The Action of Lonomia achelous Caterpillars Venom on Human Factor V

López, Marcos Pérez; Gil, Amparo; Arocha-Piñango, Carmen Luisa

doi:10.1016/s0049-3848(99)00209-1

Cited by 19 publications

(10 citation statements)

References 38 publications

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“…results]. Finally, the venom of L. achelous contains a FV inhibitor (lonomin Vl:i) which also seems to be a serine protease [22]. On the other hand, the venom of L. obliqua contains a fibrino-(geno)lytic activity which produces fragments different from plasmin and similar to those reported for L. achelous [6,23].…”

Section: Anticoagulant Compoundsmentioning

confidence: 66%

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<i>Lonomia</i> Genus Caterpillar Envenomation: Clinical and Biological Aspects

Arocha-Piñango

Guerrero²

2001

Pathophysiol Haemos Thromb

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Persons who have been in contact with Lonomia achelous or Lonomia obliqua caterpillars present external and internal bleeding and opening of recently healed wounds. Hematological tests show normal platelet count, prolonged prothrombin time, activated partial thromboplastin time and thrombin time, totally corrected by normal plasma. Decreased fibrinogen (Fg), factor (F) V, FXIII, plasminogen and α₂-antiplasmin with increased FVIII: C, von Willebrand factor, Fg degradation products and D dimers. Tissue plasminogen activator, plasminogen activator inhibitor and protein C varied. In L. achelous biological fluids, compounds with anticoagulant or procoagulant properties have been identified. In L. obliqua bristle extracts, mainly procoagulant activities have been identified. Subcutaneous injections of L. achelous crude extracts and a semipurified fraction reduce Fg, plasminogen and FXIII in rabbits. Intravenous injections of a very purified fraction of L. achelous in rabbits produce lysis of preformed thrombi, a decrease of Fg, plasminogen, α₂-antiplasmin, FXIII and inhibition of postthrombolytic thrombus growth. Subcutaneous injections of L. obliqua bristle extracts prolong prothrombin time and activated partial thromboplastin time and reduce FXIII. Intravenous injections of crude bristle extract and a purified fraction of L. obliqua induce disseminated intravascular coagulation.

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Section: Anticoagulant Compoundsmentioning

confidence: 66%

“…In addition, there is a FV activator (lonomin VI:a) which seems to be a metalloproteinase [22]. In L. obliqua, a calciumindependent FX activator [25] and a calciumdependent prothrombin activator named L. obliqua prothrombin activator protease (Lopap) have been identified (table 1).…”

Section: Procoagulant Compoundsmentioning

confidence: 99%

<i>Lonomia</i> Genus Caterpillar Envenomation: Clinical and Biological Aspects

Arocha-Piñango

Guerrero²

2001

Pathophysiol Haemos Thromb

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“…In this respect, it should be noted that besides venom activators of factor V, which have the potential to cause ischemia due to thromboembolism, inactivators of factor V are also among the enzymes that effect this coagulation protein (Table 1). Inactivation of factor V by venom proteases reduces the procoagulant activity of factor V, which causes prolonged clotting times in vitro and is thought to Toxin Reviews Downloaded from informahealthcare.com by McMaster University on 11/03/14 Dermacentor andersoni Inactivation Gordon and Allen, 1991 contribute to bleeding syndromes such as those reported for the venom from the larvae of Lonomia achelous (Lopez et al, 2000). This is in line with the reported effects of factor Va on the kinetic parameters of prothrombin activation (Nesheim et al, 1979;Rosing et al, 1980) that indicate that coagulation factor V is an essential cofactor of the prothrombinase complex.…”

Section: Classification Of Factor V Activators and Inactivatorsmentioning

confidence: 99%

Activation of Factor v by Venom Proteases

Nicolaes

Rosing

2006

Toxin Reviews

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Blood coagulation factor V is the nonenzymatic protein cofactor essential to the formation of thrombin. Activated factor V, FVa, is a cofactor of FXa in the socalled prothrombinase complex. Inclusion of FVa in this complex results in a more than 1,000-fold enhancement of the rate of prothrombin activation. Several animal venoms contain activities that have the capacity to activate human factor V. Besides activators of factor V, inactivating enzymes are also found in animal venoms. Of those venom proteases that affect FV activity, snake venoms of different families, including those of the Viperidae, Crotalidae, and Elapidae, have been most widely studied. Venom factor V activators have proven to be excellent tools in studying the structure-function relationship of factor V(a). In particular, one of the proteases of the Viperidae family, the factor V activator from the venom of Russell's viper (RVV-V) has been very helpful, because it is 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 paper, we present an up-to-date overview of those venom proteases that possess the capacity to activate or inactivate coagulation factor V and, where possible, summarize structural and functional properties of these proteases. Furthermore, we provide a novel detailed three-dimensional homology model for RVV-V, the factor V activator from Russell's viper venom. This model will be helpful to explain the remarkable substrate specificity of RVV-V on the basis of its threedimensional structure.

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“…Lopez and Arocha-Pinango [7] identified a factor V activator in the hemolymph of L. achelous. The partially purified activator ap-Rosing/Govers-Riemslag/Yukelson/ Tans pears to be a thermostable metalloprotease which has a molecular mass less than 97 kD.…”

Section: Factor V Activators Present In the Venoms From Bothrops Atromentioning

confidence: 99%

“…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]. 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.…”

Section: Introductionmentioning

confidence: 99%

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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The Action of Lonomia achelous Caterpillars Venom on Human Factor V

Cited by 19 publications

References 38 publications

<i>Lonomia</i> Genus Caterpillar Envenomation: Clinical and Biological Aspects

<i>Lonomia</i> Genus Caterpillar Envenomation: Clinical and Biological Aspects

Activation of Factor v by Venom Proteases

Factor V Activation and Inactivation by Venom Proteases

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