Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms
Identifieur interne : 000348 ( Istex/Corpus ); précédent : 000347; suivant : 000349Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms
Auteurs : Cindy Araya ; Bruno LomonteSource :
- Cell Biology International [ 1065-6995 ] ; 2007-03.
English descriptors
- Teeft :
- Antimicrobial, Antimicrobial activity, Antimicrobial peptides, Antitumor, Antitumor activity, Antitumor effect, Antitumor effects, Asper, Bactericidal activity, Biol chem, Body weight, Bothrops, Bothrops asper, Bothrops asper snake venom, Carcinoma cells, Cationic, Cationic peptides, Cell biology, Cell line control, Cell lines, Comparative study, Costa rica, Crotalid snake venoms, Cytolytic, Cytolytic activity, Cytolytic effect, Emt6, Endothelial cells, Fetal calf serum, High concentrations, Homologues, Innate immunity, International federation, Intraperitoneal route, Lactate dehydrogenase, Latter case, Lomonte, Lomonte cell biology, Lytic action, Murine, Murine tumor cell lines, Myotoxic, Myotoxic phospholipases, Myotoxin, Normal cells, Papo, Peptide, Phospholipase, Piscivorus, Pla2, Pla2 homologues, Present work, Proc natl acad, Similar magnitude, Skeletal muscle, Skeletal muscle myoblasts, Snake venom, Snake venoms, Synthetic peptides, Toxicon, Toxicon lomonte, Toxin, Tumor cell lines, Tumor cells, Tumor growth, Tumor mass reduction, Tumor masses, Venom.
Abstract
The effects of two cationic synthetic peptides, derived from the C‐terminal region of Lys49 phospholipase A2 homologues from snake venoms, upon various murine tumor cell lines (B16 melanoma, EMT6 mammary carcinoma, S‐180 sarcoma, P3X myeloma, tEnd endothelial cells) were evaluated. The peptides are 13‐mers derived from Agkistrodon piscivorus piscivorus Lys49 PLA2 (p‐AppK: KKYKAYFKLKCKK) and Bothrops asper Lys49 myotoxin II (pEM‐2[d]: KKWRWWLKALAKK), respectively, in the latter case with slight modifications and with all‐d amino acids. All tumor cells tested were susceptible to the lytic action of the peptides. The susceptibility of tumor cell lines was not higher than that of C2C12 skeletal muscle myoblasts, utilized as a non‐transformed cell line control. However, in a murine model of subcutaneous solid tumor growth of EMT6 mammary carcinoma, the intraperitoneal administration of pEM‐2[d] caused a tumor mass reduction of 36% (p < 0.05), which was of similar magnitude to that achieved by the administration of paclitaxel, an antitumor drug in clinical use. Thus, the C‐terminal peptides of Lys49 phospholipase A2 homologues present antitumor effects that might be of interest in developing therapeutic strategies against cancer.
Url:
DOI: 10.1016/j.cellbi.2006.11.007
Links to Exploration step
ISTEX:2EAFEB48E226E56C407278CAF1C10FD4C30E7ADDLe document en format XML
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serum</term><term>High concentrations</term><term>Homologues</term><term>Innate immunity</term><term>International federation</term><term>Intraperitoneal route</term><term>Lactate dehydrogenase</term><term>Latter case</term><term>Lomonte</term><term>Lomonte cell biology</term><term>Lytic action</term><term>Murine</term><term>Murine tumor cell lines</term><term>Myotoxic</term><term>Myotoxic phospholipases</term><term>Myotoxin</term><term>Normal cells</term><term>Papo</term><term>Peptide</term><term>Phospholipase</term><term>Piscivorus</term><term>Pla2</term><term>Pla2 homologues</term><term>Present work</term><term>Proc natl acad</term><term>Similar magnitude</term><term>Skeletal muscle</term><term>Skeletal muscle myoblasts</term><term>Snake venom</term><term>Snake venoms</term><term>Synthetic peptides</term><term>Toxicon</term><term>Toxicon lomonte</term><term>Toxin</term><term>Tumor cell lines</term><term>Tumor cells</term><term>Tumor growth</term><term>Tumor mass 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The peptides are 13‐mers derived from Agkistrodon piscivorus piscivorus Lys49 PLA2 (p‐AppK: KKYKAYFKLKCKK) and Bothrops asper Lys49 myotoxin II (pEM‐2[d]: KKWRWWLKALAKK), respectively, in the latter case with slight modifications and with all‐d amino acids. All tumor cells tested were susceptible to the lytic action of the peptides. The susceptibility of tumor cell lines was not higher than that of C2C12 skeletal muscle myoblasts, utilized as a non‐transformed cell line control. However, in a murine model of subcutaneous solid tumor growth of EMT6 mammary carcinoma, the intraperitoneal administration of pEM‐2[d] caused a tumor mass reduction of 36% (p < 0.05), which was of similar magnitude to that achieved by the administration of paclitaxel, an antitumor drug in clinical use. 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The peptides are 13‐mers derived from Agkistrodon piscivorus piscivorus Lys49 PLA2 (p‐AppK: KKYKAYFKLKCKK) and Bothrops asper Lys49 myotoxin II (pEM‐2[d]: KKWRWWLKALAKK), respectively, in the latter case with slight modifications and with all‐d amino acids. All tumor cells tested were susceptible to the lytic action of the peptides. The susceptibility of tumor cell lines was not higher than that of C2C12 skeletal muscle myoblasts, utilized as a non‐transformed cell line control. However, in a murine model of subcutaneous solid tumor growth of EMT6 mammary carcinoma, the intraperitoneal administration of pEM‐2[d] caused a tumor mass reduction of 36% (p > 0.05), which was of similar magnitude to that achieved by the administration of paclitaxel, an antitumor drug in clinical use. 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Araya</json:string><json:string>O. Enhanced</json:string><json:string>Results</json:string><json:string>John Wiley</json:string><json:string>B. Identi</json:string><json:string>Carlos Santamar</json:string><json:string>Marietta Flores</json:string><json:string>Shai Y. Suppression</json:string><json:string>Bruno Lomonte</json:string><json:string>B. Lomonte</json:string><json:string>T. Identi</json:string><json:string>Paclitaxel</json:string></persName><placeName><json:string>Bristol</json:string><json:string>SY</json:string><json:string>America</json:string><json:string>Sweden</json:string></placeName><ref_url></ref_url><ref_bibl><json:string>Papo et al., 2003</json:string><json:string>Walker, 1994</json:string><json:string>Paramo et al., 1998</json:string><json:string>Glukhov et al., 2005</json:string><json:string>Okumura et al., 2004</json:string><json:string>Gutierrez and Lomonte, 1997</json:string><json:string>Wang et al., 2000</json:string><json:string>Wani et al., 1971</json:string><json:string>Nunez et al., 2001</json:string><json:string>Mora et al., 2005</json:string><json:string>Correa et al., 2002</json:string><json:string>Braganca and Hospattankar, 1978</json:string><json:string>Yamazaki et al., 2005</json:string><json:string>Lomonte et al., 2003b</json:string><json:string>Pereira-Bittencourt et al., 1999</json:string><json:string>Yang et al., 2002</json:string><json:string>Xiao et al., 2006</json:string><json:string>Papo et al., 2003, 2004</json:string><json:string>Lomonte et al., 1994</json:string><json:string>Lomonte et al., 2003a</json:string><json:string>Renetseder et al., 1985</json:string><json:string>Lomonte et al., 1999</json:string><json:string>Cura et al., 2002</json:string><json:string>Papo and Shai, 2003</json:string><json:string>Hancock and Scott, 2000</json:string><json:string>Furlong et al., 2006</json:string><json:string>Bussolino et al., 1991</json:string><json:string>Shin et al., 2000</json:string><json:string>Costa et al., 1997</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/WNG-DVT2V7BG-R</json:string></ark><categories><wos><json:string>1 - 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<ref target="http://www.tei-c.org/">We use TEI</ref></desc></application></appInfo></encodingDesc><profileDesc><abstract xml:lang="en" style="main"><head>Abstract</head><p>The effects of two cationic synthetic peptides, derived from the C‐terminal region of Lys49 phospholipase A<hi rend="subscript">2</hi> homologues from snake venoms, upon various murine tumor cell lines (B16 melanoma, EMT6 mammary carcinoma, S‐180 sarcoma, P3X myeloma, tEnd endothelial cells) were evaluated. The peptides are 13‐mers derived from <hi rend="italic">Agkistrodon piscivorus piscivorus</hi> Lys49 PLA<hi rend="subscript">2</hi> (p‐AppK: KKYKAYFKLKCKK) and <hi rend="italic">Bothrops asper</hi> Lys49 myotoxin II (pEM‐2[<hi rend="smallCaps">d</hi>]: KKWRWWLKALAKK), respectively, in the latter case with slight modifications and with all‐<hi rend="smallCaps">d</hi> amino acids. All tumor cells tested were susceptible to the lytic action of the peptides. The susceptibility of tumor cell lines was not higher than that of C2C12 skeletal muscle myoblasts, utilized as a non‐transformed cell line control. However, in a murine model of subcutaneous solid tumor growth of EMT6 mammary carcinoma, the intraperitoneal administration of pEM‐2[<hi rend="smallCaps">d</hi>] caused a tumor mass reduction of 36% (<hi rend="italic">p</hi> < 0.05), which was of similar magnitude to that achieved by the administration of paclitaxel, an antitumor drug in clinical use. Thus, the C‐terminal peptides of Lys49 phospholipase A<hi rend="subscript">2</hi> homologues present antitumor effects that might be of interest in developing therapeutic strategies against cancer.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">Cationic peptides</term><term xml:id="k2">Antitumor</term><term xml:id="k3">Phospholipase A<hi rend="subscript">2</hi></term><term xml:id="k4">Snake venom</term><term xml:id="k5">Myotoxin</term></keywords><keywords rend="tocHeading1"><term>Regular Article</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc><revisionDesc><change when="2019-12-20" who="#istex" xml:id="pub2tei">formatting</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/WNG-DVT2V7BG-R/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Publishing Ltd</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1002/(ISSN)1095-8355</doi><issn type="print">1065-6995</issn><issn type="electronic">1095-8355</issn><idGroup><id type="product" value="CBIN"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="CELL BIOLOGY INTERNATIONAL">Cell Biology International</title></titleGroup></publicationMeta><publicationMeta level="part" position="03103"><doi origin="wiley">10.1002/cbin.2007.31.issue-3</doi><numberingGroup><numbering type="journalVolume" number="31">31</numbering><numbering type="journalIssue" number="3">3</numbering></numberingGroup><coverDate startDate="2007-03">March 2007</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="11" status="forIssue"><doi origin="wiley">10.1016/j.cellbi.2006.11.007</doi><idGroup><id type="unit" value="CBIN1826"></id></idGroup><countGroup><count type="pageTotal" number="6"></count></countGroup><titleGroup><title type="tocHeading1">Regular Article</title></titleGroup><copyright>© The Author(s) Journal compilation © 2007 International Federation for Cell Biology</copyright><eventGroup><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:3.1.9 mode:FullText" date="2012-12-20"></event><event type="firstOnline" date="2013-01-02"></event><event type="publishedOnlineFinalForm" date="2013-01-02"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-08"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-15"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="263">263</numbering><numbering type="pageLast" number="268">268</numbering></numberingGroup><correspondenceTo> Corresponding author. Tel.: +506 229 0344; fax: +506 292 0485. <email>blomonte@cariari.ucr.ac.cr</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:CBIN.CBIN1826.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 3 August 2006; revised 27 September 2006; accepted 5 November 2006</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="32"></count><count type="linksCrossRef" number="3"></count></countGroup><titleGroup><title type="main">Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A<sub>2</sub> homologues of snake venoms</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>Cindy</givenNames><familyName>Araya</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1" corresponding="yes"><personName><givenNames>Bruno</givenNames><familyName>Lomonte</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="CR"><unparsedAffiliation>Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 2060, Costa Rica</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">Cationic peptides</keyword><keyword xml:id="k2">Antitumor</keyword><keyword xml:id="k3">Phospholipase A<sub>2</sub></keyword><keyword xml:id="k4">Snake venom</keyword><keyword xml:id="k5">Myotoxin</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>The effects of two cationic synthetic peptides, derived from the C‐terminal region of Lys49 phospholipase A<sub>2</sub> homologues from snake venoms, upon various murine tumor cell lines (B16 melanoma, EMT6 mammary carcinoma, S‐180 sarcoma, P3X myeloma, tEnd endothelial cells) were evaluated. The peptides are 13‐mers derived from <i>Agkistrodon piscivorus piscivorus</i> Lys49 PLA<sub>2</sub> (p‐AppK: KKYKAYFKLKCKK) and <i>Bothrops asper</i> Lys49 myotoxin II (pEM‐2[<sc>d</sc>]: KKWRWWLKALAKK), respectively, in the latter case with slight modifications and with all‐<sc>d</sc> amino acids. All tumor cells tested were susceptible to the lytic action of the peptides. The susceptibility of tumor cell lines was not higher than that of C2C12 skeletal muscle myoblasts, utilized as a non‐transformed cell line control. However, in a murine model of subcutaneous solid tumor growth of EMT6 mammary carcinoma, the intraperitoneal administration of pEM‐2[<sc>d</sc>] caused a tumor mass reduction of 36% (<i>p</i> < 0.05), which was of similar magnitude to that achieved by the administration of paclitaxel, an antitumor drug in clinical use. Thus, the C‐terminal peptides of Lys49 phospholipase A<sub>2</sub> homologues present antitumor effects that might be of interest in developing therapeutic strategies against cancer.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms</title></titleInfo><name type="personal"><namePart type="given">Cindy</namePart><namePart type="family">Araya</namePart><affiliation>Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 2060, Costa Rica</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Bruno</namePart><namePart type="family">Lomonte</namePart><affiliation>Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 2060, Costa Rica</affiliation><affiliation>E-mail: blomonte@cariari.ucr.ac.cr</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">2007-03</dateIssued><edition>Received 3 August 2006; revised 27 September 2006; accepted 5 November 2006</edition><copyrightDate encoding="w3cdtf">2007</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="references">32</extent><extent unit="linksCrossRef">3</extent></physicalDescription><abstract lang="en">The effects of two cationic synthetic peptides, derived from the C‐terminal region of Lys49 phospholipase A2 homologues from snake venoms, upon various murine tumor cell lines (B16 melanoma, EMT6 mammary carcinoma, S‐180 sarcoma, P3X myeloma, tEnd endothelial cells) were evaluated. The peptides are 13‐mers derived from Agkistrodon piscivorus piscivorus Lys49 PLA2 (p‐AppK: KKYKAYFKLKCKK) and Bothrops asper Lys49 myotoxin II (pEM‐2[d]: KKWRWWLKALAKK), respectively, in the latter case with slight modifications and with all‐d amino acids. All tumor cells tested were susceptible to the lytic action of the peptides. The susceptibility of tumor cell lines was not higher than that of C2C12 skeletal muscle myoblasts, utilized as a non‐transformed cell line control. However, in a murine model of subcutaneous solid tumor growth of EMT6 mammary carcinoma, the intraperitoneal administration of pEM‐2[d] caused a tumor mass reduction of 36% (p < 0.05), which was of similar magnitude to that achieved by the administration of paclitaxel, an antitumor drug in clinical use. 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