title: CcMP-II, a new hemorrhagic metalloproteinase from Cerastes cerastes snake venom: purification, biochemical characterization and amino acid sequence analysis.
abstract: 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 35kDa 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.
authors.affiliation: USTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, BP 32, El-Alia Bab Ezzouar, 16111 Algiers, Algeria.
authors.forename: Hinda
authors.initials: H
authors.lastname: Boukhalfa-Abib
authors.affiliation: USTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, BP 32, El-Alia Bab Ezzouar, 16111 Algiers, Algeria. Electronic address: flaraba@hotmail.com.
authors.forename: Fatima
authors.initials: F
authors.lastname: Laraba-Djebari
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002364:Caseins / Q000378:metabolism; D005337:Fibrin; D005340:Fibrinogen / Q000378:metabolism; D006470:Hemorrhage / Q000139:chemically induced; D045726:Metalloproteases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D051379:Mice; D014757:Viper Venoms / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D017819:Viperidae / Q000502:physiology*
chemical_list: D002364:Caseins; D014757:Viper Venoms; D005337:Fibrin; D005340:Fibrinogen; D045726:Metalloproteases
keywords: Cerastes cerastes; Hemorrhage; Metalloproteinase; Snake venom