Abstract
Alternagin-C (ALT-C) is a disintegrin-like protein isolated from Rhinocerophis alternatus snake venom, which induces endothelial cell proliferation and angiogenesis. The aim of this study was to evaluate the systemic effects of a single dose of alternagin-C (0.5 mg·kg−1, via intra-arterial) on oxidative stress biomarkers, histological alterations, vascular endothelial growth factor (VEGF) production, and the degree of vascularization in the liver of the freshwater fish traíra, Hoplias malabaricus, seven days after the initiation of therapy. ALT-C treatment increased VEGF levels and hepatic angiogenesis. ALT-C also enhanced hepatic antioxidant enzymes activities such as superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase, decreasing the basal oxidative damage to lipids and proteins in the fish liver. These results indicate that ALT-C improved hepatic tissue and may play a crucial role in tissue regeneration mechanisms.
Highlights
Snake venoms contain a complex pool of proteins, organic compounds with a low molecular mass, and inorganic compounds [1]
Disintegrins of snake venoms are mostly derived from proteolytically processed precursor forms having a metalloprotease (SVMP) domain [3]
ALT-C competitively interacts with the α2 β1 integrin, the major collagen receptor, triggering intracellular signaling typical of integrin-activated pathways and inducing the expression of several growth factors, mainly vascular endothelial growth factor (VEGF), one of the most effective angiogenic peptides [11]
Summary
Snake venoms contain a complex pool of proteins (more than 90% of the dry weight), organic compounds with a low molecular mass, and inorganic compounds [1]. Among these compounds are acetylcholinesterases, ADPases, phospholipases, hialuronidases, and hemostasis active compounds such as metalloproteases, named the snake venom metalloproteases (SVMPs), and serinoproteases [2]. Disintegrins of snake venoms are mostly derived from proteolytically processed precursor forms having a metalloprotease (SVMP) domain [3]. Alternagin-C (ALT-C) is an ECD (Glu-Cys-Asp sequence)-containing disintegrin-like/cysteine-rich domain released from metalloprotease alternagin isolated from the crude venom of the snake Rhinocerophis alternatus, popularly known in South America as urutu. Disintegrin-like proteins trigger integrin-mediated intracellular signal transduction events that modify gene expression and cell responses and interfere with cell-cell and cell-matrix interactions in a bi-directional manner across cell membranes [4,5].
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
