Integrins, cancer and snake toxins (mini-review)

• Published in: Journal of Venomous Animals and Toxins including Tropical Diseases
• Main Author: G. Rádis-Baptista
• Format: Article in Journal/Newspaper
• Language: English
• Published: SciELO 2005
• Subjects: integrin; angiogenesis; cancer; apoptosis; snake toxin; snake venom C-type lectin; metalloprotease; disintegrin; Arctic medicine. Tropical medicine; RC955-962; Toxicology. Poisons; RA1190-1270; Zoology; QL1-991; Arctic
• Online Access: https://doi.org/10.1590/S1678-91992005000300002; https://doaj.org/article/db9f93f43503414bbe3dbbd7ee467d25

Integrins encompass a family of transmembrane heterodimeric proteins of adhesion that maintain cells attached to other cells and to the extracellular matrix (ECM). Integrins work as bi-directional mechanotransducers, conveying mechanical signal from outside to inside the cell through a cascade of phosphorylation signals. On the other hand, the signal from inside to outside controls the strength and affinity of integrin adhesion. As proteins of focal contact, integrins are involved in diverse cell functions, such as cell activation, migration, growth, and survival. In the development of neoplastic disease and metastatic tumor, integrins can influence cancer invasiveness and progression, as well as mediate the formation of new blood vessels (angiogenesis). Diverse snake venom toxins have the ability to interact with multiple integrins, what results in inhibition of cell attachment, inhibition of angiogenesis, and induction of apoptotic death of tumor and vascular endothelial cells. The aim of this review is to present data about snake venom toxins that bind to integrins and evoke antiangiogenesis and antitumoral effects.