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Regulation by long-chain fatty acids of the expression of cholesteryl ester transfer protein in HepG2 cells

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Lipids

Abstract

Cholesteryl ester transfer protein (CETP) is an important determinant of lipoprotein function, especially high density lipoprotein (HDL) metabolism, and contributes to the regulation of plasma HDL levels. Since saturated and polyunsaturated fatty acids (FA) appear to influence the CETP activity differently, we decided to investigate the effects of FA on the expression of CETP mRNA in HepG2 cells using an RNA blot hybridization analysis. Long-chain FA (>18 carbons) at a 0.5 mM concentration were added to the medium and incubated with cells for 48 h at 37°C under 5% CO2. After treatment with 0.5 mM arachidonic (AA), eicosapentaenoic (EPA), and docosahexaenoic acid (DHA), the levels of CETP mRNA were less than 50% of the control levels (AA, P=0.0005; EPA, P<0.01; DHA, P<0.0001), with a corresponding significant decrease in the CETP mass. These results suggest that FA regulate the gene expression of CETP in HepG2 and this effect is dependent upon the degree of unsaturation of the acyl carbon chain in FA.

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Abbreviations

AA:

arachidonic acid

aLA:

α-linolenic acid

BSA:

bovine serum albumin

C/EBP:

CCAAT/enhancer binding protein

CETP:

cholesteryl ester transfer protein

DgLA:

dihomo-γ-linolenic acid

DHA:

docosahexaenoic acid

DMEM:

Dulbecco's modified Eagle's medium

ELISA:

enzyme-linked immunosorbent assay

EPA:

eicosapentaenoic acid

FA:

fatty acid

gLA:

γ-linolenic acid

LA:

linoleic acid

LCAT:

lecithin-cholesterol acyltransferase

LPL:

lipoprotein lipase

OA:

oleic acid

PBS:

phosphatebuffered saline

PUFA:

polyunsaturated fatty acid

SA:

stearic acid

SDS:

sodium dodecyl sulfate

SREBP:

sterol regulatory element-binding protein

SSPE:

saline-sodium dihydrogenphosphate-ethylenediaminetetraacetate buffer

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Correspondence to Akiyo Matsumoto.

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Hirano, R., Igarashi, O., Kondo, K. et al. Regulation by long-chain fatty acids of the expression of cholesteryl ester transfer protein in HepG2 cells. Lipids 36, 401–406 (2001). https://doi.org/10.1007/s11745-001-0735-3

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  • DOI: https://doi.org/10.1007/s11745-001-0735-3

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