Ca +2-phosphatidylserine-dependent protein kinase C activfty in fetal, neonatal and adult rabbit lung and isolated lamellar bodies

Abstract

Evidence indicates that Ca +2-phosphatidylserine-dependent protein kinase C (PKC) is involved in regulation of surfactant secretion. This study was done to examine PKC activity in lung as surfactant synthesis and secretion is initiated, and at birth and to compare these enzyme levels with those in the adult lung. NZW rabbits were used. Fetal and adult lungs were fractionated into subcellular compartments including a lamellar body fraction, which represents intracellular surfactant. The time course for microsomal enzyme activity was compared between 24th gestational day and adult rabbit lung. The reactivity appeared similar in both fractions. PKC specific activity displayed a prominent peak between the 27th and 30th gestational days in total homogenate and lamellar bodies. Specific activity was also high in nuclear, mitochondrial and microsomal fractions the day prior to birth. Adult levels were similar or higher. Total PKC activity was high during late gestation but declined sharply the day prior to birth. A marked increase was present on the first postnatal day. In contrast lamellar bodies displayed a peak in activity between the 27th and 30th gestational days followed by a decline to adult levels. Delipidation of lamellar body fraction indicated that the high enzyme activity in this fraction on the 27th gestational day was not artifactual. The changes observed in PKC in fetal, neonatal and adult lung indicate this enzyme activity changes in lung during the period of onset of surfactant synthesis and secretion during late gestation and may be associated with lamellar bodies, in 27th gestational day fetal lung.