Phosphatidylcholine mobility in liver microsomal membranes.

Purified phosphatidylcholine exchange protein from bovine liver was used to exchange rat liver microsomal phosphatidylcholine for egg phosphatidylcholine. It was found that at 25 and 37 degrees C rat liver microsomal phosphatidylcholine was completely and rapidly available for replacement by egg phosphatidylcholine. In contrast, phosphatidylcholine in vesicles prepared from total microsomal lipids could only be exchanged for about 60%. At 8 and 0 degrees C complex exchange kinetics were observed for phosphatidylcholine in rat liver microsomes. The exchange process had neither effect on the permeability of the microsomal membrane to mannose 6-phosphate, nor on the permeability of the phosphatidylcholine vesicles to neodymium (III) cations. Purified phospholipase A2 from Naja naja could hydrolyze some 55-60% of microsomal phosphatidylcholine at 0 degrees C, but 70-80% at 37 degrees C. Microsomal phosphatidylcholine, remaining after phospholipase treatment at 37 degrees C, could be exchanged for egg phosphatidylcholine at 37 degrees C, but at a slower rate than with intact microsomes. Microsomal phosphatidylcholine remaining after phospholipase treatment at 0 and 37 degrees C had a lower content of arachidonic acid than the original phosphatidylcholine. These results are discussed with respect to the localization and transmembrane movement of phosphatidylcholine in liver microsomes.