Imaizumi Katsumi

Absorption and transport of base moieties of phosphatidylcholine and phosphatidylethanolamine in rats

The absorption and transport of the base moieties of phosphatidylethanolamine (PE) and phosphatidylcholine (PC) which were fed to rats were compared. The major absorption site of ethanolamine-labeled PE was proximal jejunum while choline-labeled PC was absorbed almost equally throughout the jejunum. Lysophospholipids, glycerophosphoryl bases and constituent bases were the main digested products in intestinal content. This shows that base-labeled phospholipids were hydrolyzed to water-soluble products as well as lysophospholipids before absorption. The radioactivities from both phospholipids existed mainly in their parent phospholipids and water-soluble products in the intestinal mucosa. The amounts of lymphatic transport of the radioactivities from choline-labeled PC and ethanolamine-labeled PE were 17% and 8%, respectively, at 8 h after administration. The liver in lymph-cannulated rats contained 23% and 48% radioactivity from PC and PE, respectively, suggesting that base moieties of phospholipids, especially PE, were transported mainly via a non-lymphatic route, probably the portal vein, to the liver, as water-soluble products. The radioactivity from both base-labeled phospholipids in the liver was distributed in the parent phospholipids and water-soluble fractions. Ethanolamine-labeled PE was also incorporated into PC in the liver. These results indicate that intestinal absorption and transport of the base moiety of dietary PC and PE are similar; however, their intestinal absorption site and the extent of their separation during transport between the lymphatic and portal systems differ markedly.

Characterization of serum apolipoprotein patterns in rats during suckling and post-weaning periods.

Changes of serum apolipoprotein patterns during the suckling and post-weaning periods were studied in rats. Concentrations of apolipoprotein A-IV and the high-molecular-weight form of apolipoprotein B were markedly high during the early suckling periods and decreased at weaning. Secretion of apolipoprotein A-IV into the mesenteric lymph in 2-week-old rats was as high as that in adult rats into which the high-fat diet was infused constantly. Apolipoprotein A-IV was found both in high-density lipoprotein and lipoprotein-free fractions, and the relative distribution in the latter decreased developmentally. The concentration of apolipoprotein A-I was low for 1 week after birth, after which it increased to the adult level. The apolipoprotein E level during the suckling and post-weaning periods was similar to or above that of adult rats. The newly formed apolipoprotein B in very-low-density lipoproteins secreted by the isolated liver and by the primary culture hepatocytes of suckling rats was predominantly a high-molecular-weight form. Overnight fasting and early weaning caused a remarkable alteration of the serum apolipoprotein profile. It therefore appears that frequent ingestion of dams milk as well as ontogenic development are relevant to the serum apolipoprotein patterns characteristic for suckling rats.

Secretion of apolipoproteins in the suckling rat. Absence of low-molecular-weight apolipoprotein B of hepatic origin

Synthesis of apolipoprotein B in the intestine and liver in suckling rats whose duodena had been infused with [3H]lysine was estimated by measuring the radioactivity in the mesenteric lymph and blood serum. Apolipoprotein B synthesized in the suckling rat intestine was an exclusively low-molecular-weight form. In the serum d < 1.21 g/ml fraction obtained from the lymph-diverted rats, apolipoprotein B of high molecular weight was only labeled with [3H]lysine in suckling rats, whereas both forms of apolipoprotein B were labeled in the adult rats. These results suggest developmental changes in hepatic apolipoprotein B synthesis and secretion.