Cholesteryl ester transfer protein (CETP) mRNA abundance in human adipose tissue: relationship to cell size and membrane cholesterol content.

Radeau, Thierry; Lau, Paulina; Robb, Malcolm; McDonnell, Michael; Ailhaud, Gérard; McPherson, Ruth

doi:10.1016/s0022-2275(20)41091-0

Cited by 69 publications

(7 citation statements)

References 32 publications

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“…Media aliquots were taken at different times of incubation and treated as previously described (24). At the end of the experiment, the cells were solubilized in 2-propanol and the cholesterol content was determined by gas chromatography (29) after extraction of cellular lipids by the method of Bligh and Dyer (30). Results are expressed as the percentage of labeled cholesterol remaining in the cells as a function of time.…”

Section: Methodsmentioning

confidence: 99%

Deletion of the C-Terminal Domain of Apolipoprotein A-I Impairs Cell Surface Binding and Lipid Efflux in Macrophage

et al. 1999

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The contribution of the amphipathic alpha-helices of apoA-I toward lipid efflux from human skin fibroblasts and macrophage was examined. Four apoA-I mutants were designed, each by deletion of a pair of predicted adjacent helices. Three mutants lacked two consecutive central alpha-helices [Delta(100-143), Delta(122-165), and Delta(144-186)], whereas the final mutant lacked the C-terminal domain [Delta(187-243)]. When compared to recombinant wild-type apoA-I and mutants with central domain deletions, Delta(187-243) exhibited a marked reduction in its ability to promote either cholesterol or phospholipid efflux from THP-1 macrophages. This mutant also demonstrated a decreased ability to bind lipids and to form lipoprotein complexes. In contrast, the four mutants and apoA-I equally supported cholesterol efflux from fibroblasts, albeit with a reduced capacity when compared to macrophages. Delta(187-243) bound poorly to the macrophage cell surface when compared to apoA-I, and competitive binding studies with the central domain and C-terminal deletions mutants showed that only Delta(187-243) did not compete effectively with [(125)I]apoA-I. Omission of PMA during cholesterol loading enhanced cholesterol efflux to both apoA-I (1.5-fold) and the C-terminal deletion mutant (2.5-fold). Inclusion of the Sandoz ACAT inhibitor (58-035) during loading and, in the absence of PMA, increased and equalized cholesterol efflux to apoA-I and Delta(187-243). Surprisingly, omission of PMA during cholesterol loading had minimal effects on the binding of apoA-I or Delta(187-243) to the THP-1 cell surface. Overall, these results show that cholesterol efflux from cells such as fibroblasts does not require any specific sequence between residues 100 and 243 of apoA-I. In contrast, optimal cholesterol efflux in macrophages requires binding of the C-terminal domain of apoA-I to a cell surface-binding site and the subsequent translocation of intracellular cholesterol to an efflux-competent pool.

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Section: Methodsmentioning

confidence: 99%

Deletion of the C-Terminal Domain of Apolipoprotein A-I Impairs Cell Surface Binding and Lipid Efflux in Macrophage

et al. 1999

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“…Cholesteryl ester transfer protein (CETP) is a 74 kDa hydrophobic plasma glycoprotein that mediates the hetero-and homo-exchange of neutral lipid between apoA-I and apoB-containing lipoproteins (1 -3). In humans, adipose tissue is the largest organ expressing CETP (4,5). We have demonstrated, in both humans and hamsters, that there is a strong correlation between adipose tissue CETP mRNA abundance and plasma CETP concentrations (5,6).…”

mentioning

confidence: 72%

Characterization of a cholesterol response element (CRE) in the promoter of the cholesteryl ester transfer protein gene: functional role of the transcription factors SREBP-1a, -2, and YY1.

Gauthier

Robb

Gaudet

et al. 1999

Journal of Lipid Research

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“…Expression of proteins on HDL particles is different depending upon the maturation stage of HDL, with some proteins preferring either HDL2 or HDL3 subclasses, whereas other proteins not displaying any preference presence of ApoA-II compared to ApoA-I alone (Lagrost, Persegol, Lallemant, & Gambert, 1994). While CETP is mainly produced in the liver and adipose tissue (Radeau et al, 1995;Swenson, Simmons, Hesler, Bisgaier, & Tall, 1987), PLTP is ubiquitously expressed (Albers et al, 1995;Guo et al, 1999;Jiang et al, 1998;Vuletic et al, 2003).…”

Section: Remodelling Of Hdlmentioning

confidence: 99%

High‐density lipoprotein‐related cholesterol metabolism in Alzheimer’s disease

Pedrini

Chatterjee

Hone

et al. 2020

Journal of Neurochemistry

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Alzheimer's disease (AD) is the leading cause of dementia in the elderly and the number of affected individuals is set to increase in the next decades. The two main features of AD are represented by extracellular amyloid plaques of amyloid β (Aβ) in the brain parenchyma and intracellular neurofibrillary tangles of tau protein. In the past decades several lines of evidence have indicated that high-density lipoproteins (HDL) are strongly involved in the aetiology and the progression of the disease, although the overall analysis of HDL levels and their association with cognitive functions somehow lacked consensus. Many of the proteins associated with HDL are also linked to AD and Aβ formation/catabolism, some displaying protective features while others do not, it is not surprising the association between HDL levels and AD provided confounding results. It is therefore possible that components of HDL 'protein cargo', more than the HDL levels alone, are responsible for neuroprotection and affect Aβ formation and/or deposition.

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Cholesteryl ester transfer protein (CETP) mRNA abundance in human adipose tissue: relationship to cell size and membrane cholesterol content.

Cited by 69 publications

References 32 publications

Deletion of the C-Terminal Domain of Apolipoprotein A-I Impairs Cell Surface Binding and Lipid Efflux in Macrophage

Deletion of the C-Terminal Domain of Apolipoprotein A-I Impairs Cell Surface Binding and Lipid Efflux in Macrophage

Characterization of a cholesterol response element (CRE) in the promoter of the cholesteryl ester transfer protein gene: functional role of the transcription factors SREBP-1a, -2, and YY1.

High‐density lipoprotein‐related cholesterol metabolism in Alzheimer’s disease

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