ABSTRACT
Previous studies showed that chick kidney is a site of synthesis of apolipoprotein (apo) B(B-100) and A-I. Aims of the present study were: a) to compare apoB and apoA-I production in chick kidney and liver; b) to investigate whether kidney apolipoproteins were secreted as constituents of lipoproteins; and c) to define the cellular sites of renal apolipoprotein synthesis. Kidney and liver slices taken from the same animals were incubated with 35S-labeled amino acids and radioactive apoB and apoA-I were immunoprecipitated from cell homogenate and incubation medium. The percentage of total protein radioactivity incorporated into cell plus medium apoB and apoA-I was 0.23+/-0.08 and 0.19+/-0.11 in kidney and 0.38+/-0.05 and 0.38+/-0.07 in liver, respectively (P < 0.05 kidney vs. liver). 35S-labeled medium lipoproteins were separated by density gradient ultracentrifugation and three major classes corresponding to VLDL + IDL, LDL, and HDL were identified. Most of the apoB secreted by the liver was found in VLDL, IDL, and LDL whereas kidney apoB was found in VLDL, LDL and "light" HDL (d 1.070-1.130 g/ml). In both hepatic and renal lipoproteins apoA-I was found not only in HDL but also in the other lipoproteins. Immunohistochemical analysis of kidney sections showed that apoB and apoA-I were present almost exclusively in the epithelial cells of proximal and distal convoluted tubules. Thus apoB and apoA-I synthesized by the epithelial cells of the proximal and distal convoluted tubules of chick kidneys are secreted as constituents of lipoprotein particles floating within the density range of plasma lipoproteins. These observations suggest that in the chick, the kidneys may contribute to the plasma lipoprotein pool.
