New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom

Amorim, Fernanda Gobbi; Menaldo, Danilo L.; Carone, Sante Emmanuel Imai; Silva, Thiago A.; Sartim, Marco A.; Pauw, Edwin De; Quinton, Loïc; Sampaio, Suely Vilela

doi:10.3390/toxins10120500

Cited by 19 publications

(17 citation statements)

References 61 publications

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“…In venoms, serine proteases are present in a wide span of animals as well, being well described in snakes and bees. These proteases have thrombin-like effects, promote fibrinogen degradation in prey and activate the phenoloxidase cascade that induces a lethal melanization response in insects attacking bees and their hives [ 36 , 37 , 38 ].…”

Section: Discussionmentioning

confidence: 99%

Specific Antiproliferative Properties of Proteinaceous Toxin Secretions from the Marine Annelid Eulalia sp. onto Ovarian Cancer Cells

et al. 2021

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As Yondelis joins the ranks of approved anti-cancer drugs, the benefit from exploring the oceans’ biodiversity becomes clear. From marine toxins, relevant bioproducts can be obtained due to their potential to interfere with specific pathways. We explored the cytotoxicity of toxin-bearing secretions of the polychaete Eulalia onto a battery of normal and cancer human cell lines and discovered that the cocktail of proteins is more toxic towards an ovarian cancer cell line (A2780). The secretions’ main proteins were identified by proteomics and transcriptomics: 14-3-3 protein, Hsp70, Rab3, Arylsulfatase B and serine protease, the latter two being known toxins. This mixture of toxins induces cell-cycle arrest at G2/M phase after 3h exposure in A2780 cells and extrinsic programmed cell death. These findings indicate that partial re-activation of the G2/M checkpoint, which is inactivated in many cancer cells, can be partly reversed by the toxic mixture. Protein–protein interaction networks partake in two cytotoxic effects: cell-cycle arrest with a link to RAB3C and RAF1; and lytic activity of arylsulfatases. The discovery of both mechanisms indicates that venomous mixtures may affect proliferating cells in a specific manner, highlighting the cocktails’ potential in the fine-tuning of anti-cancer therapeutics targeting cell cycle and protein homeostasis.

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Section: Discussionmentioning

confidence: 99%

Specific Antiproliferative Properties of Proteinaceous Toxin Secretions from the Marine Annelid Eulalia sp. onto Ovarian Cancer Cells

et al. 2021

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“…Estas proteínas del veneno tienen masas moleculares entre 30 y 35 kDa (23) y, según el perfil electroforético, estarían presentes en el veneno de B. roedingeri (figura 1). Se sabe que las serina proteasas del veneno afectan el sistema de coagulación al quebrar el fibrinógeno en sus fibrinopéptidos promoviendo la coagulación, por lo que se las conoce como "similares a trombina" (16,23), efecto propiciador de la coagulación que también fue observado en el veneno de B. roedingeri, así como en otros venenos de especies Bothrops que habitan en Perú (cuadro 1). La actividad hemorrágica de los venenos botrópicos varía de acuerdo con la región, la ontogenia y, específicamente, la especie (24).…”

Section: Discussionunclassified

Caracterización bioquímica del veneno de la serpiente Bothrops roedingeri Mertens, 1942, y sus actividades edematógena, hemorrágica y miotóxica

et al. 2020

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Introducción. El envenenamiento por mordedura de serpiente es considerado por la Organización Mundial de la Salud (OMS) una enfermedad tropical desatendida. Si bien los venenos de otras serpientes Bothrops se vienen estudiado ampliamente, poco se conoce del de Bothrops roedingeri.Objetivos. Caracterizar bioquímicamente el veneno total de la serpiente B. roedingeri y evaluar su actividad miotóxica, edematógena y hemorrágica.Materiales y métodos. Se hizo la caracterización enzimática del veneno de B. roedingeri determinando la actividad de la fosfolipasa A2 (PLA2) y de las enzimas proteolíticas, así como su acción fibrinogenolítica mediante electroforesis en gel de poliacrilamida con duodecilsulfato sódico (sodium dodecyl sulfate polyacrylamide gel electrophoresis, SDSPAGE), y la caracterización tóxica del veneno estableciendo la dosis hemorrágica mínima, la dosis edematógena mínima y el efecto miotóxico local y sistémico.Resultados. La actividad de las PLA2 del veneno total de B. roedingeri fue de 3,45 ± 0,11 nmoles/minuto, la proteolítica, de 0,145 ± 0,009 nmoles/minuto, en tanto que el índice de coagulación del fibrinógeno fue de 6,67 ± 1,33 segundos. Por otro lado, el veneno produjo una dosis hemorrágica mínima de 24,5 μg, una dosis edematógena mínima de 15,6 μg y un pronunciado efecto miotóxico local evidenciado por la elevación de los niveles plasmáticos de creatina cinasa después de la inoculación por vía intramuscular. No se registró miotoxicidad sistémica.Conclusiones. El veneno de B. roedingeri tiene efectos hemorrágicos, edematógenos y miotóxicos locales, así como una elevada actividad de la PLA2, que sería responsable de los efectos miotóxico y edematógeno. También presentó actividad proteolítica, la cual podría afectar la coagulación, dada su capacidad para degradar el fibrinógeno y producir hemorragia por acción de las metaloproteasas.

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“…Serine proteases are abundant in snake venoms and have been identified in venoms mainly from the subfamilies Crotalinae (genera Agkistrodon , Crotalus , Lachesis , Trimeresurus ), Viperinae ( Cerastes cerastes , Cerastes vipera , Bitis gabonica ), and Colubrinae ( Dipholidustypus ) [ 96 ]. SVSPs cause interference and imbalances of the hemostatic system by promoting specific proteolysis at various key points of the coagulation cascade [ 97 , 98 ]. Furthermore, SVSPs have been demonstrated to induce significant edema via the metabolism of arachidonic acid (AA), involving protease-activated receptors (PARs), protein kinase c (PKC), phospholipase C (PLC), and cyclooxygenase-2 (COX-2) receptors, and also induce a significant increase in malondialdehyde (MDA) levels [ 99 ].…”

Section: Neurotherapeutics and Preconditioning In Surgical Brain Injumentioning

confidence: 99%

Surgically-induced brain injury: where are we now?

et al. 2019

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Neurosurgical procedures cause inevitable brain damage from the multitude of surgical manipulations utilized. Incisions, retraction, thermal damage from electrocautery, and intraoperative hemorrhage cause immediate and long-term brain injuries that are directly linked to neurosurgical operations, and these types of injuries, collectively, have been termed surgical brain injury (SBI). For the past decade, a model developed to study the underlying brain pathologies resulting from SBI has provided insight on cellular mechanisms and potential therapeutic targets. This model, as seen in a rat, mouse, and rabbit, mimics a neurosurgical operation and causes commonly encountered post-operative complications such as brain edema, neuroinflammation, and hemorrhage. In this review, we elaborate on SBI and its clinical impact, the SBI animal models and their clinical relevance, the importance of applying therapeutics before neurosurgical procedures (i.e., preconditioning), and the new direction of applying venom-derived proteins to attenuate SBI.

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New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom

Cited by 19 publications

References 61 publications

Specific Antiproliferative Properties of Proteinaceous Toxin Secretions from the Marine Annelid Eulalia sp. onto Ovarian Cancer Cells

Specific Antiproliferative Properties of Proteinaceous Toxin Secretions from the Marine Annelid Eulalia sp. onto Ovarian Cancer Cells

Caracterización bioquímica del veneno de la serpiente Bothrops roedingeri Mertens, 1942, y sus actividades edematógena, hemorrágica y miotóxica

Surgically-induced brain injury: where are we now?

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