Use of immunoelectron microscopy and intestinal models to explore the elaboration of apolipoproteins required for intraenterocyte lipid transport.

The intestine is the organ that contributes the majority of circulating alimentary lipoproteins. Intestinal epithelial cells have the unique ability to elaborate chylomicrons, the largest triglyceride-rich lipoproteins and the main vehicle for the transport of dietary lipids. The final intracellular assembly and exocytosis of chylomicrons require enterocyte-derived apolipoproteins (apo). As research on lipoprotein metabolism evolved, it has become increasingly evident that apo B is a crucial protein for the normal packaging of triglyceride-rich lipoproteins. Immunocytochemical techniques have successfully been used to demonstrate the presence of two types of apo B, the B-100 and the B-48, in different subcellular compartments of the human enterocyte. Confirmation was obtained by biochemically analyzing human lymph and intestine from pediatric patients. In addition, the immunoelectron microscopic approach revealed the location of apo A-I in the rough endoplasmic reticulum (ER) and predominantly in the Golgi apparatus and the basolateral membrane, which confirms the rapid transport of apo A-I documented by other studies. Proven utility and experimental conditions were defined to demonstrate the ability of Caco-2 cells, a colon carcinoma cell line, to esterify lipids, synthesize apo, and assemble lipoproteins. Thus, immunocytochemical and biochemical techniques can be combined with in vivo and in vitro intestinal models for the study of the intestinal lipid transport.