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Journal of Lipid Research, Vol 38, 2173-2192, Copyright © 1997 by Lipid Research, Inc.
Hepatic uptake of chylomicron remnants
AD Cooper
Research Institute, Palo Alto Medical Foundation, CA 94301, USA.
Chylomicrons are formed in the intestine and transport dietary triglyceride
to peripheral tissues and cholesterol to the liver. The enzyme lipoprotein
lipase, with apolipoprotein (apo)C-II as a co- factor, hydrolyzes
chylomicron triglyceride allowing the delivery of free fatty acids to
muscle and adipose tissue. As a result, a new particle called a chylomicron
remnant is formed. This particle is enriched in cholesteryl ester and
fat-soluble vitamins and contains apoB-48 and apoE. It is rapidly removed
from the circulation by the liver. ApoE is the moiety required for rapid
hepatic removal. Its activity is inhibited by C apolipoproteins, especially
apoC-I. Hepatic removal appears to be accomplished by several overlapping
mechanisms. The particle must first achieve a size that allows it to be
"sieved" through the endothelial fenestre allowing entrance into the space
of Disse. Here, it may 1) be removed directly by LDL receptors; 2) acquire
additional apoE that is secreted free into the space, and then be removed
directly by the LDL receptor-related protein (LRP); or 3) it may be
sequestered in the space. Sequestration occurs by binding of apoE to
heparan sulfate proteoglycans and/or binding of apoB to hepatic lipase.
Sequestered particles may be further metabolized allowing apoE, and
lysophospholipid enrichment, followed by transfer to one of the above
receptors for hepatic uptake. The above formulation is based upon animal
studies. In humans, delayed removal of chylomicron remnants has been
documented in diabetes, renal failure, and familial combined hyperlipemia
and is the abnormality resulting in type III hyperlipidemia. Case control
studies have identified delayed remnant removal as an independent risk
factor for atherosclerotic cardiovascular disease. Thus, understanding the
further details of the processes, and how it can be regulated in humans, is
an important challenge for the future.

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K. C-W. Yu, Y. Jiang, W. Chen, and A. D. Cooper
Evaluation of the components of the chylomicron remnant removal mechanism by use of the isolated perfused mouse liver
J. Lipid Res.,
October 1, 1999;
40(10):
1899 - 1910.
[Abstract]
[Full Text]
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N. Mero, L. Suurinkeroinen, M. Syvanne, P. Knudsen, H. Yki-Jarvinen, and M.-R. Taskinen
Delayed clearance of postprandial large TG-rich particles in normolipidemic carriers of LPL Asn291Ser gene variant
J. Lipid Res.,
September 1, 1999;
40(9):
1663 - 1670.
[Abstract]
[Full Text]
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C. T Phan, B.-C. Mortimer, I. J Martins, and T. G Redgrave
Plasma clearance of chylomicrons from butterfat is not dependent on saturation: studies with butterfat fractions and other fats containing triacylglycerols with low or high melting points
Am. J. Clinical Nutrition,
June 1, 1999;
69(6):
1151 - 1161.
[Abstract]
[Full Text]
[PDF]
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F. T. Yen, M. Masson, N. Clossais-Besnard, P. Andre, J.-M. Grosset, L. Bougueleret, J.-B. Dumas, O. Guerassimenko, and B. E. Bihain
Molecular Cloning of a Lipolysis-stimulated Remnant Receptor Expressed in the Liver
J. Biol. Chem.,
May 7, 1999;
274(19):
13390 - 13398.
[Abstract]
[Full Text]
[PDF]
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S. E. Crawford and J. Borensztajn
Plasma clearance and liver uptake of chylomicron remnants generated by hepatic lipase lipolysis: evidence for a lactoferrin-sensitive and apolipoprotein E-independent pathway
J. Lipid Res.,
May 1, 1999;
40(5):
797 - 805.
[Abstract]
[Full Text]
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W. A. Bradley, M. L. Brown, M. P. Ramprasad, R. Li, R. Song, and S. H. Gianturco
Antipeptide antibodies reveal interrelationships of MBP 200 and MBP 235: unique apoB-specific receptors for triglyceride-rich lipoproteins on human monocyte-macrophages
J. Lipid Res.,
April 1, 1999;
40(4):
744 - 752.
[Abstract]
[Full Text]
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A. M. van Bennekum, Y. Kako, P. H. Weinstock, E. H. Harrison, R. J. Deckelbaum, I. J. Goldberg, and W. S. Blaner
Lipoprotein lipase expression level influences tissue clearance of chylomicron retinyl ester
J. Lipid Res.,
March 1, 1999;
40(3):
565 - 574.
[Abstract]
[Full Text]
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D. L. Silver, X.-c. Jiang, and A. R. Tall
Increased High Density Lipoprotein (HDL), Defective Hepatic Catabolism of ApoA-I and ApoA-II, and Decreased ApoA-I mRNA in ob/ob Mice. POSSIBLE ROLE OF LEPTIN IN STIMULATION OF HDL TURNOVER
J. Biol. Chem.,
February 12, 1999;
274(7):
4140 - 4146.
[Abstract]
[Full Text]
[PDF]
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J Heeren, W Weber, and U Beisiegel
Intracellular processing of endocytosed triglyceride-rich lipoproteins comprises both recycling and degradation
J. Cell Sci.,
January 2, 1999;
112(3):
349 - 359.
[Abstract]
[PDF]
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R. W. Mahley and Z.-S. Ji
Remnant lipoprotein metabolism: key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E
J. Lipid Res.,
January 1, 1999;
40(1):
1 - 16.
[Abstract]
[Full Text]
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M. Schmitt and T. Grand-Perret
Regulated turnover of a cell surface-associated pool of newly synthesized apolipoprotein E in HepG2 cells
J. Lipid Res.,
January 1, 1999;
40(1):
39 - 49.
[Abstract]
[Full Text]
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D. M. Pitterle, R. T. Sperling, M. G. Myers Jr., M. F. White, and P. J. Blackshear
Early biochemical events in insulin-stimulated fluid phase endocytosis
Am J Physiol Endocrinol Metab,
January 1, 1999;
276(1):
E94 - E105.
[Abstract]
[Full Text]
[PDF]
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S. D. Turley, D. K. Burns, and J. M. Dietschy
Preferential utilization of newly synthesized cholesterol for brain growth in neonatal lambs
Am J Physiol Endocrinol Metab,
June 1, 1998;
274(6):
E1099 - E1105.
[Abstract]
[Full Text]
[PDF]
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A. M. van Bennekum, S. Wei, M. V. Gamble, S. Vogel, R. Piantedosi, M. Gottesman, V. Episkopou, and W. S. Blaner
Biochemical Basis for Depressed Serum Retinol Levels in Transthyretin-deficient Mice
J. Biol. Chem.,
January 5, 2001;
276(2):
1107 - 1113.
[Abstract]
[Full Text]
[PDF]
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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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