Effects of three novel metalloproteinases from the venom of the West African saw-scaled viper, Echis ocellatus on blood coagulation and platelets.
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 metalloproteinase 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.
Howes
J-M
JM
Venom Research Unit, Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK.
Kamiguti
A S
AS
Theakston
R D G
RD
Wilkinson
M C
MC
Laing
G D
GD
D000595:Amino Acid Sequence; D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects*; D005340:Fibrinogen / Q000037:antagonists & inhibitors / Q000737:chemistry; D045726:Metalloproteases / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010974:Platelet Aggregation / Q000187:drug effects*; D011516:Prothrombin / Q000037:antagonists & inhibitors / Q000737:chemistry; D014757:Viper Venoms / Q000201:enzymology* / Q000302:isolation & purification; D017819:Viperidae / Q000378:metabolism
D014757:Viper Venoms; D011516:Prothrombin; D005340:Fibrinogen; D045726:Metalloproteases