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Article: Oral treatment with a chemically characterized parsley (

Frattani, Flávia Serra / Assafim, Mariane / Casanova, Livia Marques / de Souza, Jacqueline Elis / Chaves, Douglas Siqueira de Almeida / Costa, Sônia Soares / Zingali, Russolina Benedeta

Journal of traditional and complementary medicine

2020 Volume 11, Issue 3, Page(s) 287–291

Abstract: Petroselinum ... ...

Abstract	Petroselinum crispum
Language	English
Publishing date	2020-04-17
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2709698-1
ISSN	2225-4110
ISSN	2225-4110
DOI	10.1016/j.jtcme.2020.04.003
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Article ; Online: Exploiting the antithrombotic effect of the (pro)thrombin inhibitor bothrojaracin.

Assafim, Mariane / Frattani, Flávia S / Ferreira, Marcos S / Silva, Dione M / Monteiro, Robson Q / Zingali, Russolina B

Toxicon : official journal of the International Society on Toxinology

2016 Volume 119, Page(s) 46–51

Abstract: Bothrojaracin is a 27 kDa C-type lectin-like protein from Bothrops jararaca snake venom. It behaves as a potent thrombin inhibitor upon high-affinity binding to thrombin exosites. Bothrojaracin also forms a stable complex with prothrombin that can be ... ...

Abstract	Bothrojaracin is a 27 kDa C-type lectin-like protein from Bothrops jararaca snake venom. It behaves as a potent thrombin inhibitor upon high-affinity binding to thrombin exosites. Bothrojaracin also forms a stable complex with prothrombin that can be detected in human plasma. Formation of the zymogen-inhibitor complex severely decreases prothrombin activation and contributes to the anticoagulant activity of bothrojaracin. In the present study, we employed two rodent models to evaluate the antithrombotic effect of bothrojaracin in vivo: stasis-induced thrombosis and thrombin-induced pulmonary thromboembolism. It was observed that bothrojaracin interacts with rat prothrombin in plasma. Ex-vivo assays showed stable complex formation even after 24 h of a single bothrojaracin dose. As a result, bothrojaracin showed significant antithrombotic activity in a rat venous thrombosis model elicited by thromboplastin combined with stasis. The antithrombotic activity of bothrojaracin (1 mg/kg) persisted for up to 24 h and it was associated with moderate bleeding as assessed by a tail transection method. Formation of bothrojaracin-prothrombin complex has been also observed following intravenous administration of the inhibitor into mice. As a result, bothrojaracin effectively protected mice from thrombin-induced fatal thromboembolism. We conclude that bothrojaracin is a potent antithrombotic agent in vivo and may serve as a prototype for the development of new zymogen-directed drugs that could result in prolonged half-life and possible decreased hemorrhagic risk.
MeSH term(s)	Animals ; Antithrombins/toxicity ; Crotalid Venoms/toxicity ; Female ; Male ; Mice ; Mice, Inbred BALB C ; Prothrombin/antagonists & inhibitors ; Rats ; Rats, Wistar
Chemical Substances	Antithrombins ; Crotalid Venoms ; bothrojaracin (150633-76-4) ; Prothrombin (9001-26-7)
Language	English
Publishing date	2016-09-01
Publishing country	England
Document type	Journal Article
ZDB-ID	204479-1
ISSN	1879-3150 ; 0041-0101
ISSN (online)	1879-3150
ISSN	0041-0101
DOI	10.1016/j.toxicon.2016.05.007
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Article: Phenolic chemical composition of Petroselinum crispum extract and its effect on haemostasis.

Chaves, Douglas S A / Frattani, Flávia S / Assafim, Mariane / de Almeida, Ana Paula / de Zingali, Russolina B / Costa, Sônia S

Natural product communications

2011 Volume 6, Issue 7, Page(s) 961–964

Abstract: From the aqueous extract (Pc) of Petroselinum crispum (Mill) flat leaves specimens were isolated and identified the flavonoids apigenin (1), apigenin-7-O-glucoside or cosmosiin (2), apigenin-7-O-apiosyl-(1 --> 2)-O-glucoside or apiin (3) and the coumarin ...

Abstract	From the aqueous extract (Pc) of Petroselinum crispum (Mill) flat leaves specimens were isolated and identified the flavonoids apigenin (1), apigenin-7-O-glucoside or cosmosiin (2), apigenin-7-O-apiosyl-(1 --> 2)-O-glucoside or apiin (3) and the coumarin 2",3"-dihydroxyfuranocoumarin or oxypeucedanin hydrate (4). The inhibitory activity toward clotting formation and platelet aggregation was assessed for Pc flavonoids (1) and (2), and the coumarin (4). Pc showed no inhibition on clotting activity when compared with the control. On the other hand, a strong antiplatelet aggregation activity was observed for Pc (IC50 = 1.81 mg/mL), apigenin (IC50 = 0.036 mg/mL) and cosmosiin (IC50 = 0.18 mg/mL). In all cases ADP was used as inductor of platelet aggregation. Our results showed that Pc, apigenin and cosmosiin interfere on haemostasis inhibiting platelet aggregation. To the best of our knowledge this is the first report for the cosmosiin antiplatelet aggregation in vitro activity.
MeSH term(s)	Coumarins/chemistry ; Coumarins/isolation & purification ; Coumarins/pharmacology ; Flavonoids/chemistry ; Flavonoids/isolation & purification ; Flavonoids/pharmacology ; Humans ; Inhibitory Concentration 50 ; Molecular Structure ; Nuclear Magnetic Resonance, Biomolecular ; Optical Rotation ; Partial Thromboplastin Time ; Petroselinum/chemistry ; Plant Extracts/chemistry ; Plant Extracts/isolation & purification ; Plant Extracts/pharmacology ; Plant Leaves/chemistry ; Platelet Aggregation Inhibitors/chemistry ; Platelet Aggregation Inhibitors/isolation & purification ; Platelet Aggregation Inhibitors/pharmacology ; Prothrombin Time ; Spectrometry, Mass, Electrospray Ionization
Chemical Substances	Coumarins ; Flavonoids ; Plant Extracts ; Platelet Aggregation Inhibitors
Language	English
Publishing date	2011-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1934-578X
ISSN	1934-578X
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Article: Bothrojaracin, a Bothrops jararaca snake venom-derived (pro)thrombin inhibitor, as an anti-thrombotic molecule.

Zingali, Russolina B / Ferreira, Marcos S / Assafim, Mariane / Frattani, Flávia S / Monteiro, Robson Q

Pathophysiology of haemostasis and thrombosis

2005 Volume 34, Issue 4-5, Page(s) 160–163

Abstract: Bothrojaracin (BJC) is a selective and potent thrombin inhibitor (KD = 0.6 nM) which also binds to prothrombin on proexosite I (KD = 175 nM). Incubation of BJC with human or rat plasma produced a band that co-migrates with purified prothrombin-BJC ... ...

Abstract	Bothrojaracin (BJC) is a selective and potent thrombin inhibitor (KD = 0.6 nM) which also binds to prothrombin on proexosite I (KD = 175 nM). Incubation of BJC with human or rat plasma produced a band that co-migrates with purified prothrombin-BJC complex. We further analyzed the in vivo anti-thrombotic effect of BJC on a venous thrombosis model in rats that combines stasis and hypercoagulability. The administration of 1 mg/kg (i.v.) doses of BJC decreased thrombus weight by approximately 95%. Evaluation of the in vivo effect of BJC in mice using a pulmonary thromboembolism model induced by thrombin showed that BJC protects 100% of mice from death. Altogether, our data show that BJC is a potent anti-thrombotic agent that could further help the development of new prothrombin-directed drugs.
MeSH term(s)	Animals ; Crotalid Venoms/therapeutic use ; Humans ; Murinae ; Snake Venoms/therapeutic use ; Thrombin/antagonists & inhibitors ; Venous Thrombosis/drug therapy
Chemical Substances	Crotalid Venoms ; Snake Venoms ; bothrojaracin (150633-76-4) ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2005
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2080537-8
ISSN	1424-8840 ; 1424-8832
ISSN (online)	1424-8840
ISSN	1424-8832
DOI	10.1159/000092416
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Suramin counteracts the haemostatic disturbances produced by Bothrops jararaca snake venom.

Fernandes, Renato S / Assafim, Mariane / Arruda, Emerson Z / Melo, Paulo A / Zingali, Russolina B / Monteiro, Robson Q

Toxicon : official journal of the International Society on Toxinology

2007 Volume 49, Issue 7, Page(s) 931–938

Abstract: Snakebite accidents produced by Bothrops jararaca typically results in haemostatic changes including pro- and anticoagulant disturbs as well as interference with platelets. Suramin is a hexasulfonated naphthylurea derivative that was recently ... ...

Abstract	Snakebite accidents produced by Bothrops jararaca typically results in haemostatic changes including pro- and anticoagulant disturbs as well as interference with platelets. Suramin is a hexasulfonated naphthylurea derivative that was recently characterized as a thrombin inhibitor (Monteiro et al., 2004. Suramin interaction with human alpha-thrombin: inhibitory effects and binding studies. Int. J. Biochem. Cell Biol. 36(10), 2077-2085). Here, we evaluated the ability of suramin to counteract some of the haemostatic disturbs produced by B. jararaca venom. In vitro assays showed that suramin inhibited venom-induced hydrolysis of a number of synthetic substrates: S-2238, S-2266, S-2302 and S-2288, being this ability more prominent towards the thrombin substrate S-2238 (IC(50)=4.3 microM). It was also observed that suramin impaired the fibrinogen clotting induced by B. jararaca venom (IC(50)=124 microM). Accordingly, increasing concentrations of suramin progressively delayed venom-induced plasma clotting, with complete inhibition attained at concentrations above 1.0 mM. In addition, the platelet-aggregating properties of B. jararaca venom were inhibited by suramin in a dose-dependent fashion (IC(50)=127 microM). Suramin showed no effect in the in vivo hemorrhagic effect of venom in mouse skin. The in vivo effect of suramin was further tested using a previously established venous thrombosis model in rats induced by intravenous administration of B. jararaca venom combined with stasis. Venom doses of 100 microg/kg produced 100% of thrombus incidence (10.6+/-1.7 mg). On the other hand, previous administration of suramin partially inhibited thrombus formation. Thus, 12.5 or 25 mg/kg of suramin decreased thrombus weight by 24% and 40%, respectively. Remarkably, co-administration of 3 microL/kg of antibothropic serum (which has no effect on thrombus formation) and 12.5 mg/kg of suramin decreased thrombus weight by 75%, suggesting a synergic effect. Altogether, we demonstrate here that suramin inhibits in vitro and in vivo haemostatic changes caused by B. jararaca venom. At this point, this drug could be of potential interest for association with conventional antiserum therapy.
MeSH term(s)	Animals ; Blood Coagulation/drug effects ; Bothrops ; Crotalid Venoms/antagonists & inhibitors ; Crotalid Venoms/toxicity ; Hemostasis/drug effects ; Male ; Mice ; Suramin/pharmacology
Chemical Substances	Crotalid Venoms ; Suramin (6032D45BEM)
Language	English
Publishing date	2007-06-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	204479-1
ISSN	1879-3150 ; 0041-0101
ISSN (online)	1879-3150
ISSN	0041-0101
DOI	10.1016/j.toxicon.2007.01.002
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Article ; Online: Hypericum brasiliense plant extract neutralizes some biological effects of Bothrops jararaca snake venom.

Assafim, Mariane / de Coriolano, Eduardo Coriolano / Benedito, Sérgio Eufrázio / Fernandes, Caio Pinho / Lobo, Jonathas Felipe Revoredo / Sanchez, Eladio Florez / Rocha, Leandro Machado / Fuly, André Lopes

Journal of venom research

2011 Volume 2, Page(s) 11–16

Abstract: Alternative treatments for snake bite are currently being extensively studied, and plant metabolites are considered good candidates for such purpose. Here, the ability of a crude ethanolic extract of Hypericum brasiliense plant in neutralizing Bothrops ... ...

Abstract	Alternative treatments for snake bite are currently being extensively studied, and plant metabolites are considered good candidates for such purpose. Here, the ability of a crude ethanolic extract of Hypericum brasiliense plant in neutralizing Bothrops jararaca snake venom was investigated by in vitro (coagulation, hemolysis or proteolysis) and in vivo (hemorrhage, lethality and edema) biological assays. We describe for the first time the ability of H. brasiliense extracts to inhibit some pharmacological effects of a Brazilian snake venom. Inhibitory assays were performed by incubating B. jararaca venom with H. brasiliense extracts for 30min at room temperature before the assays were performed. The results showed that H. brasiliense extracts impaired lethality, edema, hemorrhage, hemolysis, proteolysis as well as fibrinogen or plasma clotting induced by B. jararaca venom. This indicates that H. brasiliense extracts can provide promising agents to treat B. jararaca envenomation.
Language	English
Publishing date	2011-05-25
Publishing country	England
Document type	Journal Article
ISSN	2044-0324
ISSN (online)	2044-0324
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Article: Ecotin modulates thrombin activity through exosite-2 interactions.

Castro, Helena C / Monteiro, Robson Q / Assafim, Mariane / Loureiro, Natália I V / Craik, Charles / Zingali, Russolina B

The international journal of biochemistry & cell biology

2006 Volume 38, Issue 11, Page(s) 1893–1900

Abstract: Ecotin is a Escherichia coli-derived protein that has been characterized as a potent inhibitor of serine-proteases. This protein is highly effective against several mammalian enzymes, which includes pancreatic and neutrophil-derived elastases, ... ...

Abstract	Ecotin is a Escherichia coli-derived protein that has been characterized as a potent inhibitor of serine-proteases. This protein is highly effective against several mammalian enzymes, which includes pancreatic and neutrophil-derived elastases, chymotrypsin, trypsin, factor Xa, and kallikrein. In this work we showed that ecotin binds to human alpha-thrombin via its secondary binding site, and modulates thrombin catalytic activity. Formation of wild type ecotin-alpha-thrombin complex was observed by native PAGE and remarkably, gel filtration chromatography showed an unusual 2:1 ecotin:enzyme stoichiometry. Analysis of the protease inhibitor effects on thrombin biological activities showed that (i) it decreases the inhibition of thrombin by heparin/antithrombin complex (IC50=3.2 microM); (ii) it produces a two-fold increase in the thrombin-induced fibrinogen clotting; and (iii) it inhibits thrombin-induced platelet aggregation (IC50=4.5 microM). Allosteric changes on thrombin structure were then evaluated. Complex formation with ecotin caused a three-fold increase in the rate of thrombin inhibition by BPTI, suggesting a displacement of the enzyme's 60-loop. In addition, ecotin modulated the enzyme's catalytic site, as demonstrated by changes in the fluorescence emission of fluorescein-FPRCK-alpha-thrombin (EC50=3.5 microM). Finally, solid phase competition assays demonstrated that heparin and prothrombin fragment 2 prevents thrombin interaction with ecotin. Altogether, these observations strongly support an ecotin interaction with thrombin anion-binding exosite-2, resulting in modulation of its biological activities. At this point, ecotin might be useful as a new tool for studying thrombin allosteric modulation.
MeSH term(s)	Binding Sites ; Dose-Response Relationship, Drug ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/metabolism ; Escherichia coli Proteins/pharmacology ; Humans ; Periplasmic Proteins/chemistry ; Periplasmic Proteins/metabolism ; Periplasmic Proteins/pharmacology ; Platelet Aggregation/drug effects ; Platelet Aggregation Inhibitors/pharmacology ; Protein Binding/drug effects ; Protein Conformation/drug effects ; Serine Endopeptidases/metabolism ; Serine Proteinase Inhibitors/chemistry ; Serine Proteinase Inhibitors/metabolism ; Serine Proteinase Inhibitors/pharmacology ; Spectrometry, Fluorescence ; Thrombin/metabolism
Chemical Substances	Eco protein, E coli ; Escherichia coli Proteins ; Periplasmic Proteins ; Platelet Aggregation Inhibitors ; Serine Proteinase Inhibitors ; Serine Endopeptidases (EC 3.4.21.-) ; Thrombin (EC 3.4.21.5)
Language	English
Publishing date	2006
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1228429-4
ISSN	1878-5875 ; 1357-2725
ISSN (online)	1878-5875
ISSN	1357-2725
DOI	10.1016/j.biocel.2006.05.001
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Article: Counteracting effect of glycyrrhizin on the hemostatic abnormalities induced by Bothrops jararaca snake venom.

Assafim, Mariane / Ferreira, Marcos S / Frattani, Flávia S / Guimarães, Jorge A / Monteiro, Robson Q / Zingali, Russolina B

British journal of pharmacology

2006 Volume 148, Issue 6, Page(s) 807–813

Abstract: 1. Envenomation by the snake Bothrops jararaca is typically associated with hemostatic abnormalities including pro- and anticoagulant disturbances. Glycyrrhizin (GL) is a plant-derived thrombin inhibitor that also exhibits in vivo antithrombotic ... ...

Abstract	1. Envenomation by the snake Bothrops jararaca is typically associated with hemostatic abnormalities including pro- and anticoagulant disturbances. Glycyrrhizin (GL) is a plant-derived thrombin inhibitor that also exhibits in vivo antithrombotic properties. Here, we evaluated the ability of GL to counteract the hemostatic abnormalities promoted by B. jararaca venom. 2. GL inhibited the human fibrinogen clotting (IC50 = approximately 1.0 mg ml(-1); 1.2 mM), H-D-phenylalanyl-L-pipecolyl-L-arginine-p-nitroanilide dihydrochloride hydrolysis (IC50 = approximately 0.4 mg ml(-1); 0.47 mM) and platelet aggregation (IC50 = approximately 0.28 mg ml(-1); 0.33 mM) induced by B. jararaca venom, in vitro. 3. The in vivo effect of GL was tested in rats using a model of venous thrombosis in which intravenous (i.v.) administration of B. jararaca venom (100 microg kg(-1)) produced in all animals a thrombus with a mean weight of 10.6+/-1.7 mg. 4. Prior administration of GL (180 mg kg(-1)) or antibothropic serum (27 microl kg(-1)) inhibited thrombus formation by 86 and 67%, respectively. Remarkably, co-administration of ineffective doses of GL and antibothropic serum markedly decreased thrombus weight, suggesting a synergistic effect. 5. Co-administration of GL with antibothropic serum abolished venom-induced bleeding. Ex vivo clotting times showed that rat plasma was non-clotting after i.v. administration of B. jararaca venom. Treatment with GL, antibothropic serum or both before venom administration efficiently prevented this abnormality. 6. Altogether, we demonstrate here that GL prevents both in vitro and in vivo venom-induced changes in hemostasis, suggesting a potential antiophidic activity.
MeSH term(s)	Animals ; Antivenins/pharmacology ; Bothrops ; Crotalid Venoms/poisoning ; Glycyrrhizic Acid/pharmacology ; Hemorrhage/drug therapy ; Hemostasis/drug effects ; Partial Thromboplastin Time ; Prothrombin Time ; Rabbits ; Rats ; Rats, Wistar ; Venous Thrombosis/drug therapy
Chemical Substances	Antivenins ; Crotalid Venoms ; Glycyrrhizic Acid (6FO62043WK)
Language	English
Publishing date	2006-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80081-8
ISSN	1476-5381 ; 0007-1188
ISSN (online)	1476-5381
ISSN	0007-1188
DOI	10.1038/sj.bjp.0706786
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Article: Bothrojaracin, a ; Snake Venom-Derived (Pro)Thrombin Inhibitor, as an Anti-Thrombotic Molecule

Zingali, Russolina B. / Ferreira, Marcos S. / Assafim, Mariane / Frattani, Flávia S. / Monteiro, Robson Q.

Pathophysiology of Haemostasis and Thrombosis

2006 Volume 34, Issue 4-5, Page(s) 160–163

Institution	Instituto de Bioquímica Médica, CCS, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil
Abstract	Bothrojaracin (BJC) is a selective and potent thrombin inhibitor (KD = 0.6 nM) which also binds to prothrombin on proexosite I (KD = 175 nM). Incubation of BJC with human or rat plasma produced a band that co-migrates with purified prothrombin-BJC complex. We further analyzed the in vivo anti-thrombotic effect of BJC on a venous thrombosis model in rats that combines stasis and hypercoagulability. The administration of 1 mg/kg (i.v.) doses of BJC decreased thrombus weight by ∼95%. Evaluation of the in vivo effect of BJC in mice using a pulmonary thromboembolism model induced by thrombin showed that BJC protects 100% of mice from death. Altogether, our data show that BJC is a potent anti-thrombotic agent that could further help the development of new prothrombin-directed drugs.
Keywords	Prothrombin ; Bothrojaracin ; Snake venom ; Anti-thrombotic effects ; Thrombin
Language	English
Publishing date	2006-05-19
Publisher	S. Karger AG
Publishing place	Basel, Switzerland
Document type	Article
Note	Paper
ZDB-ID	2080537-8
ISBN	978-3-8055-8150-9 ; 978-3-318-01375-7 ; 3-8055-8150-5 ; 3-318-01375-7
ISSN	1424-8840 ; 1424-8832
ISSN (online)	1424-8840
ISSN	1424-8832
DOI	10.1159/000092416
Database	Karger publisher's database

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Article ; Online: Bothrojaracin, a Bothrops jararaca Snake Venom-Derived (Pro)Thrombin Inhibitor, as an Anti-Thrombotic Molecule

Zingali, Russolina B. / Ferreira, Marcos S. / Assafim, Mariane / Frattani, Flávia S. / Monteiro, Robson Q.

Pathophysiology of Haemostasis and Thrombosis

2005 Volume 34, Issue 4-5, Page(s) 160–163

Abstract	Bothrojaracin (BJC) is a selective and potent thrombin inhibitor (KD = 0.6 nM) which also binds to prothrombin on proexosite I (KD = 175 nM). Incubation of BJC with human or rat plasma produced a band that co-migrates with purified prothrombin-BJC complex. We further analyzed the in vivo anti-thrombotic effect of BJC on a venous thrombosis model in rats that combines stasis and hypercoagulability. The administration of 1 mg/kg (i.v.) doses of BJC decreased thrombus weight by ∼95%. Evaluation of the in vivo effect of BJC in mice using a pulmonary thromboembolism model induced by thrombin showed that BJC protects 100% of mice from death. Altogether, our data show that BJC is a potent anti-thrombotic agent that could further help the development of new prothrombin-directed drugs.
Keywords	Bothrojaracin ; Snake venom ; Anti-thrombotic effects ; Thrombin ; Prothrombin
Language	English
Publisher	S. Karger AG
Publishing place	Basel
Publishing country	Switzerland
Document type	Article ; Online
ISSN	1424-8840 ; 1424-8832 ; 1424-8832
ISSN (online)	1424-8840
ISSN	1424-8832
DOI	10.1159/000092416
Database	Karger publisher's database

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