Purification and characterization of two high molecular mass snake venom metalloproteinases (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegans (Sakishima-habu)

Oyama, Etsuko; Takahashi, Hiroyuki

doi:10.1016/j.toxicon.2015.06.010

Cited by 9 publications

(6 citation statements)

References 26 publications

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“… VaF1 P-IIIa Metalloproteinase, disintegrin-like and cysteine rich domains Vipera ammodytes ammodytes α-fibrinogenase activity Leonardi et al (2015) 3. HR-Ele1 P-IIIa Metalloproteinase, disintegrin-like and cysteine rich domains Protobothrops elegans Hemorrhagic, αβ-fibrinogenase, type I collagenase Oyama and Takahashi (2015) 4. Atrolysin A P-IIIa Metalloproteinase, disintegrin-like and cysteine rich domains Crotalus atrox Hemorrhagic, proteolytic, degrades plasma fibronectin, type-I collagenase, type-IV collagenase, fibrinogenase, gelatinase, sheddase of glycoprotein VI, Fox and Bjarnason, 1995 , Pinto et al, 2007 5.…”

Section: Snake Venom Metalloproteinases (Svmps)mentioning

confidence: 99%

Snake Venom Metalloproteinases (SVMPs): A structure-function update

et al. 2020

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Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain proteins with several biological activities such as the ability to induce hemorrhage, proteolytic degradation of fibrinogen and fibrin, induction of apoptosis and inhibition of platelet aggregation. Due to these activities, SVMPs are responsible for many of the well-known pathological phenotypes in snake envenomations caused particularly by species from the Viperidae family and the Crotalinae subfamily. These proteins have been classified based on their size and domain structure into P–I, P-II and P-III classes. Comparatively, members of the P–I SVMPs possess the simplest structures, formed by the catalytic metalloproteinase domain only; the P-II SVMPs are moderately more complex, having the canonical disintegrin domain in addition to the metalloproteinase domain; members of the P-III class are more structurally varied, comprising the metalloproteinase, disintegrin-like, and cysteine-rich domains. Proteolytic cleavage, repeated domain loss and presence of other ancillary domains are responsible for structural diversities in the P-III class. However, studies continue to unveil the relationship between the structure and function of these proteins. In this review, we recovered evidences from literature on the structural peculiarities and functional classification of Snake Venom Metalloproteinases. In addition, we reflect on diversities that exist among each class while taking into account specific and up-to-date class-based activities.

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Section: Snake Venom Metalloproteinases (Svmps)mentioning

confidence: 99%

Snake Venom Metalloproteinases (SVMPs): A structure-function update

et al. 2020

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“…As SVMPs são sintetizadas como proteínas multimodulares na forma inativa ou zimogênio e de acordo com os aspectos estruturais e funcionais, elas foram classificadas em 3 classes principais (classes P-I, P-II, P-III) e 11 subclasses: P-I, que apresenta somente o domínio metaloprotease, P-II que apresenta a domínio Apesar das SVMPs poderem causar efeitos danosos durante o envenenamento, estas podem atuar na alteração da hemostasia tendo atividades fibrinogenolítica (OYAMA et al, 2015), fibrinolítica e antiplaquetária tornando-se moléculas com alto valor biológico. Muitas SVMPs já se mostraram capazes de atuar como antitumorais ou em processos relacionados ao câncer, como os mecanismos de adesão celular (CORRÊA et al, 2002;GABRIEL et al, 2012).…”

Section: Metaloproteases De Peçonha De Serpentes (Svmps)unclassified

Estratégias Metodológicas De Educação Em Saúde Na Área De Parasitologia Para Aplicação Em Atividades Em Ambientes Não Formais De Ensino Com Crianças, Jovens E Adultos

Teixeira¹,

Gomes²,

Lima³

et al. 2020

Ciências Biológicas: Considerações E Novos Segmentos 2

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Direitos para esta edição cedidos à Atena Editora pelos autores. Todo o conteúdo deste livro está licenciado sob uma Licença de Atribuição Creative Commons. Atribuição 4.0 Internacional (CC BY 4.0). O conteúdo dos artigos e seus dados em sua forma, correção e confiabilidade são de responsabilidade exclusiva dos autores, inclusive não representam necessariamente a posição oficial da Atena Editora. Permitido o download da obra e o compartilhamento desde que sejam atribuídos créditos aos autores, mas sem a possibilidade de alterá-la de nenhuma forma ou utilizá-la para fins comerciais. A Atena Editora não se responsabiliza por eventuais mudanças ocorridas nos endereços convencionais ou eletrônicos citados nesta obra. Todos os manuscritos foram previamente submetidos à avaliação cega pelos pares, membros do Conselho Editorial desta Editora, tendo sido aprovados para a publicação.

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“…On the other hand, P-I and P-III SVMP, which inhibit platelet aggregation, have been purified from the venoms of P. flavoviridis and P. elegans. In addition, HR1A, HR1B [ 22 ], and SV-PAD-2 [ 54 ], which are P-III SVMP, have been isolated from Protobothrops snake venom in Japan. HR1A and HR1B derived from P. flavoviridis venom undergo autoproteolysis and are released as single major fragments of 32 and 34 kDa, respectively, containing D and C domains.…”

Section: Inhibition Of Platelet Aggregationmentioning

confidence: 99%

“…Moreover, SV-PAD-2 from P. elegans venom had a marked effect on adenosine diphosphate (ADP)- and collagen-induced platelet aggregation (half maximal inhibitory concentrations [IC 50 ]: 240 nM and 185 nM, respectively) and rapidly inhibited ADP-induced platelet aggregation. SV-PAD-2 can be subclassified as a P-IIIc SVMP based on the fact that it undergoes dimerization because its molecular mass according to SDS-PAGE was 110 kDa under non-reducing conditions and 52 kDa under reducing conditions [ 54 ].…”

Section: Inhibition Of Platelet Aggregationmentioning

confidence: 99%

Structures and Functions of Snake Venom Metalloproteinases (SVMP) from Protobothrops venom Collected in Japan

Oyama

Takahashi

2017

Molecules

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Snake venom metalloproteinases (SVMP) are widely distributed among the venoms of Crotalinae and Viperidae, and are organized into three classes (P-I, P-II and P-III) according to their size and domain structure. P-I SVMP are the smallest SVMP, as they only have a metalloproteinase (M) domain. P-II SVMP contain a disintegrin-like (D) domain, which is connected by a short spacer region to the carboxyl terminus of the M domain. P-III SVMP contain a cysteine-rich (C) domain, which is attached to the carboxyl terminus of the D domain. Some SVMP exhibit hemorrhagic activity, whereas others do not. In addition, SVMP display fibrinolytic/fibrinogenolytic (FL) activity, and the physiological functions of SVMP are controlled by their structures. Furthermore, these proteinases also demonstrate fibrinogenolytic and proteolytic activity against synthetic substrates for matrix metalloproteinases and ADAM (a disintegrin and metalloproteinase). This article describes the structures and FL, hemorrhagic, and platelet aggregation-inhibiting activity of SVMP derived from Protobothrops snake venom that was collected in Japan.

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Purification and characterization of two high molecular mass snake venom metalloproteinases (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegans (Sakishima-habu)

Cited by 9 publications

References 26 publications

Snake Venom Metalloproteinases (SVMPs): A structure-function update

Snake Venom Metalloproteinases (SVMPs): A structure-function update

Estratégias Metodológicas De Educação Em Saúde Na Área De Parasitologia Para Aplicação Em Atividades Em Ambientes Não Formais De Ensino Com Crianças, Jovens E Adultos

Structures and Functions of Snake Venom Metalloproteinases (SVMP) from Protobothrops venom Collected in Japan

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