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Effects of three novel metalloproteinases from the venom of the West African saw-scaled viper, Echis ocellatus on blood coagulation and platelets

Howes, J.M., Kamiguti, A. S., Theakston, R.David G., Wilkinson, M. C. and Laing, Gavin (2005) 'Effects of three novel metalloproteinases from the venom of the West African saw-scaled viper, Echis ocellatus on blood coagulation and platelets'. Biochimica Et Biophysica Acta-General Subjects, Vol 1724, Issue 1-2, pp. 194-202.

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Abstract

Two metalloproteinases, a 24-kDa P-I EoVMP1 and a 56-kDa P-III EoVMP2, have recently been isolated from the venom of the West African saw-scaled viper Echis ocellatus. We now reveal a new 65-kDa haemorrhagic group P-III metalloprotemase which we have designated EoVMP3. The aim of this study was to determine whether these three snake venom metalloproteinases (SVmps) affect platelets and blood coagulation. EoVMP1 had no effect on the aggregation of washed human platelets, whereas EoVMP2 inhibited collagen-induced platelet aggregation. In contrast, EoVMP3 did not inhibit the aggregation of platelets by collagen but instead activated platelets in the absence of any additional co-factors. All three SVMPs were capable of activating prothrombin to varying degrees and can therefore be described as procoagulants. EoVMP1, EoVMP2 and EoVMP3 share sequence identity with other members of the reprolysin family, but differ greatly in their effects on some of the components that control haemostasis. (c) 2005 Elsevier B.V. All rights reserved.

Item Type: Article
Uncontrolled Keywords: echis venom metalloproteinase platelet coagulation inhibition bothrops-jararaca venom disintegrin-like domain carpet viper snake-venoms hemorrhagic metalloproteinases alpha(2)beta(1) integrin aggregation inhibitor molecular-cloning gene family jararhagin
Subjects: QW Microbiology and Immunology > Antigens and Antibodies. Toxins and Antitoxins > QW 630 Toxins. Antitoxins
WD Disorders of Systemic, Metabolic or Environmental Origin, etc > Animal Poisons > WD 410 Reptiles
Faculty: Department: Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group
Digital Object Identifer (DOI): https://doi.org/10.1016/j.bbagen.2005.03.011
Depositing User: Sarah Lewis-Newton
Date Deposited: 07 Oct 2011 14:38
Last Modified: 06 Feb 2018 13:02
URI: http://archive.lstmed.ac.uk/id/eprint/1861

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