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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Peptides derived from plasma proteins released by bothropasin, a metalloprotease present in the Bothrops jararaca venom

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Fernandes Silva, Cristiane Castilho ; Menezes, Milene Cristina ; Palomino, Miryam ; Oliveira, Ana Karina ; Iwai, Leo Kei ; Faria, Marcella ; Portaro, Fernanda Vieira
Total Authors: 7
Document type: Journal article
Source: Toxicon; v. 137, p. 65-72, OCT 2017.
Web of Science Citations: 1

Viperid snake venoms contain proteases that affect hemostasis by degrading important proteins such as those that participate in the coagulation cascade. The Bothrops jararaca venom presents as its main components metallo and serine proteases, which comprise around 65% of the venom composition. Bothropasin is a hemorrhagic metalloprotease from the B. jararaca venom which causes disruption of the basement membrane of the vascular endothelium, resulting in bleeding. Although the bothropasin ability to degrade plasmatic and extracellular matrix proteins in vitro has been described, the primary sequence of the released peptides is unknown. This research study presents the peptide identification from both fibrinogen and fibronectin, generated by bothropasin proteolytic activity. Among the fibrinogen derived peptides identified by mass spectrometry, analogous of endogenous products like the fibrinopeptides A and B were found, as well as other sequences described in the literature with vasoactive or antiangiogenic properties. A series of peptides derived from fibronectin by the action of bothropasin were described, and for most of them no biological activity has been described. However, exceptionally a peptide that is known as a bond site for B cells was found. This study indicates that, beyond to the degradation of human proteins, bothropasin can generate bioactive peptides, which may participate in the envenoming process by Bothrops snakes. Also important, the knowledge of the formed peptides, based on the cleavage sites of the hydrolyzed proteins, provided the opportunity to study the primary specificity of bothropasin. (C) 2017 Elsevier Ltd. All rights reserved. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 14/02788-7 - Characterization of polypeptide modulators of angiogenesis derived from the degradation of kininogen and fibrinogen by Bothropasin
Grantee:Cristiane Castilho Fernandes da Silva
Support type: Scholarships in Brazil - Master
FAPESP's process: 15/15364-3 - Toxic potential analysis of proteases and peptides present in scorpion Tityus serrulatus venom and the blockage capacity of commercial antivenoms: enhancing the knowledge of venom and its mechanism of action
Grantee:Fernanda Calheta Vieira Portaro
Support type: Regular Research Grants