Skip to main navigation Skip to search Skip to main content

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

  • J. M. Howes
  • , A. S. Kamiguti
  • , R. D.G. Theakston
  • , Mark Wilkinson
  • , G. D. Laing
  • Liverpool School of Tropical Medicine
  • University of Liverpool

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)194-202
Number of pages9
JournalBiochimica et Biophysica Acta - General Subjects
Volume1724
Issue number1-2
DOIs
Publication statusPublished - 20 Jun 2005

Keywords

  • Coagulation
  • Echis
  • Inhibition
  • Metalloproteinase
  • Platelet
  • Venom

Fingerprint

Dive into the research topics of 'Effects of three novel metalloproteinases from the venom of the West African saw-scaled viper, Echis ocellatus on blood coagulation and platelets'. Together they form a unique fingerprint.

Cite this