Dykellic acid inhibits drug-induced caspase-3-like protease activation
Dykellic acid is a novel microbial metabolite isolated from the broth of Westerdykella multispora F50733. Investigations on the molecular function of dykellic acid revealed that this compound partially inhibits calcium influx, resulting in a decrease in Ca 2+-dependent endonuclease activation and DN...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2003-03, Vol.302 (3), p.539-544 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Lee, Sang-Han Youk, Eun-Soo Lee, Ho-Jae Kho, Yung-Hee Kim, Hwan Mook Kim, Sung-Uk |
| description | Dykellic acid is a novel microbial metabolite isolated from the broth of
Westerdykella multispora F50733. Investigations on the molecular function of dykellic acid revealed that this compound partially inhibits calcium influx, resulting in a decrease in Ca
2+-dependent endonuclease activation and DNA fragmentation induced by camptothecin. In our experiments, active caspase-3-like protease cleavage of procaspase-3, PARP, and cytosolic cytochrome
c was inhibited by dykellic acid in a concentration-dependent manner when the apoptosis was induced by camptothecin as well as doxorubicin. We confirmed that dykellic acid did not bind to camptothecin using surface plasmon resonance analysis. These results suggest that dykellic acid inhibits drug-induced apoptosis via a caspase-3-like protease-suppressing mechanism. Our data provide important information on the mechanism of action of dykellic acid and indicate that this compound may be employed in the treatment of specific caspase-3-like protease-mediated diseases. |
| doi_str_mv | 10.1016/S0006-291X(03)00210-9 |
| format | Article |
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Westerdykella multispora F50733. Investigations on the molecular function of dykellic acid revealed that this compound partially inhibits calcium influx, resulting in a decrease in Ca
2+-dependent endonuclease activation and DNA fragmentation induced by camptothecin. In our experiments, active caspase-3-like protease cleavage of procaspase-3, PARP, and cytosolic cytochrome
c was inhibited by dykellic acid in a concentration-dependent manner when the apoptosis was induced by camptothecin as well as doxorubicin. We confirmed that dykellic acid did not bind to camptothecin using surface plasmon resonance analysis. These results suggest that dykellic acid inhibits drug-induced apoptosis via a caspase-3-like protease-suppressing mechanism. Our data provide important information on the mechanism of action of dykellic acid and indicate that this compound may be employed in the treatment of specific caspase-3-like protease-mediated diseases.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(03)00210-9</identifier><identifier>PMID: 12615068</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Apoptosis ; Apoptosis inhibitor ; Blotting, Western ; Calcium - metabolism ; Camptothecin ; Camptothecin - metabolism ; Camptothecin - pharmacology ; Caspase 3 ; Caspase-3-like protease ; Caspases - metabolism ; Cell Line ; Cytochrome c Group - metabolism ; Cytosol - enzymology ; DNA Fragmentation ; Dose-Response Relationship, Drug ; Dykellic acid ; Endonucleases - metabolism ; Enzyme Activation ; Enzyme Precursors - metabolism ; HL-60 Cells ; Humans ; Inhibitor ; Jurkat Cells ; Microscopy, Electron, Scanning ; Models, Chemical ; Poly(ADP-ribose) Polymerases - metabolism ; Propionates - pharmacology ; Pyrones - pharmacology ; Spectrometry, Fluorescence ; Surface Plasmon Resonance ; Time Factors ; U937 Cells</subject><ispartof>Biochemical and biophysical research communications, 2003-03, Vol.302 (3), p.539-544</ispartof><rights>2003 Elsevier Science (USA)</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-eee17f4d61eb831d0835cb0efe705fe2c40978bdac4683b40c7475e64b799c9a3</citedby><cites>FETCH-LOGICAL-c427t-eee17f4d61eb831d0835cb0efe705fe2c40978bdac4683b40c7475e64b799c9a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X03002109$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12615068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, Sang-Han</creatorcontrib><creatorcontrib>Youk, Eun-Soo</creatorcontrib><creatorcontrib>Lee, Ho-Jae</creatorcontrib><creatorcontrib>Kho, Yung-Hee</creatorcontrib><creatorcontrib>Kim, Hwan Mook</creatorcontrib><creatorcontrib>Kim, Sung-Uk</creatorcontrib><title>Dykellic acid inhibits drug-induced caspase-3-like protease activation</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Dykellic acid is a novel microbial metabolite isolated from the broth of
Westerdykella multispora F50733. Investigations on the molecular function of dykellic acid revealed that this compound partially inhibits calcium influx, resulting in a decrease in Ca
2+-dependent endonuclease activation and DNA fragmentation induced by camptothecin. In our experiments, active caspase-3-like protease cleavage of procaspase-3, PARP, and cytosolic cytochrome
c was inhibited by dykellic acid in a concentration-dependent manner when the apoptosis was induced by camptothecin as well as doxorubicin. We confirmed that dykellic acid did not bind to camptothecin using surface plasmon resonance analysis. These results suggest that dykellic acid inhibits drug-induced apoptosis via a caspase-3-like protease-suppressing mechanism. Our data provide important information on the mechanism of action of dykellic acid and indicate that this compound may be employed in the treatment of specific caspase-3-like protease-mediated diseases.</description><subject>Apoptosis</subject><subject>Apoptosis inhibitor</subject><subject>Blotting, Western</subject><subject>Calcium - metabolism</subject><subject>Camptothecin</subject><subject>Camptothecin - metabolism</subject><subject>Camptothecin - pharmacology</subject><subject>Caspase 3</subject><subject>Caspase-3-like protease</subject><subject>Caspases - metabolism</subject><subject>Cell Line</subject><subject>Cytochrome c Group - metabolism</subject><subject>Cytosol - enzymology</subject><subject>DNA Fragmentation</subject><subject>Dose-Response Relationship, Drug</subject><subject>Dykellic acid</subject><subject>Endonucleases - metabolism</subject><subject>Enzyme Activation</subject><subject>Enzyme Precursors - metabolism</subject><subject>HL-60 Cells</subject><subject>Humans</subject><subject>Inhibitor</subject><subject>Jurkat Cells</subject><subject>Microscopy, Electron, Scanning</subject><subject>Models, Chemical</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Propionates - pharmacology</subject><subject>Pyrones - pharmacology</subject><subject>Spectrometry, Fluorescence</subject><subject>Surface Plasmon Resonance</subject><subject>Time Factors</subject><subject>U937 Cells</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtKxDAUhoMoznh5BKUr0UX0pEnTZiUyOioMuFDBXUiTU43OtGPTDszbm7mgS1eHA99_Lh8hJwwuGTB59QwAkqaKvZ0DvwBIGVC1Q4YMFNDYiF0y_EUG5CCETwDGhFT7ZMBSyTKQxZCMb5dfOJ16mxjrXeLrD1_6LiSu7d-pr11v0SXWhLkJSDmd-i9M5m3TYexjpPML0_mmPiJ7lZkGPN7WQ_I6vnsZPdDJ0_3j6GZCrUjzjiIiyyvhJMOy4MxBwTNbAlaYQ1ZhagWovCidsUIWvBRgc5FnKEWZK2WV4YfkbDM33vDdY-j0zAcbHzA1Nn3QOYdMclARzDagbZsQWqz0vPUz0y41A70SqNcC9cqOBq7XAvUqd7pd0JczdH-prbEIXG8AjG8uPLY6WI911ORbtJ12jf9nxQ8PaYA8</recordid><startdate>20030314</startdate><enddate>20030314</enddate><creator>Lee, Sang-Han</creator><creator>Youk, Eun-Soo</creator><creator>Lee, Ho-Jae</creator><creator>Kho, Yung-Hee</creator><creator>Kim, Hwan Mook</creator><creator>Kim, Sung-Uk</creator><general>Elsevier Inc</general><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>20030314</creationdate><title>Dykellic acid inhibits drug-induced caspase-3-like protease activation</title><author>Lee, Sang-Han ; Youk, Eun-Soo ; Lee, Ho-Jae ; Kho, Yung-Hee ; Kim, Hwan Mook ; Kim, Sung-Uk</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-eee17f4d61eb831d0835cb0efe705fe2c40978bdac4683b40c7475e64b799c9a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Apoptosis</topic><topic>Apoptosis inhibitor</topic><topic>Blotting, Western</topic><topic>Calcium - metabolism</topic><topic>Camptothecin</topic><topic>Camptothecin - metabolism</topic><topic>Camptothecin - pharmacology</topic><topic>Caspase 3</topic><topic>Caspase-3-like protease</topic><topic>Caspases - metabolism</topic><topic>Cell Line</topic><topic>Cytochrome c Group - metabolism</topic><topic>Cytosol - enzymology</topic><topic>DNA Fragmentation</topic><topic>Dose-Response Relationship, Drug</topic><topic>Dykellic acid</topic><topic>Endonucleases - metabolism</topic><topic>Enzyme Activation</topic><topic>Enzyme Precursors - metabolism</topic><topic>HL-60 Cells</topic><topic>Humans</topic><topic>Inhibitor</topic><topic>Jurkat Cells</topic><topic>Microscopy, Electron, Scanning</topic><topic>Models, Chemical</topic><topic>Poly(ADP-ribose) Polymerases - metabolism</topic><topic>Propionates - pharmacology</topic><topic>Pyrones - pharmacology</topic><topic>Spectrometry, Fluorescence</topic><topic>Surface Plasmon Resonance</topic><topic>Time Factors</topic><topic>U937 Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Sang-Han</creatorcontrib><creatorcontrib>Youk, Eun-Soo</creatorcontrib><creatorcontrib>Lee, Ho-Jae</creatorcontrib><creatorcontrib>Kho, Yung-Hee</creatorcontrib><creatorcontrib>Kim, Hwan Mook</creatorcontrib><creatorcontrib>Kim, Sung-Uk</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Sang-Han</au><au>Youk, Eun-Soo</au><au>Lee, Ho-Jae</au><au>Kho, Yung-Hee</au><au>Kim, Hwan Mook</au><au>Kim, Sung-Uk</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dykellic acid inhibits drug-induced caspase-3-like protease activation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2003-03-14</date><risdate>2003</risdate><volume>302</volume><issue>3</issue><spage>539</spage><epage>544</epage><pages>539-544</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Dykellic acid is a novel microbial metabolite isolated from the broth of
Westerdykella multispora F50733. Investigations on the molecular function of dykellic acid revealed that this compound partially inhibits calcium influx, resulting in a decrease in Ca
2+-dependent endonuclease activation and DNA fragmentation induced by camptothecin. In our experiments, active caspase-3-like protease cleavage of procaspase-3, PARP, and cytosolic cytochrome
c was inhibited by dykellic acid in a concentration-dependent manner when the apoptosis was induced by camptothecin as well as doxorubicin. We confirmed that dykellic acid did not bind to camptothecin using surface plasmon resonance analysis. These results suggest that dykellic acid inhibits drug-induced apoptosis via a caspase-3-like protease-suppressing mechanism. Our data provide important information on the mechanism of action of dykellic acid and indicate that this compound may be employed in the treatment of specific caspase-3-like protease-mediated diseases.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12615068</pmid><doi>10.1016/S0006-291X(03)00210-9</doi><tpages>6</tpages></addata></record> |
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| subjects | Apoptosis Apoptosis inhibitor Blotting, Western Calcium - metabolism Camptothecin Camptothecin - metabolism Camptothecin - pharmacology Caspase 3 Caspase-3-like protease Caspases - metabolism Cell Line Cytochrome c Group - metabolism Cytosol - enzymology DNA Fragmentation Dose-Response Relationship, Drug Dykellic acid Endonucleases - metabolism Enzyme Activation Enzyme Precursors - metabolism HL-60 Cells Humans Inhibitor Jurkat Cells Microscopy, Electron, Scanning Models, Chemical Poly(ADP-ribose) Polymerases - metabolism Propionates - pharmacology Pyrones - pharmacology Spectrometry, Fluorescence Surface Plasmon Resonance Time Factors U937 Cells |
| title | Dykellic acid inhibits drug-induced caspase-3-like protease activation |
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