Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms.
Identifieur interne : 002208 ( PubMed/Corpus ); précédent : 002207; suivant : 002209Antitumor 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.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antineoplastic Agents (pharmacology), Cell Death (drug effects), Crotalid Venoms (chemistry), Group II Phospholipases A2, Injections, Intraperitoneal, Mammary Neoplasms, Experimental (drug therapy), Membranes (drug effects), Mice, Mice, Inbred BALB C, Neoplasms, Experimental (drug therapy), Neoplasms, Experimental (metabolism), Neoplasms, Experimental (pathology), Peptide Fragments (chemical synthesis), Peptide Fragments (chemistry), Peptide Fragments (pharmacology), Phospholipases A (chemistry), Phospholipases A2, Reptilian Proteins, Tumor Cells, Cultured.
- MESH :
- chemical , chemical synthesis : Peptide Fragments.
- chemical , chemistry : Crotalid Venoms, Peptide Fragments, Phospholipases A.
- chemical , pharmacology : Antineoplastic Agents, Peptide Fragments.
- drug effects : Cell Death, Membranes.
- drug therapy : Mammary Neoplasms, Experimental, Neoplasms, Experimental.
- metabolism : Neoplasms, Experimental.
- pathology : Neoplasms, Experimental.
- Amino Acid Sequence, Animals, Group II Phospholipases A2, Injections, Intraperitoneal, Mice, Mice, Inbred BALB C, Phospholipases A2, Reptilian Proteins, Tumor Cells, Cultured.
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.
DOI: 10.1016/j.cellbi.2006.11.007
PubMed: 17178238
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pubmed:17178238Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms.</title><author><name sortKey="Araya, Cindy" sort="Araya, Cindy" uniqKey="Araya C" first="Cindy" last="Araya">Cindy Araya</name><affiliation><nlm:affiliation>Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 2060, Costa Rica.</nlm:affiliation></affiliation></author><author><name sortKey="Lomonte, Bruno" sort="Lomonte, Bruno" uniqKey="Lomonte B" first="Bruno" last="Lomonte">Bruno Lomonte</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17178238</idno><idno type="pmid">17178238</idno><idno type="doi">10.1016/j.cellbi.2006.11.007</idno><idno type="wicri:Area/PubMed/Corpus">002208</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002208</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms.</title><author><name sortKey="Araya, Cindy" sort="Araya, Cindy" uniqKey="Araya C" first="Cindy" last="Araya">Cindy Araya</name><affiliation><nlm:affiliation>Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 2060, Costa Rica.</nlm:affiliation></affiliation></author><author><name sortKey="Lomonte, Bruno" sort="Lomonte, Bruno" uniqKey="Lomonte B" first="Bruno" last="Lomonte">Bruno Lomonte</name></author></analytic><series><title level="j">Cell biology international</title><idno type="ISSN">1065-6995</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antineoplastic Agents (pharmacology)</term><term>Cell Death (drug effects)</term><term>Crotalid Venoms (chemistry)</term><term>Group II Phospholipases A2</term><term>Injections, Intraperitoneal</term><term>Mammary Neoplasms, Experimental (drug therapy)</term><term>Membranes (drug effects)</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Neoplasms, Experimental (drug therapy)</term><term>Neoplasms, Experimental (metabolism)</term><term>Neoplasms, Experimental (pathology)</term><term>Peptide Fragments (chemical synthesis)</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (pharmacology)</term><term>Phospholipases A (chemistry)</term><term>Phospholipases A2</term><term>Reptilian Proteins</term><term>Tumor Cells, Cultured</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Crotalid Venoms</term><term>Peptide Fragments</term><term>Phospholipases A</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antineoplastic Agents</term><term>Peptide Fragments</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Death</term><term>Membranes</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Mammary Neoplasms, Experimental</term><term>Neoplasms, Experimental</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Neoplasms, Experimental</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Neoplasms, Experimental</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Group II Phospholipases A2</term><term>Injections, Intraperitoneal</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Phospholipases A2</term><term>Reptilian Proteins</term><term>Tumor Cells, Cultured</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml: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. Thus, the C-terminal peptides of Lys49 phospholipase A2 homologues present antitumor effects that might be of interest in developing therapeutic strategies against cancer.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17178238</PMID><DateCompleted><Year>2007</Year><Month>05</Month><Day>17</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1065-6995</ISSN><JournalIssue CitedMedium="Print"><Volume>31</Volume><Issue>3</Issue><PubDate><Year>2007</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Cell biology international</Title><ISOAbbreviation>Cell Biol. Int.</ISOAbbreviation></Journal><ArticleTitle>Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms.</ArticleTitle><Pagination><MedlinePgn>263-8</MedlinePgn></Pagination><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Araya</LastName><ForeName>Cindy</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José 2060, Costa Rica.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lomonte</LastName><ForeName>Bruno</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>11</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Cell Biol 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