SECRETORY LEUKOCYTE PROTEASE INHIBITOR (SLPI) EXPRESSION DOWNREGULATES E-CADHERIN, INDUCES -CATENIN RE-LOCALIZATION AND TRIGGERS APOPTOSIS-RELATED EVENTS IN BREAST CANCER CELLS

ROSSO, M; LAPYCKYJ, L.; AMIANO, N.; BESSO, MJ; SANCHEZ, M.; CHULUYAN, E.; VAZQUEZ-LEVIN, MH

BIOLOGY OF THE CELL

PORTLAND PRESS LTD

Lugar: Londres; Año: 2014

0248-4900

Background Information: Epithelial cadherin (E-cadherin) is involved in cell-cell adhesion through its extracellular domain, while the intracellular domain interacts with adaptor proteins, i.e. β-catenin, links E-cadherin to the actin cytoskeleton and participates in signal transduction events. E-cadherin protects mammary epithelial cells from apoptosis and its loss during tumor progression has been documented. Secretory Leukocyte Protease Inhibitor (SLPI) has anti- and pro-tumorigenic activities but its role in breast cancer has not been fully elucidated. Notwithstanding its relevance, how SLPI affects E-cadherin in breast cancer is still unknown. This study evaluated the effect of SLPI upon E-cadherin expression in murine (F3II) and human (MCF-7) breast tumor cells either treated with exogenous recombinant human SLPI (rhSLPI) or stably transfected with a plasmid encoding its sequence. In addition, expression of β-catenin, Neural (N-) and Placental (P-) cadherin and apoptosis-related markers was evaluated. Results: Addition of rhSLPI to murine breast cancer cells (F3II) caused a decrease (P