CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom

It has been recently demonstrated that the hemotoxic venom activity of several species of snakes can be inhibited by carbon monoxide (CO) or a metheme forming agent. These and other data suggest that the biometal, heme, may be attached to venom enzymes and may be modulated by CO. A novel fibrinogeno...

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Bibliographic Details
Published in:Biometals 2018-08, Vol.31 (4), p.585-593
Main Authors: Suntravat, Montamas, Langlais, Paul R., Sánchez, Elda E., Nielsen, Vance G.
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Biomedical and Life Sciences
Blood Coagulation - drug effects
Blood plasma
Carbon monoxide
Carbon Monoxide - pharmacology
Cell Biology
Crotalid Venoms - enzymology
Crotalus
Crotalus atrox
Fibrinogen - metabolism
Heme
Heme - metabolism
Kinetics
Life Sciences
Mass spectroscopy
Medicine/Public Health
Metalloproteases - antagonists & inhibitors
Metalloproteases - isolation & purification
Metalloproteases - metabolism
Metalloproteinase
Microbiology
Molecular chains
Pharmacology/Toxicology
Plant Physiology
Proteolysis
Snakes
Venom
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Summary:It has been recently demonstrated that the hemotoxic venom activity of several species of snakes can be inhibited by carbon monoxide (CO) or a metheme forming agent. These and other data suggest that the biometal, heme, may be attached to venom enzymes and may be modulated by CO. A novel fibrinogenolytic metalloproteinase, named CatroxMP-II, was isolated and purified from the venom of a Crotalus atrox viper, and subjected to proteolysis and mass spectroscopy. An ion similar to the predicted singly charged m/z of heme at 617.18 was identified. Lastly, CORM-2 (tricarbonyldichlororuthenium (II) dimer, a CO releasing molecule) inhibited the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma. In conclusion, we present the first example of a snake venom metalloproteinase that is heme-bound and CO-inhibited.
ISSN:0966-0844
1572-8773
DOI:10.1007/s10534-018-0107-5