Cited by 424Lipid metabolism and disordersLipoproteins and Cardiovascular HealthCholesterol and Lipid Metabolism

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Apolipoprotein B metabolism in subjects with deficiency of apolipoproteins CIII and AI: evidence that apolipoprotein CIII inhibits catabolism of triglyceride-rich lipoproteins by lipoprotein lipase in vivo

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Ginsberg, H N, Le, N A, Goldberg, I J, Gibson, J C, Rubinstein, A, Wang-Iverson, P, Norum, R, Brown, W V·1986·Journal of Clinical Investigation

DOI 10.1172/jci112713PMC PMC423815

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Abstract

Previous data suggest that apolipoprotein (apo) CIII may inhibit both triglyceride hydrolysis by lipoprotein lipase (LPL) and apo E-mediated uptake of triglyceride-rich lipoproteins by the liver. We studied apo B metabolism in very low density (VLDL), intermediate density (IDL), and low density lipoproteins (LDL) in two sisters with apo CIII-apo AI deficiency. The subjects had reduced levels of VLDL triglyceride, normal LDL cholesterol, and near absence of high density lipoprotein (HDL) cholesterol. Compartmental analysis of the kinetics of apo B metabolism after injection of 125I-VLDL and 131I-LDL revealed fractional catabolic rates (FCR) for VLDL apo B that were six to seven times faster than normal. Simultaneous injection of [3H]glycerol demonstrated rapid catabolism of VLDL triglyceride. VLDL apo B was rapidly and efficiently converted to IDL and LDL. The FCR for LDL apo B was normal. In vitro experiments indicated that, although sera from the apo CIII-apo-AI deficient patients were able to normally activate purified LPL, increasing volumes of these sera did not result in the progressive inhibition of LPL activity demonstrable with normal sera. Addition of purified apo CIII to the deficient sera resulted in 20-50% reductions in maximal LPL activity compared with levels of activity attained with the same volumes of the native, deficient sera. These in vitro studies, together with the in vivo results, indicate that in normal subjects apo CIII can inhibit the catabolism of triglyceride-rich lipoproteins by lipoprotein lipase.

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Authors: Ginsberg, H. N., Le, N. A., Goldberg, I. J., Gibson, J. C., Rubinstein, A., Wang-Iverson, P., Norum, R., & Brown, W. V.
Affiliations: Columbia University Irving Medical Center (US)
Icahn School of Medicine at Mount Sinai (US)
Henry Ford Hospital (US)
ORCID: Ginsberg, H N
Le, N A
Goldberg, I J
Rubinstein, A
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 1986-11-01
Volume: 78
Issue: 5
Pages: 1287-1295
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci112713
PMC: PMC423815
OpenAlex: W2057271976
Cited by: 424
References: 38
Citations by year: 2026: 4 · 2025: 5 · 2024: 5 · 2023: 7 · 2022: 11 · 2021: 15 · 2020: 23 · 2019: 9 · 2018: 15 · 2017: 18 · 2016: 12 · 2015: 18 · 2014: 11 · 2013: 14 · 2012: 8
FWCI: 4.39
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Clinical Investigation (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Heart, Lung, and Blood Institute (HL-23077, HL-00949)
National Center for Research Resources (RR 71)
Topics: Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
Keywords: apolipoprotein C-III, apolipoprotein A-I deficiency, lipoprotein lipase inhibition, triglyceride-rich lipoproteins, VLDL, IDL, low-density lipoprotein, fractional catabolic rate, lipoprotein catabolism, lipoprotein lipase activation
MeSH terms: Adult, Apolipoproteins A, Apolipoproteins B, Apolipoproteins C, Cholesterol, Humans, Hypolipoproteinemias, Kinetics, Lipoprotein Lipase, Lipoproteins, LDL, Lipoproteins, VLDL, Models, Biological, Triglycerides, Apolipoprotein A-I, Apolipoprotein C-II

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Apolipoprotein B metabolism in subjects with deficiency of apolipoproteins CIII and AI: evidence that apolipoprotein CIII inhibits catabolism of triglyceride-rich lipoproteins by lipoprotein lipase in vivo

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