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A C-type lectin from Bothrops jararacussu venom reprograms endothelial cell biology.

Federico G BaudouNancy L CharóMarco A ScheideggerJuan C StupirskiJuan M Pérez SáezMaría F TroncosoMora MassaroAdolfo R de RoodtMauricio C De MarziMirta SchattnerGabriel A Rabinovich
Published in: Angiogenesis (2024)
Snake venoms are intricate mixtures of enzymes and bioactive factors that induce a range of detrimental effects in afflicted hosts. Certain Viperids, including Bothrops jararacussu, harbor C-type lectins (CTLs) known for their modulation of a variety of host cellular responses. In this study, we isolated and purified BjcuL, a CTL from B. jararacussu venom and investigated its impact on endothelial cell behavior, contrasting it with human galectin-1 (Gal-1), a prototype member of the galectin family with shared β-galactoside-binding activity. We found that BjcuL binds to human dermal microvascular endothelial cells (HMECs) in a concentration- and carbohydrate-dependent fashion and reprograms the function of these cells, favoring a pro-inflammatory and pro-coagulant endothelial phenotype. In light of the quest for universal antagonists capable of mitigating the harmful consequences of snake venoms, BjcuL emerges as a promising target to be blocked in order to regulate pathological endothelial cell responses.
Keyphrases
  • endothelial cells
  • high glucose
  • vascular endothelial growth factor
  • induced apoptosis
  • ionic liquid
  • oxidative stress
  • anti inflammatory
  • endoplasmic reticulum stress
  • atomic force microscopy