Role of cholesteryl ester transfer protein in selective uptake of high density lipoprotein cholesteryl esters by adipocytes.

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  • Author(s): Vassiliou G;Vassiliou G; McPherson R
  • Source:
    Journal of lipid research [J Lipid Res] 2004 Sep; Vol. 45 (9), pp. 1683-93. Date of Electronic Publication: 2004 Jul 01.
  • Publication Type:
    Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Elsevier Country of Publication: United States NLM ID: 0376606 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0022-2275 (Print) Linking ISSN: 00222275 NLM ISO Abbreviation: J Lipid Res Subsets: MEDLINE
    • Publication Information:
      Publication: 2021- : [New York] : Elsevier
      Original Publication: Memphis, Lipid Research, inc.
    • Subject Terms:
      Adipocytes/*metabolism ; Carrier Proteins/*metabolism ; Cholesterol Esters/*metabolism ; Glycoproteins/*metabolism ; Lipoproteins, HDL/*metabolism; Animals ; Apolipoproteins B/metabolism ; Cells, Cultured ; Cholesterol Ester Transfer Proteins ; Humans ; Kinetics ; Lipoproteins/metabolism ; Mice ; Mice, Inbred Strains ; Receptors, LDL/metabolism
    • Abstract:
      Previous reports attributed cholesteryl ester transfer protein (CETP)-mediated HDL cholesteryl ester (CE) selective uptake to the CETP-mediated transfer of CE from HDL to newly secreted apolipoprotein B-containing lipoproteins, which are then internalized by the LDL receptor (LDL-R). CETP has also been implicated in the remodeling of HDL, which renders it a better substrate for selective uptake by scavenger receptor class B type I (SR-BI). However, CETP-mediated selective uptake of HDL3-derived CE was not diminished in LDL-R null adipocytes, SR-BI null adipocytes, or in the presence of the receptor-associated protein. We found that monensin treatment or energy depletion of the SW872 liposarcoma cells with 2-deoxyglucose and NaN3 had no effect on CETP-mediated selective uptake, demonstrating that endocytosis is not required. This is supported by data indicating that CETP transfers CE into a compartment from which it can be extracted by unlabeled HDL. CETP could also mediate the selective uptake of HDL3-derived triacylglycerol (TG) and phospholipid (PL). The CETP-specific kinetics for TG and CE uptake were similar, and both reached saturation at approximately 5 microg/ml HDL. In contrast, CETP-specific PL uptake did not attain saturation at 5 microg/ml HDL and was approximately 6-fold greater than the uptake of CE. We propose two possible mechanisms to account for the role of CETP in selective uptake.
      (Copyright 2004 American Society for Biochemistry and Molecular Biology, Inc.)
    • Accession Number:
      0 (Apolipoproteins B)
      0 (CETP protein, human)
      0 (Carrier Proteins)
      0 (Cholesterol Ester Transfer Proteins)
      0 (Cholesterol Esters)
      0 (Glycoproteins)
      0 (Lipoproteins)
      0 (Lipoproteins, HDL)
      0 (Receptors, LDL)
    • Publication Date:
      Date Created: 20040703 Date Completed: 20050208 Latest Revision: 20210217
    • Publication Date:
      20231215
    • Accession Number:
      10.1194/jlr.M400051-JLR200
    • Accession Number:
      15231851