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Research Article Free access | 10.1172/JCI115799

Lipoproteins containing the truncated apolipoprotein, Apo B-89, are cleared from human plasma more rapidly than Apo B-100-containing lipoproteins in vivo.

K G Parhofer, P H Barrett, D M Bier, and G Schonfeld

Division of Atherosclerosis and Lipid Research, Washington University School of Medicine, St. Louis, Missouri 63110.

Find articles by Parhofer, K. in: JCI | PubMed | Google Scholar

Division of Atherosclerosis and Lipid Research, Washington University School of Medicine, St. Louis, Missouri 63110.

Find articles by Barrett, P. in: JCI | PubMed | Google Scholar

Division of Atherosclerosis and Lipid Research, Washington University School of Medicine, St. Louis, Missouri 63110.

Find articles by Bier, D. in: JCI | PubMed | Google Scholar

Division of Atherosclerosis and Lipid Research, Washington University School of Medicine, St. Louis, Missouri 63110.

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Published June 1, 1992 - More info

Published in Volume 89, Issue 6 on June 1, 1992
J Clin Invest. 1992;89(6):1931–1937. https://doi.org/10.1172/JCI115799.
© 1992 The American Society for Clinical Investigation
Published June 1, 1992 - Version history
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Abstract

We have reported previously on two truncations of apolipoprotein B (apo B-40 and apo B-89) in a kindred with hypobetalipoproteinemia. Premature stop codons were found to be responsible for both apo B-40 and apo B-89, but the physiologic mechanisms accounting for the reduced plasma concentrations of these proteins have not been determined in vivo. This study investigates the metabolism of apo B-89 in two subjects heterozygous for apo B-89/apo B-100 and in one apo B-40/apo B-89 compound heterozygote. In both heterozygotes total apo B concentration is approximately 30% of normal and apo B-89 is present in lower concentrations in plasma than apo B-100. After the administration of [1-13C]leucine as a primed constant infusion over 8 h, 13C enrichments of plasma leucine as well as enrichments of VLDL-, IDL-, and LDL-apo B-89 leucine and VLDL-, IDL-, and LDL-apo B-100 leucine were measured over 110 h. Enrichment values were subsequently converted to tracer/tracee ratios and a multicompartmental model was used to estimate metabolic parameters. In both apo B-89/apo B-100 heterozygotes apo B-89 and apo B-100 were produced at similar rates. Respective transport rates of apo B-89 and apo B-100 for subject 1 were 2.13 +/- 0.18 and 2.56 +/- 0.13 mg.kg-1.d-1, and for subject 2, 6.59 +/- 0.18 and 8.23 +/- 0.39 mg.kg-1.d-1. However, fractional catabolic rates of VLDL, IDL, and LDL particles containing apo B-89 were 1.4-3 times higher than the rates for corresponding apo B-100-containing particles. Metabolic parameters of apo B-89 in the apo B-40/apo B-89 compound heterozygote compared favorably with those established for apo B-89 in apo B-89/apo B-100 heterozygotes. Thus, the enhanced catabolism of VLDL, IDL, and LDL particles containing the truncated apolipoprotein is responsible for the relatively low levels of apo B-89 seen in these subjects.

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