Interaction between C16 peptide, derived from laminin-111, and beta1 integrin in breast cells. Related mechanisms and functional consequences

Abstract

Malignant neoplasm of the female breast is among the most frequent in the Brazilian population, accounting for 28.1% of the tumors. In this context, the literature clearly shows the important role that the tumor microenvironment assumes during cancer progression and metastasis. Such microenvironment is composed of different cell types enmeshed into the extracellular matrix (ECM). Laminin-111, a glycoprotein present in the ECM, possess peptide sequences with relevant biological activities. Among them, the C16 peptide has a major role regulating cancer biology. Studies conducted in our laboratory have shown that this peptide influences migration, invasion, protease secretion, and invadopodia formation. In addition, C16-induced activity is reduced in tumor cells with the expression of the beta1 integrin depleted by RNAi. This prompted us to study in greater detail the interaction between C16 and beta 1 integrin. Therefore, his project will address mechanisms involved in the interaction between the C16 peptide and the beta1 integrin in breast cencer cells. We will also analyze signaling pathways activated by such interaction, as well as the inherent functional effects. (AU)