Recombinant RGD-disintegrin DisBa-01 blocks integrin α_vβ₃ and impairs VEGF signaling in endothelial cells.

ABSTRACT:

Background

Integrins mediate cell adhesion, migration, and survival by connecting the intracellular machinery with the surrounding extracellular matrix. Previous studies demonstrated the interaction between α_vβ₃ integrin and VEGF type 2 receptor (VEGFR2) in VEGF-induced angiogenesis. DisBa-01, a recombinant His-tag fusion, RGD-disintegrin from Bothrops alternatus snake venom, binds to α_vβ₃ integrin with nanomolar affinity blocking cell adhesion to the extracellular matrix. Here we present in vitro evidence of a direct interference of DisBa-01 with α_vβ₃/VEGFR2 cross-talk and its downstream pathways.

Methods

Human umbilical vein (HUVECs) were cultured in plates coated with fibronectin (FN) or vitronectin (VN) an

SUBMITTER: Danilucci TM 

PROVIDER: S-EPMC6425665 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature