scholarly journals Duplication of Coagulation Factor Genes and Evolution of Snake Venom Prothrombin Activators

10.5772/23426 ◽  
2011 ◽  
Author(s):  
Shiyang Kwong ◽  
R. Manjunatha
Keyword(s):  
Snake Venom ◽  
Coagulation Factor

scholarly journals The recruitment of blood coagulation factor X into snake venom gland as a toxin

2009 ◽  
Vol 102 (09) ◽  
pp. 469-478 ◽  
Author(s):  
Shiyang Kwong ◽  
Anthony E. Woods ◽  
Peter J. Mirtschin ◽  
Ruowen Ge ◽  
R. Kini
Keyword(s):  
Blood Coagulation ◽  
Snake Venom ◽  
Coagulation Factor ◽  
Venom Gland ◽  
Inducible Expression ◽  
Luciferase Expression ◽  
Factor X ◽  
Cis Elements ◽  
Mammalian Cell Lines ◽  
Intron 1

SummaryTrocarin D is a prothrombin activator from the Tropidechis carinatus venom. It is a functional and structural homologue to mammalian blood coagulation factor Xa.Trocarin D is hypothesised to have evolved from its factor X counterpart (TrFX) through gene duplication and recruitment.The genes of trocarin D and TrFX have significant sequence identities, except for insertions/deletions in their intron 1 and promoter regions. In trocarin D intron 1 region, there are three insertions and two deletions. In trocarin D promoter region, there is a novel 264 bp insertion which has potential cis-elements.This insertion is termed as Venom Recruitment/Switch Element (VERSE) and is hypothesised to account for switching the low-level constitutive expression of factor X in the liver to the high-level inducible expression of trocarin D in the venom gland. To understand the role of VERSE in the trocarin D expression,its cis-elements were characterised by luciferase assays in mammalian cell lines as well as snake venom gland cells. The ability of VERSE to drive luciferase expression is comparable to that of the trocarin D promoter. The predicted cis-elements are important in promoting expression as their mutagenesis resulted in lower luciferase expression.VERSE minimal core promoter and three novel cis-elements (two up-regulatory and one suppressor elements) were identified using deletion/site-directed mutagenesis studies. VERSE is primarily responsible for the increase of trocarin D expression. The insertions/deletions within trocarin D intron 1 need to be characterised for their role in tissue-specific and inducible expression of trocarin D.

Molecular changes during the activation of coagulation factor V by snake venom proteases

1983 ◽  
Vol 2 (3) ◽  
pp. 171-185
Author(s):  
Razia Rawala ◽  
Stefan Niewiarowski ◽  
Robert W. Colman
Keyword(s):  
Snake Venom ◽  
Coagulation Factor ◽  
Factor V ◽  
Molecular Changes ◽  
Coagulation Factor V

scholarly journals Snake Venom Metalloproteinases

2016 ◽  
Vol 62 (1) ◽  
pp. 106-111 ◽  
Author(s):  
Şerban Andrei Gâz Florea ◽  
Adriana Gâz Florea ◽  
Hajnal Kelemen ◽  
Daniela-Lucia Muntean
Keyword(s):  
Snake Venom ◽  
Coagulation Factor ◽  
Short Review ◽  
Post Translational Modifications ◽  
Domain Structures ◽  
Factor Ii ◽  
Hemorrhagic Events ◽  
Switch Mechanism ◽  
Fibrinogenolytic Activity ◽  
Apoptotic Activity

AbstractAs more data are generated from proteome and transcriptome analysis revealing that metalloproteinases represent most of the Viperid and Colubrid venom components authors decided to describe in a short review a classification and some of the multiple activities of snake venom metalloproteinases. SVMPs are classified in three major classes (P-I, P-II and P-III classes) based on the presence of various domain structures and according to their domain organization. Furthermore, P-II and P-III classes were separated in subclasses based on distinctive post-translational modifications. SVMPs are synthesized in a latent form, being activated through a Cys-switch mechanism similar to matrix metalloproteinases. Most of the metalloproteinases of the snake venom are responsible for the hemorrhagic events but also have fibrinogenolytic activity, poses apoptotic activity, activate blood coagulation factor II and X, inhibit platelet aggregation, demonstrating that SVMPs have multiple functions in addition to well-known hemorrhagic function.

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