In vitro biological activities of magainin alone or in combination with nisin
Antimicrobial peptides have received increasing attention not only as potential candidates to their administration as antimicrobial agents, but also as potential drugs applied in cancer therapy. Here, we have examined the action of both nisin and magainin on human promyelocytic leukemia HL-60 cells....
Gespeichert in:
| Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2006-06, Vol.27 (6), p.1201-1209 |
|---|---|
| Hauptverfasser: | , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1209 |
|---|---|
| container_issue | 6 |
| container_start_page | 1201 |
| container_title | Peptides (New York, N.Y. : 1980) |
| container_volume | 27 |
| creator | Cruz-Chamorro, Lidia Puertollano, María A. Puertollano, Elena de Cienfuegos, Gerardo Álvarez de Pablo, Manuel A. |
| description | Antimicrobial peptides have received increasing attention not only as potential candidates to their administration as antimicrobial agents, but also as potential drugs applied in cancer therapy. Here, we have examined the action of both nisin and magainin on human promyelocytic leukemia HL-60 cells. Cells were cultured in presence of either nisin or magainin 1 as well as in combination with both nisin and magainin 1. Results have revealed that magainin, but not nisin, produces a loss of cell viability in HL-60 cells, and a minor increase of hemolysis, whereas it is not responsible for cell membrane disruption and lactate dehydrogenase (LDH) leakage. In addition, magainin is involved in a significant generation of reactive oxygen species (ROS), as well as in an augment of caspase-3 activity. Magainin-induced apoptosis was verified by DNA fragmentation and annexin V-FITC/propidium iodide (PI) staining of the cells. Promotion of cell death by magainin occurs via cytochrome
c release accompanied by a substantial increase of proteasome activity. These results underline the importance of magainin as a drug capable of exerting an in vitro antitumoral activity by triggering apoptosis. |
| doi_str_mv | 10.1016/j.peptides.2005.11.008 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_68019807</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0196978105005516</els_id><sourcerecordid>20718468</sourcerecordid><originalsourceid>FETCH-LOGICAL-c427t-151278e0989a9e3de61b460dcdd037b1bad525aba1c7b7c11c1fa9f1c60ded6d3</originalsourceid><addsrcrecordid>eNqFkUtvFDEMgCMEokvhL1S5wG2GeB553EAVj0pFXOAcZRJP8WomWZLZIv49qXZRjz3Zsj7byWfGrkC0IEC-37cHPGwUsLSdEGML0Aqhn7EdaNU3I0jznO0EGNkYpeGCvSplL4QYBqNfsguQ_ShHbXbs203k97TlxCdKS7oj7xbu_Ea1SFh4mvnq7hxFitwtKSJPmdfcp3Wi6DZKkf-h7RePVCi-Zi9mtxR8c46X7OfnTz-uvza337_cXH-8bfzQqa2BETqlURhtnME-oIRpkCL4EESvJphcGLvRTQ68mpQH8DA7M4OvDAYZ-kv27jT3kNPvI5bNrlQ8LouLmI7FSl2_roV6EuyEAj1IXUF5An1OpWSc7SHT6vJfC8I-GLd7-9-4fTBuAWw1XhuvzhuO04rhse2suAJvz4ArVe6cXfRUHjmlR1NvVLkPJw6ruHvCbIsnjB4DZfSbDYmeess_26Sjcw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20718468</pqid></control><display><type>article</type><title>In vitro biological activities of magainin alone or in combination with nisin</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Cruz-Chamorro, Lidia ; Puertollano, María A. ; Puertollano, Elena ; de Cienfuegos, Gerardo Álvarez ; de Pablo, Manuel A.</creator><creatorcontrib>Cruz-Chamorro, Lidia ; Puertollano, María A. ; Puertollano, Elena ; de Cienfuegos, Gerardo Álvarez ; de Pablo, Manuel A.</creatorcontrib><description>Antimicrobial peptides have received increasing attention not only as potential candidates to their administration as antimicrobial agents, but also as potential drugs applied in cancer therapy. Here, we have examined the action of both nisin and magainin on human promyelocytic leukemia HL-60 cells. Cells were cultured in presence of either nisin or magainin 1 as well as in combination with both nisin and magainin 1. Results have revealed that magainin, but not nisin, produces a loss of cell viability in HL-60 cells, and a minor increase of hemolysis, whereas it is not responsible for cell membrane disruption and lactate dehydrogenase (LDH) leakage. In addition, magainin is involved in a significant generation of reactive oxygen species (ROS), as well as in an augment of caspase-3 activity. Magainin-induced apoptosis was verified by DNA fragmentation and annexin V-FITC/propidium iodide (PI) staining of the cells. Promotion of cell death by magainin occurs via cytochrome
c release accompanied by a substantial increase of proteasome activity. These results underline the importance of magainin as a drug capable of exerting an in vitro antitumoral activity by triggering apoptosis.</description><identifier>ISSN: 0196-9781</identifier><identifier>EISSN: 1873-5169</identifier><identifier>DOI: 10.1016/j.peptides.2005.11.008</identifier><identifier>PMID: 16356589</identifier><identifier>CODEN: PPTDD5</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Annexin-V ; Anti-Bacterial Agents - administration & dosage ; Antimicrobial Cationic Peptides - administration & dosage ; Antimicrobial Cationic Peptides - chemistry ; Antimicrobial Cationic Peptides - pharmacology ; Apoptosis ; Biological and medical sciences ; Caspase 3 ; Caspases - metabolism ; Cell Membrane - metabolism ; Cytochrome c ; Cytochromes c - metabolism ; DNA Fragmentation ; Drug Therapy, Combination ; Fundamental and applied biological sciences. Psychology ; HL-60 Cells ; Humans ; In Vitro Techniques ; L-Lactate Dehydrogenase - metabolism ; Magainin ; Nisin ; Nisin - administration & dosage ; Nisin - pharmacology ; Peptides - chemistry ; Propidium - pharmacology ; Proteasome activity ; Reactive Oxygen Species ; Vertebrates: endocrinology</subject><ispartof>Peptides (New York, N.Y. : 1980), 2006-06, Vol.27 (6), p.1201-1209</ispartof><rights>2005 Elsevier Inc.</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-151278e0989a9e3de61b460dcdd037b1bad525aba1c7b7c11c1fa9f1c60ded6d3</citedby><cites>FETCH-LOGICAL-c427t-151278e0989a9e3de61b460dcdd037b1bad525aba1c7b7c11c1fa9f1c60ded6d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.peptides.2005.11.008$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17859978$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16356589$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cruz-Chamorro, Lidia</creatorcontrib><creatorcontrib>Puertollano, María A.</creatorcontrib><creatorcontrib>Puertollano, Elena</creatorcontrib><creatorcontrib>de Cienfuegos, Gerardo Álvarez</creatorcontrib><creatorcontrib>de Pablo, Manuel A.</creatorcontrib><title>In vitro biological activities of magainin alone or in combination with nisin</title><title>Peptides (New York, N.Y. : 1980)</title><addtitle>Peptides</addtitle><description>Antimicrobial peptides have received increasing attention not only as potential candidates to their administration as antimicrobial agents, but also as potential drugs applied in cancer therapy. Here, we have examined the action of both nisin and magainin on human promyelocytic leukemia HL-60 cells. Cells were cultured in presence of either nisin or magainin 1 as well as in combination with both nisin and magainin 1. Results have revealed that magainin, but not nisin, produces a loss of cell viability in HL-60 cells, and a minor increase of hemolysis, whereas it is not responsible for cell membrane disruption and lactate dehydrogenase (LDH) leakage. In addition, magainin is involved in a significant generation of reactive oxygen species (ROS), as well as in an augment of caspase-3 activity. Magainin-induced apoptosis was verified by DNA fragmentation and annexin V-FITC/propidium iodide (PI) staining of the cells. Promotion of cell death by magainin occurs via cytochrome
c release accompanied by a substantial increase of proteasome activity. These results underline the importance of magainin as a drug capable of exerting an in vitro antitumoral activity by triggering apoptosis.</description><subject>Annexin-V</subject><subject>Anti-Bacterial Agents - administration & dosage</subject><subject>Antimicrobial Cationic Peptides - administration & dosage</subject><subject>Antimicrobial Cationic Peptides - chemistry</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Apoptosis</subject><subject>Biological and medical sciences</subject><subject>Caspase 3</subject><subject>Caspases - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Cytochrome c</subject><subject>Cytochromes c - metabolism</subject><subject>DNA Fragmentation</subject><subject>Drug Therapy, Combination</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>HL-60 Cells</subject><subject>Humans</subject><subject>In Vitro Techniques</subject><subject>L-Lactate Dehydrogenase - metabolism</subject><subject>Magainin</subject><subject>Nisin</subject><subject>Nisin - administration & dosage</subject><subject>Nisin - pharmacology</subject><subject>Peptides - chemistry</subject><subject>Propidium - pharmacology</subject><subject>Proteasome activity</subject><subject>Reactive Oxygen Species</subject><subject>Vertebrates: endocrinology</subject><issn>0196-9781</issn><issn>1873-5169</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtvFDEMgCMEokvhL1S5wG2GeB553EAVj0pFXOAcZRJP8WomWZLZIv49qXZRjz3Zsj7byWfGrkC0IEC-37cHPGwUsLSdEGML0Aqhn7EdaNU3I0jznO0EGNkYpeGCvSplL4QYBqNfsguQ_ShHbXbs203k97TlxCdKS7oj7xbu_Ea1SFh4mvnq7hxFitwtKSJPmdfcp3Wi6DZKkf-h7RePVCi-Zi9mtxR8c46X7OfnTz-uvza337_cXH-8bfzQqa2BETqlURhtnME-oIRpkCL4EESvJphcGLvRTQ68mpQH8DA7M4OvDAYZ-kv27jT3kNPvI5bNrlQ8LouLmI7FSl2_roV6EuyEAj1IXUF5An1OpWSc7SHT6vJfC8I-GLd7-9-4fTBuAWw1XhuvzhuO04rhse2suAJvz4ArVe6cXfRUHjmlR1NvVLkPJw6ruHvCbIsnjB4DZfSbDYmeess_26Sjcw</recordid><startdate>20060601</startdate><enddate>20060601</enddate><creator>Cruz-Chamorro, Lidia</creator><creator>Puertollano, María A.</creator><creator>Puertollano, Elena</creator><creator>de Cienfuegos, Gerardo Álvarez</creator><creator>de Pablo, Manuel A.</creator><general>Elsevier Inc</general><general>Elsevier Science</general><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>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20060601</creationdate><title>In vitro biological activities of magainin alone or in combination with nisin</title><author>Cruz-Chamorro, Lidia ; Puertollano, María A. ; Puertollano, Elena ; de Cienfuegos, Gerardo Álvarez ; de Pablo, Manuel A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-151278e0989a9e3de61b460dcdd037b1bad525aba1c7b7c11c1fa9f1c60ded6d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Annexin-V</topic><topic>Anti-Bacterial Agents - administration & dosage</topic><topic>Antimicrobial Cationic Peptides - administration & dosage</topic><topic>Antimicrobial Cationic Peptides - chemistry</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Apoptosis</topic><topic>Biological and medical sciences</topic><topic>Caspase 3</topic><topic>Caspases - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Cytochrome c</topic><topic>Cytochromes c - metabolism</topic><topic>DNA Fragmentation</topic><topic>Drug Therapy, Combination</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>HL-60 Cells</topic><topic>Humans</topic><topic>In Vitro Techniques</topic><topic>L-Lactate Dehydrogenase - metabolism</topic><topic>Magainin</topic><topic>Nisin</topic><topic>Nisin - administration & dosage</topic><topic>Nisin - pharmacology</topic><topic>Peptides - chemistry</topic><topic>Propidium - pharmacology</topic><topic>Proteasome activity</topic><topic>Reactive Oxygen Species</topic><topic>Vertebrates: endocrinology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cruz-Chamorro, Lidia</creatorcontrib><creatorcontrib>Puertollano, María A.</creatorcontrib><creatorcontrib>Puertollano, Elena</creatorcontrib><creatorcontrib>de Cienfuegos, Gerardo Álvarez</creatorcontrib><creatorcontrib>de Pablo, Manuel A.</creatorcontrib><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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Peptides (New York, N.Y. : 1980)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cruz-Chamorro, Lidia</au><au>Puertollano, María A.</au><au>Puertollano, Elena</au><au>de Cienfuegos, Gerardo Álvarez</au><au>de Pablo, Manuel A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In vitro biological activities of magainin alone or in combination with nisin</atitle><jtitle>Peptides (New York, N.Y. : 1980)</jtitle><addtitle>Peptides</addtitle><date>2006-06-01</date><risdate>2006</risdate><volume>27</volume><issue>6</issue><spage>1201</spage><epage>1209</epage><pages>1201-1209</pages><issn>0196-9781</issn><eissn>1873-5169</eissn><coden>PPTDD5</coden><abstract>Antimicrobial peptides have received increasing attention not only as potential candidates to their administration as antimicrobial agents, but also as potential drugs applied in cancer therapy. Here, we have examined the action of both nisin and magainin on human promyelocytic leukemia HL-60 cells. Cells were cultured in presence of either nisin or magainin 1 as well as in combination with both nisin and magainin 1. Results have revealed that magainin, but not nisin, produces a loss of cell viability in HL-60 cells, and a minor increase of hemolysis, whereas it is not responsible for cell membrane disruption and lactate dehydrogenase (LDH) leakage. In addition, magainin is involved in a significant generation of reactive oxygen species (ROS), as well as in an augment of caspase-3 activity. Magainin-induced apoptosis was verified by DNA fragmentation and annexin V-FITC/propidium iodide (PI) staining of the cells. Promotion of cell death by magainin occurs via cytochrome
c release accompanied by a substantial increase of proteasome activity. These results underline the importance of magainin as a drug capable of exerting an in vitro antitumoral activity by triggering apoptosis.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>16356589</pmid><doi>10.1016/j.peptides.2005.11.008</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0196-9781 |
| ispartof | Peptides (New York, N.Y. : 1980), 2006-06, Vol.27 (6), p.1201-1209 |
| issn | 0196-9781 1873-5169 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68019807 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Annexin-V Anti-Bacterial Agents - administration & dosage Antimicrobial Cationic Peptides - administration & dosage Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - pharmacology Apoptosis Biological and medical sciences Caspase 3 Caspases - metabolism Cell Membrane - metabolism Cytochrome c Cytochromes c - metabolism DNA Fragmentation Drug Therapy, Combination Fundamental and applied biological sciences. Psychology HL-60 Cells Humans In Vitro Techniques L-Lactate Dehydrogenase - metabolism Magainin Nisin Nisin - administration & dosage Nisin - pharmacology Peptides - chemistry Propidium - pharmacology Proteasome activity Reactive Oxygen Species Vertebrates: endocrinology |
| title | In vitro biological activities of magainin alone or in combination with nisin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-11T20%3A04%3A32IST&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=In%20vitro%20biological%20activities%20of%20magainin%20alone%20or%20in%20combination%20with%20nisin&rft.jtitle=Peptides%20(New%20York,%20N.Y.%20:%201980)&rft.au=Cruz-Chamorro,%20Lidia&rft.date=2006-06-01&rft.volume=27&rft.issue=6&rft.spage=1201&rft.epage=1209&rft.pages=1201-1209&rft.issn=0196-9781&rft.eissn=1873-5169&rft.coden=PPTDD5&rft_id=info:doi/10.1016/j.peptides.2005.11.008&rft_dat=%3Cproquest_cross%3E20718468%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=20718468&rft_id=info:pmid/16356589&rft_els_id=S0196978105005516&rfr_iscdi=true |