INVESTIGADORES
DATTILO Melina Andrea
congresos y reuniones científicas
Título:
Acyl-CoA Synthtase 4 levels are dependent on proteasome activity and modulate mitochondrial metabolism regulatory proteins expression in breast cancer cells
Autor/es:
BENZO Y. ; DATTILO M.; HELFENBERGER K.; HERRERA L.; PODEROSO C.; MALOBERTI P.
Lugar:
Buenos Aires
Reunión:
Congreso; Reunión Conjunta De Sociedades de Biociencias - LXII reunión SAIC 2017; 2017
Resumen:
ACSL enzymes catalyze the production of acyl-CoA from long chain fatty acids. ACSL4 is an enzyme with a strong preference for arachidonic acid (AA). Several functions of ACSL4 in different physiological and pathological processes have been reported including an important role in breast, liver and colon carcinogenesis. Our lab has already shown that ACSL4 expression correlates with tumor aggressiveness in breast cancer cell lines and that this enzyme plays a functional role in human breast cancer cells. Also, it is known that the activity of this enzyme is needed for the generation and metabolization of intramitochondrial AA. However, the cellular mechanisms that regulate ACSL4 expression as well as the role of ACSL4 in mitochondrial metabolism in tumor cells remain unknown. Computational data showed that ACSL4 is a possible candidate for modulating mitochondrial master regulatory genes. Then, our goal is to study stability of ACSL4 by post translational mechanisms and to study the role of ACSL4 in the regulation of mitochondrial function.