Recombinant disintegrin targets alpha(v) beta(3) integrin and leads to mediator production
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Data
2014-01-01
Autores
Ribeiro, Livia C. A. [UNESP]
Massimino, Livia C. [UNESP]
Durante, Araceli C.
Tansini, Aline [UNESP]
Urbaczek, Ana C. [UNESP]
Selistre-de-Araujo, Heloisa S.
Carlos, Iracilda Zeppone [UNESP]
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Editor
Landes Bioscience
Resumo
Integrin alpha v beta 3 is most likely the foremost modulator of angiogenesis among all known integrins. Recombinant disintegrin DisBa-01, originally obtained from snake venom glands, binds to alpha v beta 3, thereby significantly inhibiting adhesion and generating in vivo anti-metastatic ability. However, its function in mediator production is not clear. Here, we observed that the mediators VEGF-A, IL-8, and TGF-beta are not produced by human umbilical vein endothelial cells (HUVEC cell line) or monocyte/macrophage cells (SC cell line) when cells adhered to vitronectin. However, when exposed to DisBa-01, HUVECs produced higher levels of TGF-beta, and SC cells produced higher levels of VEGF-A. Nonetheless, HUVECs also showed an enhancement of apoptosis after losing adherence when exposed to disintegrin, which is a characteristic of anoikis. We propose that disintegrin DisBa-01 could be used to modulate integrin alpha v beta 3 functions.
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Palavras-chave
TGF, IL-8, endothelial cell, DisBa, macrophage, integrin alpha v beta 3, cancer, VEGF, HUVEC
Como citar
Cell Adhesion & Migration. Austin: Landes Bioscience, v. 8, n. 1, p. 60-65, 2014.