Systemic response induced by Scorpaena plumieri fish venom initiates acute lung injury in mice

Boletini-Santos, Douglas; Komegae, Evilin Naname; Figueiredo, Suely G.; Haddad, Vidal; Lopes-Ferreira, Mônica; Lima, Carla

doi:10.1016/j.toxicon.2007.11.011

Cited by 22 publications

(13 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Alveolar macrophages (AM) and neutrophils act as a source of matrix metalloproteinases that together play a key role in the cascade of events leading to lung injury. These findings also confirm a central role for macrophage and neutrophils in the pathogenesis of venom-induced lung injury and also the importance of AMs in the resolution of this SpV-triggered process [21]. …”

Section: Biological Activities Of S Plumieri Venom Extract (Spv)supporting

confidence: 75%

A review on the Scorpaena plumieri fish venom and its bioactive compounds

Campos

Menezes

Malacarne

et al. 2016

J Venom Anim Toxins Incl Trop Dis

Self Cite

View full text Add to dashboard Cite

The most poisonous fish species found along the Brazilian coast is the spotted scorpionfish Scorpaena plumieri. Though hardly ever life-threatening to humans, envenomation by S. plumieri can be quite hazardous, provoking extreme pain and imposing significant socioeconomic costs, as the victims may require days to weeks to recover from their injuries. In this review we will walk the reader through the biological features that distinguish this species as well as the current epidemiological knowledge related to the envenomation and its consequences. But above all, we will discuss the challenges involved in the biochemical characterization of the S. plumieri venom and its compounds, focusing then on the successful isolation and pharmacological analysis of some of the bioactive molecules responsible for the effects observed upon envenomation as well as on experimental models. Despite the achievement of considerable progress, much remains to be done, particularly in relation to the non-proteinaceous components of the venom. Therefore, further studies are necessary in order to provide a more complete picture of the venom’s chemical composition and physiological effects. Given that fish venoms remain considerably less studied when compared to terrestrial venoms, the exploration of their full potential opens a myriad of possibilities for the development of new drug leads and tools for elucidating the complex physiological processes.

show abstract

Section: Biological Activities Of S Plumieri Venom Extract (Spv)supporting

confidence: 75%

A review on the Scorpaena plumieri fish venom and its bioactive compounds

Campos

Menezes

Malacarne

et al. 2016

J Venom Anim Toxins Incl Trop Dis

Self Cite

View full text Add to dashboard Cite

show abstract

“…Neutrophils infiltrate lungs and migrate into the airways lead to the release of oxygen free radicals and enzymes (proteases and myeloperoxidase) exacerbating damage to endothelial cells and to subendothelial matrix proteins, and inducing tissue injury [39][40][41]. The activation of platelet-activating factor receptors, production of chemokines, and adhesion molecules (ICAM-1) were responsible of neutrophil recruitment in lungs after scorpion envenomation [40][41][42].…”

Section: Discussionmentioning

confidence: 99%

Lung Immunoreactivity and Airway Inflammation: Their Assessment After Scorpion Envenomation

et al. 2011

View full text Add to dashboard Cite

Release and activation of pro-inflammatory mediators are among the most important induced factors that are involved in the scorpion envenomation pathogenesis. Inflammatory response and lung reactivity were studied in mice following subcutaneous injection with Androctonus australis hector (Aah) venom. Venom immunodetection in lungs and sequestered cell population in the airways were determined. Cytokines, cellular peroxidase activities (eosinophil peroxidase, myeloperoxydase), and IgE antibodies were also assessed. Immunohistochemical study revealed a positive detection of the Aah venom in the alveolar wall, venule lumens, and inside inflammatory cells. Severe lung edema associated with rapid inflammatory response was observed after animal envenomation. Lung neutrophilia and eosinophilia were accompanied with IL-4, IL-5 release, and IgE synthesis. In conclusion, high cytokine levels, recruitment of inflammatory cells (eosinophils and neutrophils), and increased IgE concentration may contribute to the exacerbation and maintenance of the induced inflammatory response in lungs by scorpion venom. These results lead to the better understanding of this induced pathogenesis and could help the physicians to take care of envenomed patients.

show abstract

“…Additionally, local edema and erythema may arise as consequence of envenoming. The systemic symptoms of cardiotoxic and vasorelaxant effects are more severe, resulting in a drastic drop of blood pressure (22)(23)(24)(25). Moreover, the observed increase in the epithelial permeability of the bronchi and alveoli, similar to the observed erythema and hemorrhages, indicate a loss of cell-matrix interactions (22,23).…”

Section: Discussionmentioning

confidence: 99%

“…These symptoms indicate the presence of toxins interfering with integrin-mediated cell-matrix interactions. Some of these symptoms have been observed after envenomation by the scorpionfish (Scorpaena plumieri) (22)(23)(24)(25) and have encouraged us to analyze this fish venom for potential integrin inhibitors.…”

mentioning

confidence: 99%

Plumieribetin, a Fish Lectin Homologous to Mannose-binding B-type Lectins, Inhibits the Collagen-binding α1β1 Integrin

Evangelista

Andrich

Rezende

et al. 2009

Journal of Biological Chemistry

View full text Add to dashboard Cite

Recently, a few fish proteins have been described with a high homology to B-type lectins of monocotyledonous plants. Because of their mannose binding activity, they have been ascribed a role in innate immunity. By screening various fish venoms for their integrin inhibitory activity, we isolated a homologous protein from the fin stings and skin mucus of the scorpionfish (Scorpaena plumieri). This protein inhibits ␣1␤1 integrin binding to basement membrane collagen IV. By protein chemical and spectroscopic means, we demonstrated that this fish protein, called plumieribetin, is a homotetramer and contains a high content of anti-parallel ␤ strands, similar to the mannose-binding monocot B-lectins. It lacks both N-linked glycoconjugates and common O-glycan motifs. Despite its B-lectin-like structure, plumieribetin binds to ␣1␤1 integrin irrespective of N-glycosylation, suggesting a direct protein-protein interaction. This interaction is independent of divalent cations. On the cellular level, plumieribetin failed to completely detach hepatocarcinoma HepG2 cells and primary arterial smooth muscle cells from the collagen IV fragment CB3. However, plumieribetin weakened the cell-collagen contacts, reduced cell spreading, and altered the actin cytoskeleton, after the compensating ␣2␤1 integrin was blocked. The integrin inhibiting effect of plumieribetin adds a new function to the B-lectin family, which is known for pathogen defense.

show abstract

Systemic response induced by Scorpaena plumieri fish venom initiates acute lung injury in mice

Cited by 22 publications

References 34 publications

A review on the Scorpaena plumieri fish venom and its bioactive compounds

A review on the Scorpaena plumieri fish venom and its bioactive compounds

Lung Immunoreactivity and Airway Inflammation: Their Assessment After Scorpion Envenomation

Plumieribetin, a Fish Lectin Homologous to Mannose-binding B-type Lectins, Inhibits the Collagen-binding α1β1 Integrin

Contact Info

Product

Resources

About