ROLE OF ACYL-COA SYNTHETASE 4 OFASTROCYTES IN CELL FUNCTION.

DATTILO MELINA; LOPEZ PAULA; CARUSO CARLA; LASAGA MERCEDES; MALOBERTI PAULA

Rosario

Congreso; L Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2014

The acyl-CoA synthetase 4 (Acsl4) an enzyme involved in the metabolism of arachidonic acid is involved in cell migration in tumor cells, in the axonal transport of synaptic vesicles and required for normal development of the nervous system in Drosophila. Moreover, this enzyme is mutated in families with non-syndromic mental retardation associated with the X chromosome. Previously we demonstrated the expression and regulation of Acsl4 by cAMP on neonatal rat astrocytes. In this study we use neonatal astrocytes and C6 cells, the rat astroglioma cell line, as model of normal and tumor cells respectively, to study the expression of Acsl4 and its role in cell migration. We demonstrate by Western blot and immunofluorescense that Acsl4 is overexpressed in C6 cells, compared with rat astrocytes. Treatment with triacsine C, an inhibitor of Acsl4 activity, produced significant inhibition of cell migration in both cell models analyzed by wound healing assay. These results were confirmed in C6 cells by knocking down Acsl4 expression by siRNA treatment. The knock down of Acsl4 also reduced the levels of phospho Akt, phospho p70 S6 kinase, and phospho S6 ribosomal protein, one of the main signals in mRNA translation. These data suggest that Acsl4 is an important regulator of cell function in glia cells.