Light stimulation activates retina ganglion cell lysophosphatidic acid acyl trasnferase and phosphoatidic acid phosphatase by a c-Fos-dependent mechanism.

DE ARRIBA ZERPA GA; GUIDO ME; BUSSOLINO DF; PASQUARE SJ; CASTAGNET PI; GIUSTO NM; CAPUTTO BL

WILEY-BLACKWELL PUBLISHING, INC

Lugar: Londres; Año: 1999 vol. 1999 p. 1228 - 1228

p>We previously reported that the biosynthesis of phospholipids in the avian retina is altered by light stimulation, increasing significantly in ganglion cells in light and in photoreceptor cells in dark. In the present work, we have determined that light significantly increases the incorporation of [3H]glycerol into retina ganglion cell glycerophospholipids in vivo by a Fos-dependent mechanism because an oligonucleotide antisense to c-fos mRNA substantially blocked the light-dark differences. We also studied in vitro the enzyme activities of phosphatidate phosphohydrolase (PAPase), lysophosphatidate acyl transferase (AT II), and phosphatidylserine synthase from retinas of chickens exposed to light or dark. Higher PAPase I and AT II activities were found in incubations of retinal ganglion cells from animals exposed to light; no increase was observed in preparations obtained from light-exposed animals treated with the c-fos antisense oligonucleotide. No light-dark differences were foun