Home LiteratureArticle Details
PMID: 2845951 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Uptake of LDL in parenchymal and non-parenchymal rabbit liver cells in vivo. LDL uptake is increased in endothelial cells in cholesterol-fed rabbits.

The Biochemical journal ·Vol. 254 ·No. 2 ·1988-09-01 ·Pages 443-8

Nenseter MS, Blomhoff R, Drevon CA, Kindberg GM, Norum KR, Berg T

Abstract

1. Hepatic uptake of low-density lipoprotein (LDL) in parenchymal cells and non-parenchymal cells was studied in control-fed and cholesterol-fed rabbits after intravenous injection of radioiodinated native LDL (125I-TC-LDL) and methylated LDL (131I-TC-MetLDL). 2. LDL was taken up by rabbit liver parenchymal cells, as well as by endothelial and Kupffer cells. Parenchymal cells, however, were responsible for 92% of the hepatic LDL uptake. 3. Of LDL in the hepatocytes, 89% was taken up via the B,E receptor, whereas 16% and 32% of the uptake of LDL in liver endothelial cells and Kupffer cells, respectively, was B,E receptor-dependent. 4. Cholesterol feeding markedly reduced B,E receptor-mediated uptake of LDL in parenchymal liver cells and in Kupffer cells, to 19% and 29% of controls, respectively. Total uptake of LDL in liver endothelial cells was increased about 2-fold. This increased uptake is probably mediated via the scavenger receptor. The B,E receptor-independent association of LDL with parenchymal cells was not affected by the cholesterol feeding. 5. It is concluded that the B,E receptor is located in parenchymal as well as in the non-parenchymal rabbit liver cells, and that this receptor is down-regulated by cholesterol feeding. Parenchymal cells are the main site of hepatic uptake of LDL, both under normal conditions and when the number of B,E receptors is down-regulated by cholesterol feeding. In addition, LDL is taken up by B,E receptor-independent mechanism(s) in rabbit liver parenchymal, endothelial and Kupffer cells. The non-parenchymal liver cells may play a quantitatively important role when the concentration of circulating LDL is maintained at a high level in plasma, being responsible for 26% of hepatic uptake of LDL in cholesterol-fed rabbits as compared with 8% in control-fed rabbits. The proportion of hepatic LDL uptake in endothelial cells was greater than 5-fold higher in the diet-induced hypercholesterolaemic rabbits than in controls.

MeSH Terms
Animals Cellobiose/pharmacokinetics Cholesterol, Dietary/pharmacology Endothelium/drug effects,metabolism In Vitro Techniques Kupffer Cells/drug effects,metabolism Lipoproteins, LDL/pharmacokinetics Liver/cytology,drug effects,metabolism Male Methylation Rabbits Receptors, Cell Surface/metabolism Receptors, Lipoprotein Tissue Distribution Tyramine/pharmacokinetics
Chemicals
Cholesterol, Dietary Lipoproteins, LDL Receptors, Cell Surface Receptors, Lipoprotein apolipoprotein B,E receptor tyramine-cellobiose adduct Cellobiose Tyramine
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Nenseter M S
Institute for Nutrition Research, University of Oslo, Norway.
Blomhoff R
Drevon C A
Kindberg G M
Norum K R
Berg T
References (31)
31 references, click to expand
  1. Impaired receptor-mediated catabolism of low density lipoproteins in fasted rabbits.
    J Lipid Res. 1984 Jan;25(1):33-9 PMID: 6323605
  2. Lipoprotein metabolism in the macrophage: implications for cholesterol deposition in atherosclerosis.
    Annu Rev Biochem. 1983;52:223-61 PMID: 6311077
  3. Clearance of acetyl low density lipoprotein by rat liver endothelial cells. Implications for hepatic cholesterol metabolism.
    J Biol Chem. 1984 Jul 25;259(14):8898-903 PMID: 6086616
  4. Quantitative role of parenchymal and non-parenchymal liver cells in the uptake of [14C]sucrose-labelled low-density lipoprotein in vivo.
    Biochem J. 1984 Nov 15;224(1):21-7 PMID: 6508758
  5. Sites and mechanisms of uptake and degradation of high density and low density lipoproteins.
    J Lipid Res. 1984 Dec 15;25(13):1577-85 PMID: 6397563
  6. Increased mRNA for low density lipoprotein receptor in livers of rabbits treated with 17 alpha-ethinyl estradiol.
    Proc Natl Acad Sci U S A. 1986 Feb;83(3):792-6 PMID: 2418443
  7. A receptor-mediated pathway for cholesterol homeostasis.
    Science. 1986 Apr 4;232(4746):34-47 PMID: 3513311
  8. Hepatic processing of the cholesteryl ester from low density lipoprotein in the rat.
    J Biol Chem. 1986 Jul 5;261(19):8908-13 PMID: 3722182
  9. Role of receptor-independent low density lipoprotein transport in the maintenance of tissue cholesterol balance in the normal and WHHL rabbit.
    J Lipid Res. 1987 Jan;28(1):32-41 PMID: 3559399
  10. Intracellular transport and degradation of chylomicron remnants in rat liver cells after in vivo endocytosis.
    Biochim Biophys Acta. 1987 Jun 15;929(1):25-33 PMID: 3593771
  11. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  12. The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum.
    J Clin Invest. 1955 Sep;34(9):1345-53 PMID: 13252080
  13. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  14. Distribution of lysosomal enzymes in different types of rat liver cells.
    Exp Cell Res. 1976 Apr;99(1):146-54 PMID: 4333
  15. Chylomicron remnant cholesteryl esters as the major constituent of very low density lipoproteins in plasma of cholesterol-fed rabbits.
    J Lipid Res. 1977 Mar;18(2):169-81 PMID: 191549
  16. In vivo and in vitro uptake and degradation of acetylated low density lipoprotein by rat liver endothelial, Kupffer, and parenchymal cells.
    J Biol Chem. 1983 Oct 25;258(20):12221-7 PMID: 6313644
  17. Transport of cholesterol.
    Physiol Rev. 1983 Oct;63(4):1343-419 PMID: 6361811
  18. Newly administered [3H]retinol is transferred from hepatocytes to stellate cells in liver for storage.
    Exp Cell Res. 1984 Jan;150(1):186-93 PMID: 6420172
  19. Preparation of isolated liver endothelial cells and Kupffer cells in high yield by means of an enterotoxin.
    Exp Cell Res. 1984 Jan;150(1):194-204 PMID: 6319161
  20. Role of lysine residues of plasma lipoproteins in high affinity binding to cell surface receptors on human fibroblasts.
    J Biol Chem. 1978 Dec 25;253(24):9053-62 PMID: 214439
  21. Altered metabolism (in vivo and in vitro) of plasma lipoproteins after selective chemical modification of lysine residues of the apoproteins.
    J Clin Invest. 1979 Sep;64(3):743-50 PMID: 224077
  22. Reversible accumulation of cholesteryl esters in macrophages incubated with acetylated lipoproteins.
    J Cell Biol. 1979 Sep;82(3):597-613 PMID: 229107
  23. Inhibition of receptor-mediated clearance of lysine and arginine-modified lipoproteins from the plasma of rats and monkeys.
    Proc Natl Acad Sci U S A. 1980 Jan;77(1):225-9 PMID: 6767236
  24. Regulation of plasma cholesterol by lipoprotein receptors.
    Science. 1981 May 8;212(4495):628-35 PMID: 6261329
  25. Conversational SAAM--an interactive program for kinetic analysis of biological systems.
    Comput Programs Biomed. 1981 Mar-Jun;13(1-2):111-9 PMID: 7285558
  26. Receptor-dependent and receptor-independent degradation of low density lipoprotein in normal rabbits and in receptor-deficient mutant rabbits.
    J Biol Chem. 1982 Jul 25;257(14):7994-8000 PMID: 6282866
  27. Impaired receptor-mediated catabolism of low density lipoprotein in the WHHL rabbit, an animal model of familial hypercholesterolemia.
    Proc Natl Acad Sci U S A. 1982 May;79(10):3305-9 PMID: 6285345
  28. Receptor-mediated catabolism and tissue uptake of human low density lipoprotein in the cholesterol-fed, atherosclerotic rabbit.
    Biochim Biophys Acta. 1982 Nov 12;713(2):435-45 PMID: 6295500
  29. Enhanced macrophage degradation of biologically modified low density lipoprotein.
    Arteriosclerosis. 1983 Mar-Apr;3(2):149-59 PMID: 6838433
  30. A radioiodinated, intracellularly trapped ligand for determining the sites of plasma protein degradation in vivo.
    Biochem J. 1983 Jun 15;212(3):791-800 PMID: 6882394
  31. Measurement in vivo of irreversible degradation of low density lipoprotein in the rabbit aorta. Predominance of intimal degradation.
    Arteriosclerosis. 1984 May-Jun;4(3):214-24 PMID: 6324731
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2540443
Published
1988-09-01
Pages
443-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1135097
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2540443 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2