Lung phosphatidate phosphatase: activity during altered physiologic states.

Phosphatidic acid phosphatase (PAPase) which catalyzes the conversion of phosphatidic acid to 1,2-diacyl-sn-glycerol was studied in fetal, neonatal, and adult rat lung microsomal fractions from whole lung under normal and altered physiological states. The maximal activity was obtained at pH 7.0 with 1.0 mM phosphatidic acid as the substrate. Twenty-one-day-old fetal rat lung averaged 20.3 +/- 0.6 SE nmol/min/mg microsomal protein compared to 9.9 +/- l.0 nmol/min/mg in liver. Following birth there was a dramatic 53% increase in the PAPase activity. Twenty-one-day-old fetal rat lungs from diabetic mothers (streptozotocin-induced) and from mothers fasted the last four days of gestation did not show altered PAPase activity. Premature breathing for 3-6 hr on day 21 of gestation also did not affect the PAPase activity. These data demonstrate that the microsomal PAPase activity (l) increases dramatically only after birth (2) is not responsive to altered physiologic state (maternal diabetes, maternal fasting, and premature breathing) and (3) may not be an important regulatory enzyme in lung surfactant phospholipid production.

Base-exchange reactions of the phospholipids in cardiac membranes.

Canine cardiac microsomes were shown to incorporate the nitrogenous bases, serine, ethanolamine, and choline, into their respective phospholipids by the energy-independent, Ca2+-stimulated base-exchange reactions. The optimal Ca2+ concentration was 2.5 mM. Metal ions other than Ca2+ either inhibited or had no effect on the activities. La3+ and Mn2+ were both potent inhibitors. The pH optimum for the reactions at 2.5 mM Ca2+ was approx. 7.8 and depended upon Ca2+ concentration. Apparent Km values at 2.5 mM Ca2+ were 0.06 mM for L-serine, 0.13 mM for ethanolamine and 0.49 mM for choline. The kinetic and metal ion inhibition studies suggest that the choline-exchange reaction is a separate process from the serine and ethanolamine reactions. The ATP-stimulated Ca2+ binding system of the cardiac membranes was not related to the base-exchange reactions; however, the energy-independent Ca2+ binding to the membranes appears to be related to the exchange reactions.