Biological and Thrombolytic Properties of Fibrolase -A New Fibrinolytic Protease from Snake Venom

Ahmed, N.; Gaddis, R R; Tennant, K.D.; Lacz, J P

doi:10.1159/000216147

Cited by 9 publications

(5 citation statements)

References 12 publications

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“…Recent interest has been generated in snake venom direct-acting fibrinolytic metalloproteinases because of their clinical potential for the treatment of occlusive vascular disease. Several of these enzymes have been tested in vivo with promising results (23,47,55,77,79,101). These studies revealed that the highly purified fibrinolytic snake venom enzymes produced consistent thrombolysis.…”

mentioning

confidence: 99%

Snake Venom Fibrinogenolytic and Fibrinolytic Enzymes: An Updated Inventory

Markland

1998

Thromb Haemost

103

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mentioning

confidence: 99%

Snake Venom Fibrinogenolytic and Fibrinolytic Enzymes: An Updated Inventory

Markland

1998

Thromb Haemost

103

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“…On the other hand, using an animal model of arterial thrombosis, fibrolase dissolves femoral arterial clots after a single intravenous bolus administration. These data revealed the potential of this fibrinolytic enzyme to treat occlusive thrombotic disease, but the problem was that fibrolase is not a plasminogen activator [66]. Therefore, an alternative strategy is to produce a chimeric derivative from fibrolase that possesses the dual ability to degrade fibrin clots and to inhibit platelet aggregation and thrombus reformation.…”

Section: Fibrinolytic Enzyme Activitymentioning

confidence: 99%

Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases

et al. 2021

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Cardiovascular diseases (CVDs) are considered as a major cause of death worldwide. Therefore, identifying and developing therapeutic strategies to treat and reduce the prevalence of CVDs is a major medical challenge. Several drugs used for the treatment of CVDs, such as captopril, emerged from natural products, namely snake venoms. These venoms are complex mixtures of bioactive molecules, which, among other physiological networks, target the cardiovascular system, leading to them being considered in the development and design of new drugs. In this review, we describe some snake venom molecules targeting the cardiovascular system such as phospholipase A2 (PLA2), natriuretic peptides (NPs), bradykinin-potentiating peptides (BPPs), cysteine-rich secretory proteins (CRISPs), disintegrins, fibrinolytic enzymes, and three-finger toxins (3FTXs). In addition, their molecular targets, and mechanisms of action—vasorelaxation, inhibition of platelet aggregation, cardioprotective activities—are discussed. The dissection of their biological effects at the molecular scale give insights for the development of future snake venom-derived drugs.

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“…Among the fibrinolytic P-I SVMPs with potential as thrombolytic therapeutics, fibrolase from A. c. contortrix has been documented to have strong fibrinolytic activity in vitro [70,71]. In addition, the enzyme has been tested in experimental rabbit [72] and canine [73] animal model systems as a thrombolytic agent against artificially created thrombi.…”

Section: P-i Class Svmps As Potential Thrombolytic Enzymesmentioning

confidence: 99%

Proteases from South American Snake Venoms Affecting Fibrinolysis

Sanchez¹,

Swenson

2007

CPA

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Venoms of the viperidae (vipers and pit vipers) snakes are rich sources of proteinases which render fibrinogen incoagulable and solubilize fibrin. Many of these compounds have profound effects (stimulating or inhibiting) on the hemostatic mechanism, including, blood coagulation cascade, fibrinolysis, hypotension, vascular integrity and platelet function. The lethality of a venom often appears to be due to the combined action of several of these components, but severe consequences are frequently connected with hemostatic disorders. Viperid snake bite accidents in human and other large animals are characterized by localized or generalized bleeding and or thrombotic sequelae. This review is focused on the structural properties and features of a number of South American snake venom enzymes possessing clearly defined (pro)fibrinolytic activity. Under physiological conditions the venom proteins active on the plasminogen/fibrinolytic system can be grouped into two main categories: 1) direct-acting fibrinolytic endoproteinases which are related in amino acid sequence to the major family of metalloproteinases known as the metzincins. The members of this group are zinccontaining metalloproteinases (SVMPs) varying in size from 20 to 100 kDa and often more than one example is present in the same venom. 2) serine proteinases which specifically activate plasminogen into plasmin, and contain at least one catalytic domain structurally similar to trypsin. A number of these proteinases have been isolated and their mechanism of action established. Both direct and indirect endoproteinases on their own are practically nontoxic; however, they may act synergistically with other factors aggravating their toxic effects. Moreover, these proteinases are characterized by a relatively high degree of substrate specificity and resistance to physiological inhibitors. Indeed, some of these venom components are thought to hold promise as agents for medical applications in the field of thrombosis and diagnosis, or to hold the key for the design of pharmaceuticals.

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Biological and Thrombolytic Properties of Fibrolase -A New Fibrinolytic Protease from Snake Venom

Cited by 9 publications

References 12 publications

Snake Venom Fibrinogenolytic and Fibrinolytic Enzymes: An Updated Inventory

Snake Venom Fibrinogenolytic and Fibrinolytic Enzymes: An Updated Inventory

Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases

Proteases from South American Snake Venoms Affecting Fibrinolysis

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