Search results for CETP

Showing 13 results out of 13

×

Species

Types

Compartments

Reaction types

Search properties

Species

Types

Compartments

Reaction types

Search properties

Protein (1 results from a total of 1)

Identifier: R-HSA-194231
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: CETP: P11597

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-9035188
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000087237

Reaction (6 results from a total of 6)

Identifier: R-HSA-9035133
Species: Homo sapiens
Compartment: nucleoplasm
Cholesteryl ester transfer protein (CETP) transfers cholesteryl esters from high density lipoprotein particles to triglyceride-rich lipoproteins for subsequent clearance by the liver. CETP expression can be transcriptionally activated by liver X receptors (LXRα (NR1H3) and LXRβ (NR1H2)) that belong to the nuclear receptor superfamily of ligand-activated transcription factors. Activation of NR1H2,3 induced expression via an LXR response element (LXRE) consisting of 2 hexanucleotide sequences separated by 4 intervening bases (an LXRE of the DR4 type) in the CETP promoter (Luo Y & Tall AR 2000), which may be more responsive to NR1H3 (LXRα) rather than NR1H2 (LXRβ) (Honzumi S et al. 2010). Treatment with T0901317, a synthetic agonist of NR1H2, 3, increased CETP mRNA levels in human liver carcinoma HepG2 cells by approximately 220%, while NR1H3 silencing markedly diminished the increased expression of CETP (Shimada A et al. 2016). It should be noted that CETP is not expressed in the mouse or rat (it is a pseudogene in these species, Hogarth CA et al. 2003), so studies of LXR-mediated regulation of CETP and its effects have been performed in human, hamster, and non-human primates (Groot PHE, et al. 2005).
Identifier: R-HSA-9035169
Species: Homo sapiens
Compartment: nucleoplasm
The CETP gene is transcribed to yield mRNA and the mRNA is translated to yield protein. CETP expression can be transcriptionally activated by liver X receptors (LXRα (NR1H3) and LXRβ (NR1H2)) that belong to the nuclear receptor superfamily of ligand-activated transcription factors. Activation of NR1H2,3 induced expression via an LXR response element (LXRE) consisting of 2 hexanucleotide sequences separated by 4 intervening bases (an LXRE of the DR4 type) in the CETP promoter (Luo Y & Tall AR 2000), which may be more responsive to LXRα rather than LXRβ (Honzumi S et al. 2010). Treatment with T0901317, a synthetic agonist of NR1H2,3, increased CETP mRNA levels in human liver carcinoma HepG2 cells by approximately 220%, while NR1H3 silencing markedly diminished the increased expression of CETP (Shimada A et al. 2016). It should be noted that CETP is not expressed in the mouse or rat (it is a pseudogene in these species, Hogarth CA et al. 2003) so studies of LXR-mediated regulation of CETP have been performed in human, hamster, and non-human primates (Groot PHE, et al. 2005).
Identifier: R-HSA-349404
Species: Homo sapiens
Compartment: extracellular region
Torcetrapib associates with a molecule of CETP and a spherical HDL particle to form a stable complex, thus trapping CETP and inhibiting CETP-mediated lipid transfer between HDL and LDL (Clark et al. 2006).
Identifier: R-HSA-266350
Species: Homo sapiens
Compartment: extracellular region
CETP (cholesterol ester transfer protein) complexed with cholesterol esters interacts with an LDL (low density lipoprotein) particle, acquiring triacylglycerol molecules and donating cholesterol ester to the LDL (Swenson et al. 1988; Morton and Zilversmit 1983). This process is reversible but in the body proceeds in the direction annotated here. A model for the lipid exchange process has been proposed based on recent studies of the structure of CETP:lipid complexes (Qiu et al. 2007).

Apolipoprotein F (APOF) can be associated with HDLs and LDLs. It can inhibit cholesteryl ester transfer protein (CETP) activity, thus inhibiting CETP-mediated transfer events specifically involving the LDL particle (Wang et al. 1999). The function of HDL-associated APOF, which represents >75% of the total plasma pool, is currently unknown. Although over-expression of mouse ApoF can accelerate plasma clearance of HDL (Lagor et al. 2009), physiological levels of ApoF do not affect HDL clearance (Lagor et al. 2012).

Apolipoprotein C-I (APOC1) is an Inhibitor of lipoproteins binding to their respective low density lipoprotein LDL receptor (LDLR), LDL receptor-related protein, and very low density lipoprotein receptor (VLDLR). It directly binds circulating fatty acids therby inhibiting their cellular uptake and is also the major plasma inhibitor of CETP (Westerterp et al. 2007).
Identifier: R-HSA-266328
Species: Homo sapiens
Compartment: extracellular region
CETP (cholesterol ester transfer protein) complexed with triacylglycerol interacts with a spherical HDL (high density lipoprotein) particle, acquiring cholesterol ester molecules and donating triacylglycerol to the HDL (Swenson et al. 1988; Morton and Zilversmit 1983). This process is reversible but in the body proceeds in the direction annotated here. A model for the lipid exchange process has been proposed based on recent studies of the structure of CETP:lipid complexes (Qiu et al. 2007).
Identifier: R-HSA-9031518
Species: Homo sapiens
Compartment: nucleoplasm
Ligand-activated liver X receptors (LXRα, NR1H3 and LXRβ NR1H2) induce expression of a cluster of apolipoprotein genes APOE, APOC1, APOC2 and APOC4 in both human and mouse macrophages (Mak PA et al. 2002). Induction was attenuated or abolished in macrophages derived from LXR α/β-/- mice. Studies with reporter genes suggest that the LXR response element (LXRE) in the distal multienhancer regions ME.1 and ME.2 are necessary for the expression of this gene cluster (Mak PA et al. 2002). These secreted apolipoproteins regulate lipid transport and catabolism. In particular, APOC1 has been suggested to serve as an inhibitor of cholesteryl ester transfer protein (CETP) activity to impact cholesterol distribution among lipoprotein particles (Gautier T et al. 2000).

Complex (3 results from a total of 3)

Identifier: R-HSA-266351
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-266340
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-349410
Species: Homo sapiens
Compartment: extracellular region

Pathway (2 results from a total of 2)

Identifier: R-HSA-8964058
Species: Homo sapiens
HDL (high-density lipoprotein) particles play a central role in the reverse transport of cholesterol, the process by which cholesterol in tissues other than the liver is returned to the liver for conversion to bile salts and excretion from the body and provided to tissues such as the adrenals and gonads for steroid hormone synthesis (Tall et al. 2008).
ABCG1 mediates the movement of intracellular cholesterol to the extracellular face of the plasma membrane where it is accessible to circulating HDL (Vaughan & Oram 2005). Spherical (mature) HDL particles can acquire additional molecules of free cholesterol (CHOL) and phospholipid (PL) from cell membranes.
At the HDL surface, LCAT (lecithin-cholesterol acyltransferase) associates strongly with HDL particles and, activated by apoA-I, catalyzes the reaction of cholesterol and phosphatidylcholine to yield cholesterol esterified with a long-chain fatty acid and 2-lysophosphatidylcholine. The hydrophobic cholesterol ester reaction product is strongly associated with the HDL particle while the 2-lysophosphatidylcholine product is released. Torcetrapib associates with a molecule of CETP and a spherical HDL particle to form a stable complex, thus trapping CETP and inhibiting CETP-mediated lipid transfer between HDL and LDL (Clark et al. 2006).
Spherical HDL particles can bind apoC-II, apoC-III and and apoE proteins.
Identifier: R-HSA-8964041
Species: Homo sapiens
LDL (low density lipoproteins) are complexes of a single molecule of apoprotein B-100 (apoB-100) non-covalently associated with triacylglycerol, free cholesterol, cholesterol esters, and phospholipids. CETP (cholesterol ester transfer protein) complexed with cholesterol esters interacts with an LDL (low density lipoprotein) particle, acquiring triacylglycerol molecules and donating cholesterol ester to the LDL (Swenson et al. 1988; Morton & Zilversmit 1983), a key step in the transport of tissue cholesterol to the liver.
As an alternative to LDLR-mediated uptake and degradation, a LDL particle can bind a single molecule of LPA (apolipoprotein A), forming a Lp(a) lipoprotein particle (Lobentanz et al. 1998).
Cite Us!