Synthesis and parallel secretion of rat intestinal alkaline phosphatase and a surfactant-like particle protein.

Rat intestinal microvillous alkaline phosphatases are secreted bidirectionally from the enterocyte attached to a phospholipid-rich membrane (surfactant-like particle). To determine the intracellular pathways for newly synthesized alkaline phosphatases and for the extracellular enzyme-particle complex in the intestinal mucosa, pulse-chase experiments were performed. Synthesis of both isoforms of alkaline phosphatase in fasted rats peaked in the Golgi at 15-30 min and in the microvillous membrane at 60 min, without intermediate localization in the basolateral membranes. A second peak of incorporation was found at 15-30 min in scrapings obtained from the apical surface of the enterocytes. These results demonstrate a dominant direct Golgi-to-microvillous membrane transport for newly synthesized alkaline phosphatase. An additional precursor pool(s) appears responsible for the early appearance of enzyme in the lumen. Newly synthesized alkaline phosphatase isoforms and the 97-kDa protein of surfactant-like particles showed parallel patterns of appearance in enterocytes, luminal washings, and lamina propria after triacylglycerol feeding and were preferentially secreted into the lumen and lamina propria at times (5-7 h) when enterocyte content of these newly synthesized proteins had declined toward basal rates. Enhanced secretion of newly synthesized proteins for hours after fat feeding could explain the prolonged rise in serum and luminal washings of both the enzyme and the particle.