C-terminal-truncated and full length hemeoxygenase-1

MASCARO M; ALONSO E; GANDINI NA; FERRONATO MJ; GUEVARA JA; ALONSO E; COLO GP; PICHEL P; RECIO S; CURINO AC; FACCHINETTI MM

Congreso; LXIV Reunión Anual de la Sociedad Argentina de Investigación Clínica (SAIC); 2019

We previously reported that heme oxygenase-1 (HO-1) protein is up-regulated in human HNSCC samples and that it is localized in the cytoplasmic and nuclear compartments. We also reported that high expression of HO-1 mRNA is associated with worst survival and that pharmacological activation of HO-1 by hemin increases viability of HN13 cells. However, how HO-1 isoforms affects HNSCC remains elusive. In this study, we aim to elucidate if C-terminal truncated HO-1 impacts on head and neck cancer cells behavior. We established the wild type (FL-HO1) and the C-terminal truncated HO-1- (t-HO1) overexpressing HN13 cells. We evaluated cell viability by crystal violet method, cell cycle progression by propidium iodide staining and flow cytometry, and cell migration by wound healing assay. In addition to our previous results using hemin, we found that 80uM hemin increased cell number in S- (p