Morphological and physiological responses of rat renal glomeruli to the i.v. injection of Bothrops moojeni snake venom

It has been demonstrated that thrombin can split skeletal muscle actin (Muszbek and Laki, PNAS 1974,71,2208). In the present paper the effect of thrombin-like snake venom proteases (Ancrod and Batroxobins of Bothrops moojeni and Bothrops marajoensis) on actin was studied and compared to the thrombic cleavage of this protein. Only EDTA pretreated G and F actin were split by Ancrod, while, Batroxobins hydrolized native G actin, too. The time course of digestion was followed by SDS PAGE. A split product of 37500 m.w. appeared first which was cleaved further resulting in three lower m.w. fragments. The SDS gel pattern of thrombic fragmentation was well distinguishable from those caused by Ancrod and Batroxobins. The first split products of Batroxobin digestion were isolated and by estimating their N-, and C-terminal end groups and amino acid compositions the peptide bond hydrolyzed first was located in the primary structure of actin. It was established that while thrombin split off two actinopeptides (at Arg ( 28)-Ala(29) and Arg ( 39)-His ( 40) from the N-terminal end of the molecule only Arg ( 39)-His ( 40) was cleaved by Batroxobins.

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A New Platelet-Aggregation-Inhibiting Factor Isolated fromBothrops moojeniSnake Venom

BioMed Research International ◽

10.1155/2017/4315832 ◽

2017 ◽

Vol 2017 ◽

pp. 1-9 ◽

Cited By ~ 2

Author(s):

Bruna Barbosa de Sousa ◽

Carla Cristine Neves Mamede ◽

Mariana Santos Matias ◽

Déborah Fernanda da Cunha Pereira ◽

Mayara Ribeiro de Queiroz ◽

...

Keyword(s):

Platelet Aggregation ◽

Snake Venom ◽

Platelet Rich Plasma ◽

Functional Characterization ◽

Adenosine Diphosphate ◽

Inhibitory Effect ◽

Single Chain ◽

Inhibiting Factor ◽

Reducing Conditions ◽

Bothrops Moojeni

This work reports the purification and functional characterization of BmooPAi, a platelet-aggregation-inhibiting factor fromBothrops moojenisnake venom. The toxin was purified by a combination of three chromatographic steps (ion-exchange on DEAE-Sephacel, molecular exclusion on Sephadex G-75, and affinity chromatography on HiTrap™ Heparin HP). BmooPAi was found to be a single-chain protein with an apparent molecular mass of 32 kDa on 14% SDS-PAGE, under reducing conditions. Sequencing of BmooPAi by Edman degradation revealed the amino acid sequence LGPDIVPPNELLEVM. The toxin was devoid of proteolytic, haemorrhagic, defibrinating, or coagulant activities and induced no significant oedema or hyperalgesia. BmooPAi showed a rather specific inhibitory effect on ristocetin-induced platelet aggregation in human platelet-rich plasma, whereas it had little or no effect on platelet aggregation induced by collagen and adenosine diphosphate. The results presented in this work suggest that BmooPAi is a toxin comprised of disintegrin-like and cysteine-rich domains, originating from autolysis/proteolysis of PIII SVMPs fromB. moojenisnake venom. This toxin may be of medical interest because it is a platelet aggregation inhibitor, which could potentially be developed as a novel therapeutic agent to prevent and/or treat patients with thrombotic disorders.

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Characterization Of A Hemagglutinating Glycoprotein Isolated From Bothrops Moojeni Snake Venom

Protein and Peptide Letters ◽

10.2174/0929866013409760 ◽

2001 ◽

Vol 8 (1) ◽

pp. 13-20 ◽

Cited By ~ 6

Author(s):

B. Kassab ◽

D. de Carvalho ◽

S. Marangoni ◽

J. Novello

Keyword(s):

Snake Venom ◽

Bothrops Moojeni

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Hepatic alterations after the i.v. administration of Bothrops moojeni snake venom in wistar rats

Toxicon ◽

10.1016/s0041-0101(00)80139-7 ◽

2000 ◽

Vol 38 (4) ◽

pp. 583

Keyword(s):

Snake Venom ◽

Wistar Rats ◽

Bothrops Moojeni

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Isolation and characterization of two new Lys49 PLA2s with heparin neutralizing properties from Bothrops moojeni snake venom

Toxicon ◽

10.1016/j.toxicon.2009.12.007 ◽

2010 ◽

Vol 55 (6) ◽

pp. 1080-1092 ◽

Cited By ~ 1

Author(s):

Anna Maria Perchuc ◽

Laure Menin ◽

Philippe Favreau ◽

Beatrice Bühler ◽

Philippe Bulet ◽

...

Keyword(s):

Snake Venom ◽

Isolation And Characterization ◽

Bothrops Moojeni

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Treatment with a Zinc Metalloprotease Purified from Bothrops moojeni Snake Venom (BmooMP-Alpha-I) Reduces the Inflammation in an Experimental Model of Dextran Sulfate Sodium-Induced Colitis

Mediators of Inflammation ◽

10.1155/2019/5195134 ◽

2019 ◽

Vol 2019 ◽

pp. 1-9 ◽

Cited By ~ 1

Author(s):

Maraisa Cristina Silva ◽

Helioswilton Sales-Campos ◽

Carlo José Freire Oliveira ◽

Tamires Lopes Silva ◽

Flávia Batista Ferreira França ◽

...

Keyword(s):

Experimental Model ◽

Snake Venom ◽

Dextran Sulfate ◽

Dextran Sulfate Sodium ◽

Intestinal Inflammation ◽

Biological Effects ◽

Clinical Signs ◽

Tissue Architecture ◽

Anti Inflammatory ◽

Bothrops Moojeni

It has been described that the metalloprotease BmooMP-alpha-I purified from Bothrops moojeni snake venom is able to hydrolyze the TNF molecule. However, this observation has been based mainly on in vitro investigation, in addition to molecular modeling and docking approaches. Considering that there is no in vivo study to demonstrate the biological effects of this enzyme, the major aim to the present work was to investigate whether the BmooMP-alpha-I has any anti-inflammatory efficacy by setting up a murine experimental design of colitis induced by dextran sulfate sodium (DSS). For this purpose, C57BL/6 mice were divided into six groups, as follows: (i) animals without intestinal inflammation, (ii) animals without intestinal inflammation treated with BmooMP-alpha-I (50 μg/animal/day), and (iii) animals with intestinal inflammation induced by 3% of DSS, (iv) mice with intestinal inflammation induced by DSS and treated with BmooMP-alpha-I enzyme at the 50, 25, or 12.5 μg/animal/day dosages by intraperitoneal route. Clinical signs of colitis were observed daily for calculating the morbidity scores, cytokine measurements, and histological features. We observed that the animals treated with different doses of the enzyme presented a remarkable improvement of colitis signs, as confirmed by a significant increase of the intestine length in comparison to the DSS group. Also, no difference was observed between the groups treated with the enzyme or vehicle, as the colon length of these animals was slightly lower than that of the group of healthy animals, without induction of intestinal inflammation. The cytokine quantification in supernatants of intestinal tissue homogenates showed a significant reduction of 38% in IFN-gamma levels, when the animals were treated with 50 μg of the BmooMP-alpha-I compared to the animals receiving DSS only. A significant reduction of 39% in TNF levels was also observed in all doses of treatment with BmooMP-alpha-I, in addition to a significant reduction of 35% in the amount of IL-12p40. Histological examinations revealed that the BmooMP-alpha-I 50 μg treated group preserved colon architecture and goblet cells and reduced the ulcer area, when compared with DSS mice, which showed typical inflammatory changes in tissue architecture, such as ulceration, crypt dilation, loss of tissue architecture, and goblet cell depletion, accompanied by a significant cell infiltration. In conclusion, our results suggest that the improvement of clinical scores and histological findings related to BmooMP-alpha-I treatment in this experimental model could be attributed to the metalloprotease ability to modulate cytokine production locally at the inflamed intestine. These findings highlight the potential anti-inflammatory role and effectiveness of this enzyme as a therapeutic alternative in this type of immunopathological condition.

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