IQUIBICEN   23947
INSTITUTO DE QUIMICA BIOLOGICA DE LA FACULTAD DE CIENCIAS EXACTAS Y NATURALES
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Heme oxygenase 1 (HO-1) modulates aerobic glycolysis through regulation of lactate dehydrogenase (LDH) in prostate cancer cells
Autor/es:
CASCARDO F; LABANCA E; COTIGNOLA J; PÁEZ A; NAVONE N; VÁZQUEZ E; PÁEZ A; NAVONE N; VÁZQUEZ E; ANSELMINO N; GUERON G; ANSELMINO N; GUERON G; CASCARDO F; LABANCA E; COTIGNOLA J
Lugar:
Mar del Plata
Reunión:
Congreso; LXIV Reunión Anual de la Sociedad Argentina de Investigación Clínica (SAIC); 2019
Institución organizadora:
Sociedad Argentina de Investigación Clínica (SAIC)
Resumen:
Neoplastic proliferation requires tumour cells to reprogram their metabolic pathways in order to support the higher proliferation rate (known as the ?Warburg effect?). As a result, even under normal oxygen concentrations, transformed cells predominantly generate ATP through glycolysis followed by lactic acid fermentation, converting most incoming glucose to lactate rather than metabolizing it in the mitochondria through oxidative phosphorylation.We previously demonstrated that heme oxygenase 1 (HO-1), a cellular homeostatic regulator, has an antitumoral activity in prostate cancer (PCa) cells. In addition, after treatment with hemin, an inducer of HO-1 expression and activity, PC3 cells showed significantly lower glucose uptake, ATP production and oxygen consumption rate.In this context, we aimed to study whether HO-1 is involved in the regulation of aerobic glycolysis through modulation of lactate dehydrogenase (LDH) in PC3, C4-2B and MDA PCa 2b cell lines under HO-1 induction with hemin (80 µM, 24h). We found a significant reduction in LDHA expression by RTqPCR (P