Activation of bovine factor V by an activator purified from the venom of Naja naja oxiana

Gerads, Inge; Tans, Guido; Yukel'son, L. Ya.; Zwaal, R.F.A.; Rosing, Jan

doi:10.1016/0041-0101(92)90052-7

Cited by 26 publications

(43 citation statements)

References 32 publications

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“…The N. n. oxiana protease activates factor V by cleaving two peptide bonds yielding a factor Va molecule which, compared with thrombin-activated factor V, has a somewhat smaller heavy and larger light chain [6]. These small differences have a rather large effect on the cofactor activity of factor Va in prothrombin activation.…”

Section: Factor V Activator From the Venom Of Naja Naja Oxianamentioning

confidence: 99%

“…During a screening of the pro-and anticoagulant properties of snake venoms from the Elapidae family it was observed that the venoms from several Naja species were able to activate factor V [6,15]. The factor V activator present in the venom of N. n. oxiana, which contained the largest amount of activator, was purified by repeated chromatography on a Mono S column [6].…”

Section: Factor V Activator From the Venom Of Naja Naja Oxianamentioning

confidence: 99%

“…The factor V activator present in the venom of N. n. oxiana, which contained the largest amount of activator, was purified by repeated chromatography on a Mono S column [6]. The purified activator appears to be a single-chain protein which, as judged by polyacrylamide gel electrophoresis in the presence of SDS, has an apparent molecular mass of 48 kD.…”

Section: Factor V Activator From the Venom Of Naja Naja Oxianamentioning

confidence: 99%

“…Already around 1960 it was reported that Russel's viper venom contains both a potent factor X [3] and a factor V activator [4]. In 1978 it was shown that thrombocytin, the throm- bin-like enzyme from Bothrops atrox was able to activate factor V [5] and in the early 1990s our laboratory in Maastricht reported that the venom of several Naja species contained a factor V activator [6]. Recently, it was shown that the bristles from certain South American caterpillars contain two different proteases that can activate and inactivate factor V, respectively [7].…”

Section: Introductionmentioning

confidence: 99%

“…Recently, it was shown that the bristles from certain South American caterpillars contain two different proteases that can activate and inactivate factor V, respectively [7]. The venom factor V activator from Naja naja oxiana partially inactivates thrombin-activated factor V [6], and unpublished observations reported in the present paper indicate that the venom from Vipera lebetina turanica is also able to inactivate factor Va. In this paper we will provide further information on the structural and functional properties of the factor V activators and inactivators.…”

Section: Introductionmentioning

confidence: 99%

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Factor V Activation and Inactivation by Venom Proteases

Rosing

Govers‐Riemslag

Yukel'son

et al. 2001

Pathophysiol Haemos Thromb

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Blood coagulation factor V is a single-chain glycoprotein with M_r = 330,000 which plays an important role in the procoagulant and anticoagulant pathways. Thrombin activates factor V into factor Va, a two-chain molecule which is composed of a heavy (M_r = 105,000) and a light chain (M_r = 71,000/74,000). Factor Va accelerates factor Xa-catalysed prothrombin activation more than 1,000-fold and under physiological conditions the cofactor activity of factor Va in prothrombin activation is down-regulated by activated protein C. Factor V can also be activated by a wide variety of snake venoms (e.g. from Vipera species, Naja naja oxiana, Bothrops atrox) and by proteases present in the bristles of a South American caterpillar (Lonomia achelous). Some venoms, notably of Vipera lebetina turanica and Lonomia achelous, contain proteases that are able to inactivate factor V or factor Va. Venom factor V activators are excellent tools in studying the structure-function relationship of factor V(a) and they are also used in diagnostic tests for quantification of plasma factor V levels and for the screening of defects in the protein C pathway. In this review, the structural and functional properties of animal venom factor V activators and inactivators is described.

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Section: Factor V Activator From the Venom Of Naja Naja Oxianamentioning

confidence: 99%

Section: Factor V Activator From the Venom Of Naja Naja Oxianamentioning

confidence: 99%

Section: Factor V Activator From the Venom Of Naja Naja Oxianamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Factor V Activation and Inactivation by Venom Proteases

Rosing

Govers‐Riemslag

Yukel'son

et al. 2001

Pathophysiol Haemos Thromb

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Diagnostic Use of Snake Venom Components in the Coagulation Laboratory

Perchuc

Wilmer

2010

Toxins and Hemostasis

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Kinetics of an autocatalytic zymogen reaction in the presence of an inhibitor coupled to a monitoring reaction

Manjabacas

Valero

García-Moreno

et al. 1996

Bltn Mathcal Biology

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A global kinetic analysis of a model consisting of an autocatalytic zymogen-activation process, in which an irreversible inhibitor competes with the zymogen for the active site of the proteinase, and a monitoring coupled reaction, in which the enzyme acts upon one of its substrates, is presented. This analysis is based on the progress curves of any of the two products released in the monitoring reaction. The general solution is applied to an important particular case in which rapid equilibrium conditions prevail. Finally, we suggest a procedure to predict whether the inhibition or activation route dominates in the steady state of the system. These results generalize our previous analysis of simpler mechanisms.

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Activation of bovine factor V by an activator purified from the venom of Naja naja oxiana

Cited by 26 publications

References 32 publications

Factor V Activation and Inactivation by Venom Proteases

Factor V Activation and Inactivation by Venom Proteases

Diagnostic Use of Snake Venom Components in the Coagulation Laboratory

Kinetics of an autocatalytic zymogen reaction in the presence of an inhibitor coupled to a monitoring reaction

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