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Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms

Identifieur interne : 002C72 ( Main/Exploration ); précédent : 002C71; suivant : 002C73

Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms

Auteurs : Cindy Araya [Costa Rica] ; Bruno Lomonte [Costa Rica]

Source :

RBID : ISTEX:2EAFEB48E226E56C407278CAF1C10FD4C30E7ADD

Descripteurs français

English descriptors

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


Affiliations:


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Le document en format XML

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<term>Cell Death (drug effects)</term>
<term>Crotalid Venoms (chemistry)</term>
<term>Group II Phospholipases A2</term>
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<term>Peptide Fragments (pharmacology)</term>
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<term>Animaux</term>
<term>Antinéoplasiques (pharmacologie)</term>
<term>Cellules cancéreuses en culture</term>
<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (pharmacologie)</term>
<term>Fragments peptidiques (synthèse chimique)</term>
<term>Group II Phospholipases A2</term>
<term>Injections péritoneales</term>
<term>Membranes ()</term>
<term>Mort cellulaire ()</term>
<term>Phospholipases A ()</term>
<term>Phospholipases A2</term>
<term>Protéines de reptiles</term>
<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Séquence d'acides aminés</term>
<term>Tumeurs expérimentales (anatomopathologie)</term>
<term>Tumeurs expérimentales (métabolisme)</term>
<term>Tumeurs expérimentales (traitement médicamenteux)</term>
<term>Tumeurs expérimentales de la mamelle (traitement médicamenteux)</term>
<term>Venins de crotalidé ()</term>
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<term>Crotalid Venoms</term>
<term>Peptide Fragments</term>
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<term>Peptide Fragments</term>
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<term>Cell Death</term>
<term>Membranes</term>
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<term>Mammary Neoplasms, Experimental</term>
<term>Neoplasms, Experimental</term>
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<term>Tumeurs expérimentales</term>
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<term>Animals</term>
<term>Antimicrobial</term>
<term>Antimicrobial activity</term>
<term>Antimicrobial peptides</term>
<term>Antitumor</term>
<term>Antitumor activity</term>
<term>Antitumor effect</term>
<term>Antitumor effects</term>
<term>Asper</term>
<term>Bactericidal activity</term>
<term>Biol chem</term>
<term>Body weight</term>
<term>Bothrops</term>
<term>Bothrops asper</term>
<term>Bothrops asper snake venom</term>
<term>Carcinoma cells</term>
<term>Cationic</term>
<term>Cationic peptides</term>
<term>Cell biology</term>
<term>Cell line control</term>
<term>Cell lines</term>
<term>Comparative study</term>
<term>Costa rica</term>
<term>Crotalid snake venoms</term>
<term>Cytolytic</term>
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<term>Fetal calf serum</term>
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<term>Homologues</term>
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<term>Innate immunity</term>
<term>International federation</term>
<term>Intraperitoneal route</term>
<term>Lactate dehydrogenase</term>
<term>Latter case</term>
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<term>Lytic action</term>
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<term>Murine tumor cell lines</term>
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<term>Myotoxic phospholipases</term>
<term>Myotoxin</term>
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<term>Papo</term>
<term>Peptide</term>
<term>Phospholipase</term>
<term>Phospholipases A2</term>
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<term>Pla2</term>
<term>Pla2 homologues</term>
<term>Present work</term>
<term>Proc natl acad</term>
<term>Reptilian Proteins</term>
<term>Similar magnitude</term>
<term>Skeletal muscle</term>
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<term>Snake venom</term>
<term>Snake venoms</term>
<term>Synthetic peptides</term>
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<term>Tumor cell lines</term>
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<term>Tumor growth</term>
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<term>Venom</term>
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<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>
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