Source:http://linkedlifedata.com/resource/pubmed/id/19708222
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2009-8-26
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pubmed:abstractText |
Two non-toxic PLA2s were purified to homogeneity from Cerastes cerastes Tunisian snake venom. The purification process employed gel filtration on Sephadex G-75 followed by C18 reverse phase high-pressure liquid chromatography. These two acidic enzymes, namely CC-PLA2-1 and CC-PLA2-2, have a molecular weight of 13,737.52 and 13,705.63 Da, respectively. These two PLA2 are the first reported glycosylated phospholipases A2 purified from snake venom. The rates of glycosylation are 2.5% and 0.5% (w/w), respectively. Specific activities of 1800 U/mg and 2400 U/mg for CC-PLA2-1 and CC-PLA2-2, respectively, were measured at optimal conditions. CC-PLA2-1 and CC-PLA2-2 strongly inhibited coagulation. They also exhibited a marked dose-dependent inhibitory effect on platelet aggregation induced by ADP and arachidonic acid in platelet-rich plasma. Interestingly, CC-PLA2-1 and CC-PLA2-2 inhibited in a dose-dependent manner adhesion of IGR39 melanoma and HT1080 fibrosarcoma cells to fibrinogen and fibronectin. Furthermore, both CC-PLA2-1 and CC-PLA2-2 abolished HT1080 cell migration towards fibrinogen and fibronectin. This activity is reported for the first time for PLA2 enzymes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1879-3150
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pubmed:author |
pubmed-author:BazaaAmineA,
pubmed-author:BezzineSofianeS,
pubmed-author:El AyebMohamedM,
pubmed-author:KarrayAidaA,
pubmed-author:LoretErwannE,
pubmed-author:LuisJoséJ,
pubmed-author:MarrakchiNazihaN,
pubmed-author:OlfaKallech-ZiriKZ,
pubmed-author:Srairi-AbidNajetN,
pubmed-author:Zouari-KessentiniRaoudhaR
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
444-53
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pubmed:meshHeading |
pubmed-meshheading:19708222-Amino Acid Sequence,
pubmed-meshheading:19708222-Animals,
pubmed-meshheading:19708222-Blood Coagulation,
pubmed-meshheading:19708222-Blood Platelets,
pubmed-meshheading:19708222-Cell Adhesion,
pubmed-meshheading:19708222-Cell Line, Tumor,
pubmed-meshheading:19708222-Cell Movement,
pubmed-meshheading:19708222-Humans,
pubmed-meshheading:19708222-Molecular Sequence Data,
pubmed-meshheading:19708222-Phospholipases A2,
pubmed-meshheading:19708222-Rabbits,
pubmed-meshheading:19708222-Viper Venoms,
pubmed-meshheading:19708222-Viperidae
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pubmed:year |
2009
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pubmed:articleTitle |
Two purified and characterized phospholipases A2 from Cerastes cerastes venom, that inhibit cancerous cell adhesion and migration.
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pubmed:affiliation |
Laboramtoire des Venins et Toxines, Institut Pasteur de Tunis, 13 Place Pasteur, BP.74, 1002 Tunis Belvédère, Tunisia. zouari_raoudha@yahoo.fr
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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