PMID: 9194751Jun 1, 1997Paper

Organ loci of catabolism of short truncations of apoB

Arteriosclerosis, Thrombosis, and Vascular Biology
X F ZhuGustav Schonfeld

Abstract

Truncations of apolipoprotein (apo) B shorter than 3200 amino acids (3200/4536 = apoB-70) do not possess the LDL receptor-recognition domain and are not recognized by altered cells with normally functioning LDL receptors. To ascertain which organs remove such truncated apoB-containing particles, we isolated apoB-31-, apoB-38.9-, and apoB-43.7-containing particles from plasmas of familial hypobetalipoproteinemia heterozygous humans by a combination of sequential ultracentrifugation and preparative electrophoresis. Particles with labeled 125I- or 131I-dilactitol tyramine (I-DLT), were injected into New Zealand White rabbits, along with I-DLT-apoB-100-containing LDLs, and the decay of 125I- and 131I-TCA-precipitated counts was followed over 24 hours. At the end of 24 hours, rabbits were anesthetized and their bodies perfused. Organs were removed and homogenized, and TCA-precipitable counts determined. Fractional catabolic rates of apoB truncation particles were two to five times greater than those of apoB-100 LDLs. ApoB truncations accumulated in adrenals at one fifth the rates of apoB-100 LDL, compatible with the functional absences of LDL receptor-recognition domains in truncated apoBs. The major organ of uptake for apoB-100-LDL...Continue Reading

References

Nov 1, 1991·The Journal of Clinical Investigation·D A HardmanM J Malloy
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Citations

Aug 3, 2012·Case Reports in Gastroenterology·Mindy C W LamUrs P Steinbrecher
May 20, 1999·The Journal of Clinical Investigation·Z ChenG Schonfeld
Mar 18, 2003·Journal of Lipid Research·Gustav Schonfeld
Nov 13, 2014·Journal of Lipid Research·Emile Levy
Feb 11, 2020·Current Opinion in Lipidology·Francine K Welty
Jun 16, 2007·Atherosclerosis·Patrizia TarugiSebastiano Calandra
Aug 20, 2008·Clinica Chimica Acta; International Journal of Clinical Chemistry·Trond P Leren, Knut Erik Berge

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