CcMP-II, a new hemorrhagic metalloproteinase from Cerastes cerastes snake venom: purification, biochemical characterization and amino acid sequence analysis
| Autor: | Hinda Boukhalfa-Abib, Fatima Laraba-Djebari |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Physiology
Health Toxicology and Mutagenesis Venom Hemorrhage Viper Venoms Matrix metalloproteinase Toxicology complex mixtures Biochemistry chemistry.chemical_compound Type IV collagen Mice Viperidae Animals Amino Acid Sequence Envenomation Metalloproteinase Fibrin biology Chemistry Caseins Fibrinogen Cell Biology General Medicine Anatomy Cerastes cerastes biology.organism_classification Snake venom Metalloproteases PMSF |
| Zdroj: | Comparative biochemistry and physiology. Toxicologypharmacology : CBP. 167 |
| ISSN: | 1532-0456 |
| Popis: | Snake venom metalloproteinases (SVMPs) are the most abundant components in snake venoms. They are important in the induction of systemic alterations and local tissue damage after envenomation. CcMP-II, which is a metalloproteinase purified from Cerastes cerastes snake venom, was obtained by a combination of gel filtration, ion-exchange and affinity chromatographies. It was homogeneous on SDS-PAGE, with a molecular mass estimated to 35 kDa and presents a pI of 5.6. CcMP-II has an N-terminal sequence of EDRHINLVSVADHRMXTKY, with high levels of homology with those of the members of class P-II of SVMPs, which comprises metalloproteinase and disintegrin-like domains together. This proteinase displayed a fibrinogenolytic and hemorrhagic activities. The proteolytic and hemorrhagic activities of CcMP-II were inhibited by EDTA and 1,10-phenanthroline. However, these activities were not affected by aprotinine and PMSF, suggesting that CcMP-II is a zinc-dependent hemorrhagic metalloproteinase with an α-fibrinogenase activity. The hemorrhagic metalloproteinase CcMP-II was also able to hydrolyze extracellular matrix components, such as type IV collagen and laminin. These results indicate that CcMP-II is implicated in the local and systemic bleeding, contributing thus in the toxicity of C. cerastes venom. |
| Databáze: | OpenAIRE |
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