Biochemical characterization of atroxase and nucleotide sequence encoding the fibrinolytic enzyme

Tu, Anthony T.; Baker, Brenda; Wongvibulsin, Sirima; Willis, T. W.

doi:10.1016/s0041-0101(96)00106-7

Cited by 27 publications

(14 citation statements)

References 7 publications

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“…Fibrinogenolytic activity affected mostly the Aα-chain, had a time-dependent effect on Bβ-chains and did not affect at all the γ-chain, all of which suggests the presence of both metalloproteinases and serine proteases . Similar fibrinogenolytic activity patterns have been also reported for venoms of several other viperid species (Tu et al, 1996;Retzios Markland, 1994;Siigur et al, 1998;Rodrigues et al, 2000;Ramos et al, 2003;Leonardi et al, 2007). The absence of specific activity of the venom on the γ-chain of fibrinogen also suggests that M. xanthina venom fibrinogenases do not activate plasminogen leading to plasmin formation, which cleaves peptide bonds at the carboxy-terminal side of lysine residues in the Aα-, Bβ-and γ-chains of fibrinogen (Markland, 1998).…”

Section: Discussionsupporting

confidence: 75%

Electrophoretic Characterization of Venom Proteins of <em>Montivipera xanthina</em> (Gray, 1849) (Ophidia: Viperidae)

Arıkan

Keskin²,

Çiçek³

2017

bah

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In this study, with the aim of evaluating coagulant activities in the venom of Mo ntivipera xanthina, we analyzed venom proteins, digestion patterns of fibrinogen chains incubated with venom, and the effects of protease inhibitors on M. xanthina venom proteases. Venom samples were obtained from four adult specimens collected in Gümüldür (Izmir, Turkey). SDS-PAGE analysis showed the presence of 17 protein bands or band groups in the molecular mass range of 20 to 200 kDa. The specific digestion patterns of fibrinogen chains revealed that M. xanthina venom possesses fibrinogenolytic enzymes, which could be involved in coagulation processes during envenomation. Fibrinogenolytic activity affected the Aα-chain and showed a time-dependent effect on Bβ-chains, which suggests the presence of both metalloproteinases and serine proteases in M. xanthina venom. After observing the fibrinogenolytic activity of M. xanthina venom, further research should focus on the isolation, identification, and characterization of individual venom components in order to provide insight into their function and biological roles.

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Section: Discussionsupporting

confidence: 75%

Electrophoretic Characterization of Venom Proteins of <em>Montivipera xanthina</em> (Gray, 1849) (Ophidia: Viperidae)

Arıkan

Keskin²,

Çiçek³

2017

bah

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“…Non-hemorrhagic SVMPs: Adamalysin II from Crotalus adamanteus (Gomis-Ruth, 1993); H2 from Trimeresurus Xavoviridis (Kumasaka et al, 1996); Fibrolase from Agkistrodon contortrix contortrix (Randolph et al, 1992); ACLPREF from Agkistrodon contortrix laticinctus (Selistre de Araujo and Ownby, 1995). VlF from Vipera lebetina (Gasmi et al, 2000); Atroxase from Crotalus Atrox (Tu et al, 1996); Neuwiedase from Bothrops neuwiedi (Rodrigues et al, 2000). Hemorrhagic SVMPs: Lebetase from Vipera lebetina (Siigur et al, 1998); Acutolysin A from A. acutus (Gong et al, 1998); HT-2 from Crotalus ruber rubber (Takeya et al, 1990); atrolysin C from Crotalus atrox (Zhang et al, 1994); BaP1 from Bothrops asper (Watanabe et al, 2003); LHFII from Lachesis muta muta (Sanchez et al, 1991); ACLPREH from Agkistrodon contortrix laticinctus (Selistre de Araujo and Ownby, 1995); TM-3 from Taiwan Habu (Huang et al, 2002a,b).…”

Section: The Tri-peptide Inhibitor Binding and Its Evects On The Actimentioning

confidence: 99%

“…Like other SVMPs of the P-I class, such as Wbrolase from Agkistrodon contortrix contortrix (Randolph et al, 1992), atroxase from Crotalus atrox (Tu et al, 1996), lebetase from Vipera lebetina (Siigur et al, 1998), neuwiedase from Bothrops neuwied (Rodrigues et al, 2000) and BaPl from Bothrops asper (Gutierrez et al, 1995), FII can directly degrade the -and -chains of Wbrin and Wbrinogen in vitro (Chen et al, 1993;Liang et al, 2001) and dissolve thrombus eVectively in vivo (Chen et al, 1998), but have no inXuence on tissue-type plasminogen activator and plasminogen activator inhibitor-1 activities in plasma (Liang et al, 2001). These results imply that snake venom metalloproteinase FII has potential therapeutic use in dissolving thrombi.…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus

Lou

Hou

Liang

et al. 2005

Journal of Structural Biology

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“…It was observed that the thrombolytic effect of mut-IIa was not reversible, and blood flow from ear microcirculation remained without hemorrhage or significant alterations over a 60 min observation period (Carvalho-Tavares and Sanchez, in preparation). The thrombolytic potencial of additional P-I SVMPs, atroxase from C. atrox at a dosage of 6 mg/kg [82] and a fibrinogenase from Vipera lebetine (5 mg/kg) [83], have been examined in rat models. The reports on these enzymes reveal that intravenous administration of atroxase or fibrinogenase at the indicated dosages resulted in thrombolysis within 1 hour injection.…”

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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Biochemical characterization of atroxase and nucleotide sequence encoding the fibrinolytic enzyme

Cited by 27 publications

References 7 publications

Electrophoretic Characterization of Venom Proteins of <em>Montivipera xanthina</em> (Gray, 1849) (Ophidia: Viperidae)

Electrophoretic Characterization of Venom Proteins of <em>Montivipera xanthina</em> (Gray, 1849) (Ophidia: Viperidae)

Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus

Proteases from South American Snake Venoms Affecting Fibrinolysis

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