoto Nishizawa, Yukio Nunoi, Hiroyuki Katayama, Kouichi |
| description | Alkylamines inhibit NADPH oxidase both in intact neutrophils and in a cell-free system. The aim of this study was to examine the mechanism underlying this inhibitory effect. Among alkylamines with different chain lengths, the C12 compound (laurylamine) showed the greatest inhibitory effect on the cell-free NADPH oxidase activity induced by arachidonic acid (AA) in the presence of GTPγS. The inhibition was overcome by further addition of AA, and it was observed irrespective of whether laurylamine was added before or after the enzyme activation by AA. When added prior to the enzyme activation, laurylamine blocked translocation to the membrane of all three cytosolic components (p47-phox, p67-phox and rac) in a cell-free translocation assay. When added after the activation, laurylamine released only rac from the membrane. Laurylamine did not inhibit the reduction of cytochrome c by xanthine oxidase, suggesting that it does not have superoxide-scavenging activity. These results indicate that laurylamine inhibits both the activation process of NADPH oxidase and the activated enzyme itself by blocking the assembly of the oxidase components. |
| doi_str_mv | 10.1254/jjp.80.237 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69983145</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021519819308480</els_id><sourcerecordid>69983145</sourcerecordid><originalsourceid>FETCH-LOGICAL-c675t-d6952bf05b58a7f0cf1272a4732c15b9e91fe9c23383ebf85d0c5eb2448468f93</originalsourceid><addsrcrecordid>eNptkE1v1DAQhiMEokvhwg9AOXFA2sWfiX1Cy9LSShXlUI7IcpzJxqljL3aCWH49XqVFHLh4ZM3jxzNvUbzGaIMJZ--H4bARaENo_aRYYcrqNeWoelqsECJ4zbEUZ8WLlIZ8FQiz58UZRqzCdSVXxfdr39vGTjb4sjmWW3d_dHq0HlIZuvLL9tPXq_L2l211gvKuj2He9-VHF8y99fty6qHcpgRj444n_ML_Po5Q7sJ4CB78lF4WzzrtErx6qOfFt8uLu93V-ub28_Vue7M2Vc2ndVtJTpoO8YYLXXfIdJjURLOaEoN5I0HiDqQhlAoKTSd4iwyHhjAmWCU6Sc-Lt4v3EMOPGdKkRpsMOKc9hDmpSkpBMeMZfLeAJoaUInTqEO2o41FhpE5hqhymEkjlMDP85sE6NyO0_6BLehm4XIDctUa74F1OTg1hjj6vq0xXDUM4OIWllAohgRA9FYWyPh8sb0QIpln0YRENadJ7-PuTjpM1Dh6HostxevzYMb2OCnw2sMUAOeafFqJKxoI3ebAIZlJtsP9b8Q_Uwq6H</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69983145</pqid></control><display><type>article</type><title>Inhibition by Alkylamines of NADPH Oxidase Through Blocking the Assembly of Enzyme Components</title><source>J-STAGE Free</source><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Sawai, Tohru ; Asada, Makoto ; Nishizawa, Yukio ; Nunoi, Hiroyuki ; Katayama, Kouichi</creator><creatorcontrib>Sawai, Tohru ; Asada, Makoto ; Nishizawa, Yukio ; Nunoi, Hiroyuki ; Katayama, Kouichi ; Eisai Tsukuba Research Laboratories ; Department of Pediatrics ; Kumamoto University School of Medicine ; Department of Drug Discovery</creatorcontrib><description>Alkylamines inhibit NADPH oxidase both in intact neutrophils and in a cell-free system. The aim of this study was to examine the mechanism underlying this inhibitory effect. Among alkylamines with different chain lengths, the C12 compound (laurylamine) showed the greatest inhibitory effect on the cell-free NADPH oxidase activity induced by arachidonic acid (AA) in the presence of GTPγS. The inhibition was overcome by further addition of AA, and it was observed irrespective of whether laurylamine was added before or after the enzyme activation by AA. When added prior to the enzyme activation, laurylamine blocked translocation to the membrane of all three cytosolic components (p47-phox, p67-phox and rac) in a cell-free translocation assay. When added after the activation, laurylamine released only rac from the membrane. Laurylamine did not inhibit the reduction of cytochrome c by xanthine oxidase, suggesting that it does not have superoxide-scavenging activity. These results indicate that laurylamine inhibits both the activation process of NADPH oxidase and the activated enzyme itself by blocking the assembly of the oxidase components.</description><identifier>ISSN: 0021-5198</identifier><identifier>EISSN: 1347-3506</identifier><identifier>DOI: 10.1254/jjp.80.237</identifier><identifier>PMID: 10461769</identifier><language>eng</language><publisher>Japan: The Japanese Pharmacological Society</publisher><subject>Alkylamine ; Amines - pharmacology ; Arachidonic acid ; Arachidonic Acid - pharmacology ; Cell-Free System - drug effects ; Cell-Free System - enzymology ; Dose-Response Relationship, Drug ; Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology ; HL-60 Cells ; Humans ; NADPH oxidase ; NADPH Oxidases - antagonists & inhibitors ; NADPH Oxidases - metabolism ; Neutrophil ; Translocation</subject><ispartof>The Japanese Journal of Pharmacology, 1999, Vol.80(3), pp.237-242</ispartof><rights>1999 Elsevier B.V.</rights><rights>The Japanese Pharmacological Society 1999</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c675t-d6952bf05b58a7f0cf1272a4732c15b9e91fe9c23383ebf85d0c5eb2448468f93</citedby><cites>FETCH-LOGICAL-c675t-d6952bf05b58a7f0cf1272a4732c15b9e91fe9c23383ebf85d0c5eb2448468f93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1877,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10461769$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sawai, Tohru</creatorcontrib><creatorcontrib>Asada, Makoto</creatorcontrib><creatorcontrib>Nishizawa, Yukio</creatorcontrib><creatorcontrib>Nunoi, Hiroyuki</creatorcontrib><creatorcontrib>Katayama, Kouichi</creatorcontrib><creatorcontrib>Eisai Tsukuba Research Laboratories</creatorcontrib><creatorcontrib>Department of Pediatrics</creatorcontrib><creatorcontrib>Kumamoto University School of Medicine</creatorcontrib><creatorcontrib>Department of Drug Discovery</creatorcontrib><title>Inhibition by Alkylamines of NADPH Oxidase Through Blocking the Assembly of Enzyme Components</title><title>Japanese Journal of Pharmacology</title><addtitle>Jpn.J.Pharmacol.</addtitle><description>Alkylamines inhibit NADPH oxidase both in intact neutrophils and in a cell-free system. The aim of this study was to examine the mechanism underlying this inhibitory effect. Among alkylamines with different chain lengths, the C12 compound (laurylamine) showed the greatest inhibitory effect on the cell-free NADPH oxidase activity induced by arachidonic acid (AA) in the presence of GTPγS. The inhibition was overcome by further addition of AA, and it was observed irrespective of whether laurylamine was added before or after the enzyme activation by AA. When added prior to the enzyme activation, laurylamine blocked translocation to the membrane of all three cytosolic components (p47-phox, p67-phox and rac) in a cell-free translocation assay. When added after the activation, laurylamine released only rac from the membrane. Laurylamine did not inhibit the reduction of cytochrome c by xanthine oxidase, suggesting that it does not have superoxide-scavenging activity. These results indicate that laurylamine inhibits both the activation process of NADPH oxidase and the activated enzyme itself by blocking the assembly of the oxidase components.</description><subject>Alkylamine</subject><subject>Amines - pharmacology</subject><subject>Arachidonic acid</subject><subject>Arachidonic Acid - pharmacology</subject><subject>Cell-Free System - drug effects</subject><subject>Cell-Free System - enzymology</subject><subject>Dose-Response Relationship, Drug</subject><subject>Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology</subject><subject>HL-60 Cells</subject><subject>Humans</subject><subject>NADPH oxidase</subject><subject>NADPH Oxidases - antagonists & inhibitors</subject><subject>NADPH Oxidases - metabolism</subject><subject>Neutrophil</subject><subject>Translocation</subject><issn>0021-5198</issn><issn>1347-3506</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE1v1DAQhiMEokvhwg9AOXFA2sWfiX1Cy9LSShXlUI7IcpzJxqljL3aCWH49XqVFHLh4ZM3jxzNvUbzGaIMJZ--H4bARaENo_aRYYcrqNeWoelqsECJ4zbEUZ8WLlIZ8FQiz58UZRqzCdSVXxfdr39vGTjb4sjmWW3d_dHq0HlIZuvLL9tPXq_L2l211gvKuj2He9-VHF8y99fty6qHcpgRj444n_ML_Po5Q7sJ4CB78lF4WzzrtErx6qOfFt8uLu93V-ub28_Vue7M2Vc2ndVtJTpoO8YYLXXfIdJjURLOaEoN5I0HiDqQhlAoKTSd4iwyHhjAmWCU6Sc-Lt4v3EMOPGdKkRpsMOKc9hDmpSkpBMeMZfLeAJoaUInTqEO2o41FhpE5hqhymEkjlMDP85sE6NyO0_6BLehm4XIDctUa74F1OTg1hjj6vq0xXDUM4OIWllAohgRA9FYWyPh8sb0QIpln0YRENadJ7-PuTjpM1Dh6HostxevzYMb2OCnw2sMUAOeafFqJKxoI3ebAIZlJtsP9b8Q_Uwq6H</recordid><startdate>1999</startdate><enddate>1999</enddate><creator>Sawai, Tohru</creator><creator>Asada, Makoto</creator><creator>Nishizawa, Yukio</creator><creator>Nunoi, Hiroyuki</creator><creator>Katayama, Kouichi</creator><general>The Japanese Pharmacological Society</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>1999</creationdate><title>Inhibition by Alkylamines of NADPH Oxidase Through Blocking the Assembly of Enzyme Components</title><author>Sawai, Tohru ; Asada, Makoto ; Nishizawa, Yukio ; Nunoi, Hiroyuki ; Katayama, Kouichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c675t-d6952bf05b58a7f0cf1272a4732c15b9e91fe9c23383ebf85d0c5eb2448468f93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Alkylamine</topic><topic>Amines - pharmacology</topic><topic>Arachidonic acid</topic><topic>Arachidonic Acid - pharmacology</topic><topic>Cell-Free System - drug effects</topic><topic>Cell-Free System - enzymology</topic><topic>Dose-Response Relationship, Drug</topic><topic>Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology</topic><topic>HL-60 Cells</topic><topic>Humans</topic><topic>NADPH oxidase</topic><topic>NADPH Oxidases - antagonists & inhibitors</topic><topic>NADPH Oxidases - metabolism</topic><topic>Neutrophil</topic><topic>Translocation</topic><toplevel>online_resources</toplevel><creatorcontrib>Sawai, Tohru</creatorcontrib><creatorcontrib>Asada, Makoto</creatorcontrib><creatorcontrib>Nishizawa, Yukio</creatorcontrib><creatorcontrib>Nunoi, Hiroyuki</creatorcontrib><creatorcontrib>Katayama, Kouichi</creatorcontrib><creatorcontrib>Eisai Tsukuba Research Laboratories</creatorcontrib><creatorcontrib>Department of Pediatrics</creatorcontrib><creatorcontrib>Kumamoto University School of Medicine</creatorcontrib><creatorcontrib>Department of Drug Discovery</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>Japanese Journal of Pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sawai, Tohru</au><au>Asada, Makoto</au><au>Nishizawa, Yukio</au><au>Nunoi, Hiroyuki</au><au>Katayama, Kouichi</au><aucorp>Eisai Tsukuba Research Laboratories</aucorp><aucorp>Department of Pediatrics</aucorp><aucorp>Kumamoto University School of Medicine</aucorp><aucorp>Department of Drug Discovery</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inhibition by Alkylamines of NADPH Oxidase Through Blocking the Assembly of Enzyme Components</atitle><jtitle>Japanese Journal of Pharmacology</jtitle><addtitle>Jpn.J.Pharmacol.</addtitle><date>1999</date><risdate>1999</risdate><volume>80</volume><issue>3</issue><spage>237</spage><epage>242</epage><pages>237-242</pages><issn>0021-5198</issn><eissn>1347-3506</eissn><abstract>Alkylamines inhibit NADPH oxidase both in intact neutrophils and in a cell-free system. The aim of this study was to examine the mechanism underlying this inhibitory effect. Among alkylamines with different chain lengths, the C12 compound (laurylamine) showed the greatest inhibitory effect on the cell-free NADPH oxidase activity induced by arachidonic acid (AA) in the presence of GTPγS. The inhibition was overcome by further addition of AA, and it was observed irrespective of whether laurylamine was added before or after the enzyme activation by AA. When added prior to the enzyme activation, laurylamine blocked translocation to the membrane of all three cytosolic components (p47-phox, p67-phox and rac) in a cell-free translocation assay. When added after the activation, laurylamine released only rac from the membrane. Laurylamine did not inhibit the reduction of cytochrome c by xanthine oxidase, suggesting that it does not have superoxide-scavenging activity. These results indicate that laurylamine inhibits both the activation process of NADPH oxidase and the activated enzyme itself by blocking the assembly of the oxidase components.</abstract><cop>Japan</cop><pub>The Japanese Pharmacological Society</pub><pmid>10461769</pmid><doi>10.1254/jjp.80.237</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-5198 |
| ispartof | The Japanese Journal of Pharmacology, 1999, Vol.80(3), pp.237-242 |
| issn | 0021-5198 1347-3506 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69983145 |
| source | J-STAGE Free; MEDLINE; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Alkylamine Amines - pharmacology Arachidonic acid Arachidonic Acid - pharmacology Cell-Free System - drug effects Cell-Free System - enzymology Dose-Response Relationship, Drug Guanosine 5'-O-(3-Thiotriphosphate) - pharmacology HL-60 Cells Humans NADPH oxidase NADPH Oxidases - antagonists & inhibitors NADPH Oxidases - metabolism Neutrophil Translocation |
| title | Inhibition by Alkylamines of NADPH Oxidase Through Blocking the Assembly of Enzyme Components |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-04T07%3A58%3A04IST&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=Inhibition%20by%20Alkylamines%20of%20NADPH%20Oxidase%20Through%20Blocking%20the%20Assembly%20of%20Enzyme%20Components&rft.jtitle=Japanese%20Journal%20of%20Pharmacology&rft.au=Sawai,%20Tohru&rft.aucorp=Eisai%20Tsukuba%20Research%20Laboratories&rft.date=1999&rft.volume=80&rft.issue=3&rft.spage=237&rft.epage=242&rft.pages=237-242&rft.issn=0021-5198&rft.eissn=1347-3506&rft_id=info:doi/10.1254/jjp.80.237&rft_dat=%3Cproquest_cross%3E69983145%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=69983145&rft_id=info:pmid/10461769&rft_els_id=S0021519819308480&rfr_iscdi=true |