The antitumoral role of heme oxygenase-1 in breast cancer.

GANDINI, N.A.; ALONSO, E.N.; FERMENTO, M. E.; COLÓ, G.P.; MASCARÓ, M.; FERRONATO, M.J.; GUEVARA, J.A.; ABBA, M.C.; ARÉVALO, J.; GRIOLI, S.M.; IBARRA, A.; BARRERA LAMAS, N.; CURINO, A.C.; FACCHINETTI, M.M.

Mar del Plata

Otro; LXIII Reunión Científica Anual de la Sociedad Argentina de Investigación Clínica (SAIC); 2018

Sociedad Argentina de Investigación Clínica

It has been reported that HO-1 can translocate to multiple subcellular compartments and can have non-enzymatic signaling roles. Thus, in the nucleus the protein may act as a transcriptional co-regulator protein and may bind and modulate other important proteins. HO-1 is an enzyme involved in cellular responses to oxidative stress and has also been shown to regulate processes related to cancer progression. In this regard, HO-1 has been shown to display a dual effect with either antitumor or protumor activity, being this also true for breast cancer (BC). In this work we intended to address this discrepancy regarding the role of HO-1 in BC. HO-1 was detected in human BC tissues, and its protein levels correlated with reduced tumor size (p=0.046) and longer overall survival time of patients (p=0.004). Contrariwise, nuclear localization of HO-1 correlated with higher tumor grade (p=0.05). However, nuclear HO-1 was not significantly associated to patient overall survival time (p = 0.13). In vivo experiments showed that both pharmacological activation and genetic overexpression of HO-1 reduced the tumor burden in two different animal models of BC. Furthermore, the activation of HO-1 in several BC cell lines reduced cellular viability by inducing apoptosis (p