Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms
Identifieur interne : 002C72 ( Main/Exploration ); précédent : 002C71; suivant : 002C73Antitumor effects of cationic synthetic peptides derived from Lys49 phospholipase A2 homologues of snake venoms
Auteurs : Cindy Araya [Costa Rica] ; Bruno Lomonte [Costa Rica]Source :
- Cell Biology International [ 1065-6995 ] ; 2007-03.
Descripteurs français
- KwdFr :
- Animaux, Antinéoplasiques (pharmacologie), Cellules cancéreuses en culture, Fragments peptidiques (), Fragments peptidiques (pharmacologie), Fragments peptidiques (synthèse chimique), Group II Phospholipases A2, Injections péritoneales, Membranes (), Mort cellulaire (), Phospholipases A (), Phospholipases A2, Protéines de reptiles, Souris, Souris de lignée BALB C, Séquence d'acides aminés, Tumeurs expérimentales (anatomopathologie), Tumeurs expérimentales (métabolisme), Tumeurs expérimentales (traitement médicamenteux), Tumeurs expérimentales de la mamelle (traitement médicamenteux), Venins de crotalidé ().
- MESH :
- anatomopathologie : Tumeurs expérimentales.
- métabolisme : Tumeurs expérimentales.
- pharmacologie : Antinéoplasiques, Fragments peptidiques.
- synthèse chimique : Fragments peptidiques.
- traitement médicamenteux : Tumeurs expérimentales, Tumeurs expérimentales de la mamelle.
- Animaux, Cellules cancéreuses en culture, Fragments peptidiques, Group II Phospholipases A2, Injections péritoneales, Membranes, Mort cellulaire, Phospholipases A, Phospholipases A2, Protéines de reptiles, Souris, Souris de lignée BALB C, Séquence d'acides aminés, Venins de crotalidé.
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.
- Teeft :
- Amino Acid Sequence, Animals, 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, Group II Phospholipases A2, High concentrations, Homologues, Injections, Intraperitoneal, Innate immunity, International federation, Intraperitoneal route, Lactate dehydrogenase, Latter case, Lomonte, Lomonte cell biology, Lytic action, Mice, Mice, Inbred BALB C, Murine, Murine tumor cell lines, Myotoxic, Myotoxic phospholipases, Myotoxin, Normal cells, Papo, Peptide, Phospholipase, Phospholipases A2, Piscivorus, Pla2, Pla2 homologues, Present work, Proc natl acad, Reptilian Proteins, Similar magnitude, Skeletal muscle, Skeletal muscle myoblasts, Snake venom, Snake venoms, Synthetic peptides, Toxicon, Toxicon lomonte, Toxin, Tumor Cells, Cultured, 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
Affiliations:
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Le document en format XML
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<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>
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<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>
</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="anatomopathologie" xml:lang="fr"><term>Tumeurs expérimentales</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="métabolisme" xml:lang="fr"><term>Tumeurs expérimentales</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Neoplasms, Experimental</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antinéoplasiques</term>
<term>Fragments peptidiques</term>
</keywords>
<keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Fragments peptidiques</term>
</keywords>
<keywords scheme="MESH" qualifier="traitement médicamenteux" xml:lang="fr"><term>Tumeurs expérimentales</term>
<term>Tumeurs expérimentales de la mamelle</term>
</keywords>
<keywords scheme="Teeft" xml:lang="en"><term>Amino Acid Sequence</term>
<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>
<term>Cytolytic activity</term>
<term>Cytolytic effect</term>
<term>Emt6</term>
<term>Endothelial cells</term>
<term>Fetal calf serum</term>
<term>Group II Phospholipases A2</term>
<term>High concentrations</term>
<term>Homologues</term>
<term>Injections, Intraperitoneal</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>Mice</term>
<term>Mice, Inbred BALB C</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>Phospholipases A2</term>
<term>Piscivorus</term>
<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>
<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 Cells, Cultured</term>
<term>Tumor cell lines</term>
<term>Tumor cells</term>
<term>Tumor growth</term>
<term>Tumor mass reduction</term>
<term>Tumor masses</term>
<term>Venom</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules cancéreuses en culture</term>
<term>Fragments peptidiques</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>Venins de crotalidé</term>
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<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>
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