Endoplasmic reticulum associated glucose-6-phosphatase activity is developmentally regulated and enriched in microsomes of endo/mesoderm in sea urchins.

Glucose-6-phosphatase (G-6-Pase) activity was analyzed during early embryogenesis of the sea urchinS. purpuratus. This activity is detected in very low levels in unfertilized eggs and early embryos but is present at high levels in preparations of endoplasmic reticulum (microsomes) from gastrula stage embryos. The approximately eight-fold increase in the relative activity of G-6-Pase associated with the ER occurs abruptly during a 12 h interval at gastrulation, and thereafter remains at a level comparable to that found in mammalian liver microsomes. The enzyme activity associated with the ER of gastrula stage embryos was completely eliminated from the microsomal pellet when cell lysates were first treated with non-ionic detergent. Analysis of germlayer tissues from late stage pluteus embryos revealed that G-6-Pase activity was more highly enriched in microsomes of endo/mesoderm tissues as compared to microsomes from ectoderm. The increase in ER associated G-6-Pase activity during embryonic development and its enriched activity in the ER of endo/mesoderm, as well as the observation that the signal recognition particle becomes associated with the ER at gastrulation (Le Blanc and Infante 1989), opens the question that this cellular organelle may be differentiating during embryogenesis in sea urchins.