Deacylation-reacylation of phospholipids by rat embryos and their associated placentas. I. Placental acyltransferase.

Homogenates and subcellular fractions of rat chorioallantoic placentas obtained on the 14th day of gestation were assayed for acyl-CoA: lysophospholipid acyltransferase activities using (14C)-linoleic acid, ATP, and CoA, or (14C)-oleoyl-CoA as acyl donor and 1-acylglycerophosphorylcholine or 1-acylglycerophosphorylethanolamine as acyl acceptor. We found that: (1) the Lands' deacylation-reacylation cycle is present in the rat placenta, (2) the enzymes were concentrated in the microsomal fraction, and (3) the optimal conditions for in vitro assay of those enzyme activities were similar to those reported for adult tissues. Comparison of the acyl composition of phospholipids in maternal blood with those in placental homogenates revealed similarities which are consistent with a role for this cycle in vivo in placental uptake of phospholipids. That this cycle may function also in placental transformation of phospholipids in vivo, is suggested by differences between the acyl composition of phospholipids in placental homogenates and microsomal fractions.