Abstract
Snake venom rhodostomin, which belongs to the disintegrin family, binds to mammalian integrins with a high affinity through its Arg-Gly-Asp motif. Soluble rhodostomin served as an integrin inhibitor by competing with the integrin-ligand interaction, whereas the immobilized rhodostomin served as an integrin activator via cross-linking the integrin on cell surfaces. Based on these characteristics, rhodostomin was used either as an antithrombosis agent or, on the other hand, as an integrin agonist to trigger cell activation. Recently, rhodostomin was used to study integrin functions in many aspects, including cell signaling, integrin-mediated endocytosis, and the antithrombosis effects in infectious disease models. Results from these studies indicated that rhodostomin is a powerful tool to dissect the function of integrins.
Published Version
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