A 6.6-kDa protein component of VERY-LOW-DENSITY LIPOPROTEINS; INTERMEDIATE-DENSITY LIPOPROTEINS; and HIGH-DENSITY LIPOPROTEINS. Apo C-I displaces APO E from lipoproteins, modulate their binding to receptors (RECEPTORS, LDL), and thereby decrease their clearance from plasma. Elevated Apo C-I levels are associated with HYPERLIPOPROTEINEMIA and ATHEROSCLEROSIS.
A group of apolipoproteins that can readily exchange among the various classes of lipoproteins (HDL; VLDL; CHYLOMICRONS). After lipolysis of TRIGLYCERIDES on VLDL and chylomicrons, Apo-C proteins are normally transferred to HDL. The subtypes can modulate remnant binding to receptors, LECITHIN CHOLESTEROL ACYLTRANSFERASE, or LIPOPROTEIN LIPASE.
A 9-kDa protein component of VERY-LOW-DENSITY LIPOPROTEINS and CHYLOMICRON REMNANTS. Apo C-III, synthesized in the liver, is an inhibitor of LIPOPROTEIN LIPASE. Apo C-III modulates the binding of chylomicron remnants and VLDL to receptors (RECEPTORS, LDL) thus decreases the uptake of triglyceride-rich particles by the liver cells and subsequent degradation. The normal Apo C-III is glycosylated. There are several polymorphic forms with varying amounts of SIALIC ACID (Apo C-III-0, Apo C-III-1, and Apo C-III-2).
A class of lipoproteins of very light (0.93-1.006 g/ml) large size (30-80 nm) particles with a core composed mainly of TRIGLYCERIDES and a surface monolayer of PHOSPHOLIPIDS and CHOLESTEROL into which are imbedded the apolipoproteins B, E, and C. VLDL facilitates the transport of endogenously made triglycerides to extrahepatic tissues. As triglycerides and Apo C are removed, VLDL is converted to INTERMEDIATE-DENSITY LIPOPROTEINS, then to LOW-DENSITY LIPOPROTEINS from which cholesterol is delivered to the extrahepatic tissues.
Triglycerides are the most common type of fat in the body, stored in fat cells and used as energy; they are measured in blood tests to assess heart disease risk, with high levels often resulting from dietary habits, obesity, physical inactivity, smoking, and alcohol consumption.
The most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. This protein serves as an acceptor for CHOLESTEROL released from cells thus promoting efflux of cholesterol to HDL then to the LIVER for excretion from the body (reverse cholesterol transport). It also acts as a cofactor for LECITHIN CHOLESTEROL ACYLTRANSFERASE that forms CHOLESTEROL ESTERS on the HDL particles. Mutations of this gene APOA1 cause HDL deficiency, such as in FAMILIAL ALPHA LIPOPROTEIN DEFICIENCY DISEASE and in some patients with TANGIER DISEASE.
An inhibitory subclass of NK cell lectin-like receptors that interacts with CLASS I MAJOR HISTOCOMPATIBILITY ANTIGENS and prevents the activation of NK CELLS.
Structurally-related receptors that are typically found on NATURAL KILLER CELLS. They are considered lectin-like proteins in that they share sequence homology with the carbohydrate binding domains of C-TYPE LECTINS. They differ from classical C-type lectins, however, in that they appear to lack CALCIUM-binding domains.
A class of protein components which can be found in several lipoproteins including HIGH-DENSITY LIPOPROTEINS; VERY-LOW-DENSITY LIPOPROTEINS; and CHYLOMICRONS. Synthesized in most organs, Apo E is important in the global transport of lipids and cholesterol throughout the body. Apo E is also a ligand for LDL receptors (RECEPTORS, LDL) that mediates the binding, internalization, and catabolism of lipoprotein particles in cells. There are several allelic isoforms (such as E2, E3, and E4). Deficiency or defects in Apo E are causes of HYPERLIPOPROTEINEMIA TYPE III.
A 513-kDa protein synthesized in the LIVER. It serves as the major structural protein of low-density lipoproteins (LIPOPROTEINS, LDL; LIPOPROTEINS, VLDL). It is the ligand for the LDL receptor (RECEPTORS, LDL) that promotes cellular binding and internalization of LDL particles.
A group of lymphocyte surface antigens located on mouse LYMPHOCYTES. Specific Ly antigens are useful markers for distinguishing subpopulations of lymphocytes.
Major structural proteins of triacylglycerol-rich LIPOPROTEINS. There are two forms, apolipoprotein B-100 and apolipoprotein B-48, both derived from a single gene. ApoB-100 expressed in the liver is found in low-density lipoproteins (LIPOPROTEINS, LDL; LIPOPROTEINS, VLDL). ApoB-48 expressed in the intestine is found in CHYLOMICRONS. They are important in the biosynthesis, transport, and metabolism of triacylglycerol-rich lipoproteins. Plasma Apo-B levels are high in atherosclerotic patients but non-detectable in ABETALIPOPROTEINEMIA.
A major and the second most common isoform of apolipoprotein E. In humans, Apo E4 differs from APOLIPOPROTEIN E3 at only one residue 112 (cysteine is replaced by arginine), and exhibits a lower resistance to denaturation and greater propensity to form folded intermediates. Apo E4 is a risk factor for ALZHEIMER DISEASE and CARDIOVASCULAR DISEASES.
A 34-kDa glycosylated protein. A major and most common isoform of apolipoprotein E. Therefore, it is also known as apolipoprotein E (ApoE). In human, Apo E3 is a 299-amino acid protein with a cysteine at the 112 and an arginine at the 158 position. It is involved with the transport of TRIGLYCERIDES; PHOSPHOLIPIDS; CHOLESTEROL; and CHOLESTERYL ESTERS in and out of the cells.
The second most abundant protein component of HIGH DENSITY LIPOPROTEINS or HDL. It has a high lipid affinity and is known to displace APOLIPOPROTEIN A-I from HDL particles and generates a stable HDL complex. ApoA-II can modulate the activation of LECITHIN CHOLESTEROL ACYLTRANSFERASE in the presence of APOLIPOPROTEIN A-I, thus affecting HDL metabolism.
Protein components on the surface of LIPOPROTEINS. They form a layer surrounding the hydrophobic lipid core. There are several classes of apolipoproteins with each playing a different role in lipid transport and LIPID METABOLISM. These proteins are synthesized mainly in the LIVER and the INTESTINES.
A 9-kDa protein component of VERY-LOW-DENSITY LIPOPROTEINS. It contains a cofactor for LIPOPROTEIN LIPASE and activates several triacylglycerol lipases. The association of Apo C-II with plasma CHYLOMICRONS; VLDL, and HIGH-DENSITY LIPOPROTEINS is reversible and changes rapidly as a function of triglyceride metabolism. Clinically, Apo C-II deficiency is similar to lipoprotein lipase deficiency (HYPERLIPOPROTEINEMIA TYPE I) and is therefore called hyperlipoproteinemia type IB.
Structural proteins of the alpha-lipoproteins (HIGH DENSITY LIPOPROTEINS), including APOLIPOPROTEIN A-I and APOLIPOPROTEIN A-II. They can modulate the activity of LECITHIN CHOLESTEROL ACYLTRANSFERASE. These apolipoproteins are low in atherosclerotic patients. They are either absent or present in extremely low plasma concentration in TANGIER DISEASE.
A 241-kDa protein synthesized only in the INTESTINES. It serves as a structural protein of CHYLOMICRONS. Its exclusive association with chylomicron particles provides an indicator of intestinally derived lipoproteins in circulation. Apo B-48 is a shortened form of apo B-100 and lacks the LDL-receptor region.
One of three major isoforms of apolipoprotein E. In humans, Apo E2 differs from APOLIPOPROTEIN E3 at one residue 158 where arginine is replaced by cysteine (R158--C). In contrast to Apo E3, Apo E2 displays extremely low binding affinity for LDL receptors (RECEPTORS, LDL) which mediate the internalization and catabolism of lipoprotein particles in liver cells. ApoE2 allelic homozygosity is associated with HYPERLIPOPROTEINEMIA TYPE III.
A class of lipoproteins of small size (4-13 nm) and dense (greater than 1.063 g/ml) particles. HDL lipoproteins, synthesized in the liver without a lipid core, accumulate cholesterol esters from peripheral tissues and transport them to the liver for re-utilization or elimination from the body (the reverse cholesterol transport). Their major protein component is APOLIPOPROTEIN A-I. HDL also shuttle APOLIPOPROTEINS C and APOLIPOPROTEINS E to and from triglyceride-rich lipoproteins during their catabolism. HDL plasma level has been inversely correlated with the risk of cardiovascular diseases.
A large and highly glycosylated protein constituent of LIPOPROTEIN (A). It has very little affinity for lipids but forms disulfide-linkage to APOLIPOPROTEIN B-100. Apoprotein(a) has SERINE PROTEINASE activity and can be of varying sizes from 400- to 800-kDa. It is homologous to PLASMINOGEN and is known to modulate THROMBOSIS and FIBRINOLYSIS.
The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils.
Lipid-protein complexes involved in the transportation and metabolism of lipids in the body. They are spherical particles consisting of a hydrophobic core of TRIGLYCERIDES and CHOLESTEROL ESTERS surrounded by a layer of hydrophilic free CHOLESTEROL; PHOSPHOLIPIDS; and APOLIPOPROTEINS. Lipoproteins are classified by their varying buoyant density and sizes.
A lipoprotein that resembles the LOW-DENSITY LIPOPROTEINS but with an extra protein moiety, APOPROTEIN (A) also known as APOLIPOPROTEIN (A), linked to APOLIPOPROTEIN B-100 on the LDL by one or two disulfide bonds. High plasma level of lipoprotein (a) is associated with increased risk of atherosclerotic cardiovascular disease.
A glycoprotein component of HIGH-DENSITY LIPOPROTEINS that transports small hydrophobic ligands including CHOLESTEROL and STEROLS. It occurs in the macromolecular complex with LECITHIN CHOLESTEROL ACYLTRANSFERASE. Apo D is expressed in and secreted from a variety of tissues such as liver, placenta, brain tissue and others.
A class of lipoproteins of small size (18-25 nm) and light (1.019-1.063 g/ml) particles with a core composed mainly of CHOLESTEROL ESTERS and smaller amounts of TRIGLYCERIDES. The surface monolayer consists mostly of PHOSPHOLIPIDS, a single copy of APOLIPOPROTEIN B-100, and free cholesterol molecules. The main LDL function is to transport cholesterol and cholesterol esters to extrahepatic tissues.
A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed)
Receptors on the plasma membrane of nonhepatic cells that specifically bind LDL. The receptors are localized in specialized regions called coated pits. Hypercholesteremia is caused by an allelic genetic defect of three types: 1, receptors do not bind to LDL; 2, there is reduced binding of LDL; and 3, there is normal binding but no internalization of LDL. In consequence, entry of cholesterol esters into the cell is impaired and the intracellular feedback by cholesterol on 3-hydroxy-3-methylglutaryl CoA reductase is lacking.
A thickening and loss of elasticity of the walls of ARTERIES that occurs with formation of ATHEROSCLEROTIC PLAQUES within the ARTERIAL INTIMA.
Cholesterol which is contained in or bound to high-density lipoproteins (HDL), including CHOLESTEROL ESTERS and free cholesterol.
Thickening and loss of elasticity of the walls of ARTERIES of all sizes. There are many forms classified by the types of lesions and arteries involved, such as ATHEROSCLEROSIS with fatty lesions in the ARTERIAL INTIMA of medium and large muscular arteries.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
An enzyme secreted from the liver into the plasma of many mammalian species. It catalyzes the esterification of the hydroxyl group of lipoprotein cholesterol by the transfer of a fatty acid from the C-2 position of lecithin. In familial lecithin:cholesterol acyltransferase deficiency disease, the absence of the enzyme results in an excess of unesterified cholesterol in plasma. EC 2.3.1.43.

Reversal of hyperlipidaemia in apolipoprotein C1 transgenic mice by adenovirus-mediated gene delivery of the low-density-lipoprotein receptor, but not by the very-low-density-lipoprotein receptor. (1/107)

We have shown previously that human apolipoprotein (apo)C1 transgenic mice exhibit hyperlipidaemia, due primarily to an impaired clearance of very-low-density lipoprotein (VLDL) particles from the circulation. In the absence of at least the low-density-lipoprotein receptor (LDLR), it was shown that APOC1 overexpression in transgenic mice inhibited the hepatic uptake of VLDL via the LDLR-related protein. In the present study, we have now examined the effect of apoC1 on the binding of lipoproteins to both the VLDL receptor (VLDLR) and the LDLR. The binding specificity of the VLDLR and LDLR for apoC1-enriched lipoprotein particles was examined in vivo through adenovirus-mediated gene transfer of the VLDLR and the LDLR [giving rise to adenovirus-containing (Ad)-VLDLR and Ad-LDLR respectively] in APOC1 transgenic mice, LDLR-deficient (LDLR-/-) mice and wild-type mice. Remarkably, Ad-VLDLR treatment did not reduce hyperlipidaemia in transgenic mice overexpressing human APOC1, irrespective of both the level of transgenic expression and the presence of the LDLR, whereas Ad-VLDLR treatment did reverse hyperlipidaemia in LDLR-/- and wild-type mice. On the other hand, Ad-LDLR treatment strongly decreased plasma lipid levels in these APOC1 transgenic mice. These results suggest that apoC1 inhibits the clearance of lipoprotein particles via the VLDLR, but not via the LDLR. This hypothesis is corroborated by in vitro binding studies. Chinese hamster ovary (CHO) cells expressing the VLDLR (CHO-VLDLR) or LDLR (CHO-LDLR) bound less APOC1 transgenic VLDL than wild-type VLDL. Intriguingly, however, enrichment with apoE enhanced dose-dependently the binding of wild-type VLDL to CHO-VLDLR cells (up to 5-fold), whereas apoE did not enhance the binding of APOC1 transgenic VLDL to these cells. In contrast, for binding to CHO-LDLR cells, both wild-type and APOC1 transgenic VLDL were stimulated upon enrichment with apoE. From these studies, we conclude that apoC1 specifically inhibits the apoE-mediated binding of triacylglycerol-rich lipoprotein particles to the VLDLR, whereas apoC1-enriched lipoproteins can still bind to the LDLR. The variability in specificity of these lipoprotein receptors for apoC1-containing lipoprotein particles provides further evidence for a regulatory role of apoC1 in the delivery of lipoprotein constituents to different tissues on which these receptors are located.  (+info)

Mass spectral study of polymorphism of the apolipoproteins of very low density lipoprotein. (2/107)

New isoforms of apolipoprotein (apo)C-I and apoC-III have been detected in delipidated fractions from very low density lipoprotein (VLDL) using matrix-assisted laser desorption (MALDI) and electrospray ionization (ESI) mass spectrometry (MS). The cleavage sites of truncated apoC-III isoforms have also been identified. The VLDL fractions were isolated by fixed-angle single-spin ultracentrifugation using a self-generating sucrose density gradient and delipidated using a newly developed C18 solid phase extraction protocol. Fifteen apoC isoforms and apoE were identified in the MALDI spectra and the existence of the more abundant species was verified by ESI-MS. The relative intensities of the apoCs are closely correlated in three normolipidemic subjects. A fourth subject with type V hyperlipidemia exhibited an elevated apoC-III level and a suppressed level of the newly discovered truncated apoC-I isoform. ApoC-II was found to be particularly sensitive to in vitro oxidation. The dynamic range and specificity of the MALDI assay shows that the complete apoC isoform profile and apoE phenotype can be obtained in a single measurement from the delipidated VLDL fraction.  (+info)

Protective effect of apolipoprotein A I, A II, C I and C II on endothelial cells injury induced by low density lipoprotein. (3/107)

OBJECTIVE: To investigate the protective effect of apo-lipoprotein (apo) A I, A II, C I and C II, the main proteins in high density lipoprotein (HDL), on the morphology and function of human umbilical vein endothelial cells injured with low density lipoprotein (LDL) in vitro. METHODS: Cultured human endothelial cells derived from umbilical veins were exposed to LDL, HDL, and apoA I, A II, C I and C II. The morphology of endothelial cells was examined with phase contrast and transmission electron microscope. The released amount of lactate dehydrogenase (LDH) and 6-keto-prostaglandin F1 alpha (PGF1 alpha) was also measured. RESULTS: Endothelial cells after being injured by LDL showed cell contraction, increased release of LDH and decreased secrection of prostacyclin (PGI2). However, the addition of HDL, and apoA I, A II, C I and C II before incubation with LDL inhibited the cellular injury induced by LDL as demonstrated by lowered LDH release, increased level of PGF1 alpha and prevention of morphological changes. CONCLUSION: The results indicate that apoA I, A II, C I and C II, as well as HDL, may play an important role in combating atherogenesis by protecting endothelial cells from damages induced by LDL.  (+info)

Probing the conformation of a human apolipoprotein C-1 by amino acid substitutions and trimethylamine-N-oxide. (4/107)

To test, at the level of individual amino acids, the conformation of an exchangeable apolipoprotein in aqueous solution and in the presence of an osmolyte trimethylamine-N-oxide (TMAO), six synthetic peptide analogues of human apolipoprotein C-1 (apoC-1, 57 residues) containing point mutations in the predicted alpha-helical regions were analyzed by circular dichroism (CD). The CD spectra and the melting curves of the monomeric wild-type and plasma apoC-1 in neutral low-salt solutions superimpose, indicating 31 +/- 4% alpha-helical structure at 22 degrees C that melts reversibly with T(m,WT) = 50 +/- 2 degrees C and van't Hoff enthalpy deltaH(v,WT)(Tm) = 18 +/- 2 kcal/mol. G15A substitution leads to an increased alpha-helical content of 42 +/- 4% and an increased T(m,G15A) = 57 +/- 2 degrees C, which corresponds to stabilization by delta deltaG(app) = +0.4 +/- 1.5 kcal/mol. G15P mutant has approximately 20% alpha-helical content at 22 degrees C and unfolds with low cooperativity upon heating to 90 degrees C. R23P and T45P mutants are fully unfolded at 0-90 degrees C. In contrast, Q31P mutation leads to no destabilization or unfolding. Consequently, the R23 and T45 locations are essential for the stability of the cooperative alpha-helical unit in apoC-1 monomer, G15 is peripheral to it, and Q31 is located in a nonhelical linker region. Our results suggest that Pro mutagenesis coupled with CD provides a tool for assigning the secondary structure to protein groups, which should be useful for other self-associating proteins that are not amenable to NMR structural analysis in aqueous solution. TMAO induces a reversible cooperative coil-to-helix transition in apoC-1, with the maximal alpha-helical content reaching 74%. Comparison with the maximal alpha-helical content of 73% observed in lipid-bound apoC-1 suggests that the TMAO-stabilized secondary structure resembles the functional lipid-bound apolipoprotein conformation.  (+info)

Accumulation of apolipoprotein C-I-rich and cholesterol-rich VLDL remnants during exaggerated postprandial triglyceridemia in normolipidemic patients with coronary artery disease. (5/107)

BACKGROUND: Exaggerated postprandial triglyceridemia is common in normolipidemic patients with coronary artery disease (CAD). Alterations in the composition of triglyceride-rich lipoproteins (TRLs) are likely to underlie this metabolic disturbance. However, the composition of very-low-density lipoproteins (VLDLs), which are the most abundant postprandial TRLs, has never been defined in CAD patients. METHODS AND RESULTS: We examined postprandial changes in the number and composition of VLDLs in middle-aged, normolipidemic CAD patients and control subjects. TRLs from 14 patients and 14 control subjects aged 45 to 55 years were subfractionated by density gradient ultracentrifugation into Svedberg flotation rate (Sf) fractions >400, 60 to 400, and 20 to 60. The VLDLs were separated from chylomicron remnants by immunoaffinity chromatography. In CAD patients, the postprandial concentrations of triglycerides and large (Sf 60 to 400) VLDL particles were elevated. In addition, their postprandial large VLDLs were enriched in apolipoprotein (apo) C-I and their postprandial small (Sf 20 to 60) VLDL remnants were enriched with apo C-I and cholesterol. CONCLUSIONS: Perturbed handling of postprandial triglycerides in normolipidemic CAD patients involves the accumulation of apo C-I-rich large VLDL particles and the generation of small, apo C-I- and cholesterol-rich VLDL remnants.  (+info)

Structural studies of a baboon (Papio sp.) plasma protein inhibitor of cholesteryl ester transferase. (6/107)

A 38-residue protein associated with cholesteryl ester transfer inhibition has been identified in baboons (Papio sp.). The cholesteryl ester transfer inhibitor protein (CETIP) corresponds to the N-terminus of baboon apoC-I. Relative to CETIP, baboon apoC-I is a weak inhibitor of baboon cholesteryl ester transferase (CET). To study the structural features responsible for CET inhibition, CETIP was synthesized by solid-phase methods. Using sodium dodecyl sulfate (SDS) to model the lipoprotein environment, the solution structure of CETIP was probed by optical and 1H NMR spectroscopy. Circular dichroism data show that the protein lacks a well-defined structure in water but, upon the addition of SDS, becomes helical (56%). A small blue shift of 8 nm was observed in the intrinsic tryptophan fluorescence of CETIP in the presence of saturating amounts of SDS, suggesting that tryptophan-23 is not buried deeply in the lipid environment. The helical nature of CETIP in the presence of SDS was confirmed by upfield 1Halpha secondary shifts and an average solution structure determined by distance geometry/simulated annealing calculations using 476 NOE-based distance restraints. The backbone (N-Calpha-C=O) root-mean-square deviation of an ensemble of 17 out of 25 calculated structures superimposed on the average structure was 1.06+0.30 A using residues V4-P35 and 0.51+/-0.17 A using residues A7-S32. Although the side-chain orientations fit the basic description of a class A amphipathic helix, both intramolecular salt bridge formation and "snorkeling" of basic side chains toward the polar face play minor, if any, roles in stabilizing the lipid-bound amphipathic structure. Conformational features of the calculated structures for CETIP are discussed relative to models of CETIP inhibition of cholesteryl ester transferase.  (+info)

Human apolipoprotein C-I accounts for the ability of plasma high density lipoproteins to inhibit the cholesteryl ester transfer protein activity. (7/107)

The aim of the present study was to identify the protein that accounts for the cholesteryl ester transfer protein (CETP)-inhibitory activity that is specifically associated with human plasma high density lipoproteins (HDL). To this end, human HDL apolipoproteins were fractionated by preparative polyacrylamide gradient gel electrophoresis, and 30 distinct protein fractions with molecular masses ranging from 80 down to 2 kDa were tested for their ability to inhibit CETP activity. One single apolipoprotein fraction was able to completely inhibit CETP activity. The N-terminal sequence of the 6-kDa protein inhibitor matched the N-terminal sequence of human apoC-I, the inhibition was completely blocked by specific anti-apolipoprotein C-I antibodies, and mass spectrometry analysis confirmed the identity of the isolated inhibitor with full-length human apoC-I. Pure apoC-I was able to abolish CETP activity in a concentration-dependent manner and with a high efficiency (IC(50) = 100 nmol/liter). The inhibitory potency of total delipidated HDL apolipoproteins completely disappeared after a treatment with anti-apolipoprotein C-I antibodies, and the apoC-I deprivation of native plasma HDL by immunoaffinity chromatography produced a mean 43% rise in cholesteryl ester transfer rates. The main localization of apoC-I in HDL and not in low density lipoprotein in normolipidemic plasma provides further support for the specific property of HDL in inhibiting CETP activity.  (+info)

Long terminal repeats are used as alternative promoters for the endothelin B receptor and apolipoprotein C-I genes in humans. (8/107)

To examine the potential regulatory involvement of retroelements in the human genome, we screened the transcribed sequences of GenBank and expressed sequence tag data bases with long terminal repeat (LTR) elements derived from different human endogenous retroviruses. These screenings detected human transcripts containing LTRs belonging to the human endogenous retrovirus-E family fused to the apolipoprotein CI (apoC-I) and the endothelin B receptor (EBR) genes. However, both genes are known to have non-LTR (native) promoters. Initial reverse transcription-polymerase chain reaction experiments confirmed and authenticated the presence of transcripts from both the native and LTR promoters. Using a 5'-rapid amplification of cDNA ends protocol, we showed that the alternative transcripts of apoC-I and EBR are initiated and promoted by the LTRs. The LTR-apoC-I fusion and native apoC-I transcripts are present in many of the tissues tested. As expected, we found apoC-I preferentially expressed in liver, where about 15% of the transcripts are derived from the LTR promoter. Transient transfections suggest that the expression is not dependent on the LTR itself, but the presence of the LTR increases activity of the apoC-I promoter from both humans and baboons. The native EBR-driven transcripts were also detected in many tissues, whereas the LTR-driven transcripts appear limited to placenta. In contrast to the LTR of apoC-I, the EBR LTR promotes a significant proportion of the total EBR transcripts, and transient transfection results indicate that the LTR acts as a strong promoter and enhancer in a placental cell line. This investigation reports two examples where LTR sequences contribute to increased transcription of human genes and illustrates the impact of mobile elements on gene and genome evolution.  (+info)

Apolipoprotein C-I (apoC-I) is a small protein component of lipoproteins, which are particles that transport all fat molecules (lipids), including cholesterol, in the bloodstream. ApoC-I is primarily produced in the liver and intestines and plays a crucial role in the metabolism of triglyceride-rich lipoproteins, such as very low-density lipoproteins (VLDL) and chylomicrons.

Apolipoprotein C-I has several functions:

1. Inhibition of lipoprotein lipase (LPL): ApoC-I inhibits the activity of LPL, an enzyme responsible for breaking down triglycerides in lipoproteins. This inhibition helps regulate the rate at which fatty acids are released from triglyceride-rich lipoproteins and taken up by cells for energy production or storage.
2. Activation of hepatic lipase (HL): ApoC-I activates HL, an enzyme involved in the catabolism of intermediate-density lipoproteins (IDL) and high-density lipoproteins (HDL). This activation aids in the clearance of these particles from the circulation.
3. Regulation of cholesterol efflux: ApoC-I may also play a role in regulating cholesterol efflux, the process by which excess cholesterol is removed from cells and transported to the liver for excretion.

Genetic variations in the APOC1 gene, which encodes apoC-I, have been associated with alterations in lipid metabolism and an increased risk of cardiovascular disease.

Apolipoprotein C (apoC) is a group of proteins that are associated with lipoproteins, which are complex particles composed of lipids and proteins that play a crucial role in the transport and metabolism of lipids in the body. There are three main types of apoC proteins: apoC-I, apoC-II, and apoC-III.

ApoC-I is involved in the regulation of lipoprotein metabolism and has been shown to inhibit the activity of cholesteryl ester transfer protein (CETP), which is an enzyme that facilitates the transfer of cholesteryl esters from high-density lipoproteins (HDL) to low-density lipoproteins (LDL) and very low-density lipoproteins (VLDL).

ApoC-II is a cofactor for lipoprotein lipase, an enzyme that hydrolyzes triglycerides in chylomicrons and VLDL, leading to the formation of smaller, denser lipoproteins. A deficiency in apoC-II can lead to hypertriglyceridemia, a condition characterized by elevated levels of triglycerides in the blood.

ApoC-III is also involved in the regulation of lipoprotein metabolism and has been shown to inhibit the activity of lipoprotein lipase and CETP. Elevated levels of apoC-III have been associated with an increased risk of cardiovascular disease, possibly due to its effects on lipoprotein metabolism.

In summary, apolipoprotein C is a group of proteins that are involved in the regulation of lipoprotein metabolism and have important roles in the transport and metabolism of lipids in the body.

Apolipoprotein C-III (APOC3) is a protein that is produced in the liver and circulates in the bloodstream. It is a component of certain lipoproteins, including very low-density lipoproteins (VLDL) and chylomicrons, which are responsible for transporting fat molecules, such as triglycerides and cholesterol, throughout the body.

APOC3 plays a role in regulating the metabolism of these lipoproteins. Specifically, it inhibits the activity of an enzyme called lipoprotein lipase, which breaks down triglycerides in VLDL and chylomicrons. As a result, high levels of APOC3 can lead to an increase in triglyceride levels in the blood, which is a risk factor for cardiovascular disease.

Genetic variations in the APOC3 gene have been associated with differences in triglyceride levels and risk of cardiovascular disease. Some studies have suggested that reducing APOC3 levels through genetic editing or other means may be a promising strategy for lowering triglycerides and reducing the risk of heart disease.

VLDL (Very Low-Density Lipoproteins) are a type of lipoprotein that play a crucial role in the transport and metabolism of fat molecules, known as triglycerides, in the body. They are produced by the liver and consist of a core of triglycerides surrounded by a shell of proteins called apolipoproteins, phospholipids, and cholesterol.

VLDL particles are responsible for delivering fat molecules from the liver to peripheral tissues throughout the body, where they can be used as an energy source or stored for later use. During this process, VLDL particles lose triglycerides and acquire more cholesterol, transforming into intermediate-density lipoproteins (IDL) and eventually low-density lipoproteins (LDL), which are also known as "bad" cholesterol.

Elevated levels of VLDL in the blood can contribute to the development of cardiovascular disease due to their association with increased levels of triglycerides and LDL cholesterol, as well as decreased levels of high-density lipoproteins (HDL), which are considered "good" cholesterol.

Triglycerides are the most common type of fat in the body, and they're found in the food we eat. They're carried in the bloodstream to provide energy to the cells in our body. High levels of triglycerides in the blood can increase the risk of heart disease, especially in combination with other risk factors such as high LDL (bad) cholesterol, low HDL (good) cholesterol, and high blood pressure.

It's important to note that while triglycerides are a type of fat, they should not be confused with cholesterol, which is a waxy substance found in the cells of our body. Both triglycerides and cholesterol are important for maintaining good health, but high levels of either can increase the risk of heart disease.

Triglyceride levels are measured through a blood test called a lipid panel or lipid profile. A normal triglyceride level is less than 150 mg/dL. Borderline-high levels range from 150 to 199 mg/dL, high levels range from 200 to 499 mg/dL, and very high levels are 500 mg/dL or higher.

Elevated triglycerides can be caused by various factors such as obesity, physical inactivity, excessive alcohol consumption, smoking, and certain medical conditions like diabetes, hypothyroidism, and kidney disease. Medications such as beta-blockers, steroids, and diuretics can also raise triglyceride levels.

Lifestyle changes such as losing weight, exercising regularly, eating a healthy diet low in saturated and trans fats, avoiding excessive alcohol consumption, and quitting smoking can help lower triglyceride levels. In some cases, medication may be necessary to reduce triglycerides to recommended levels.

Apolipoprotein A-I (ApoA-I) is a major protein component of high-density lipoproteins (HDL) in human plasma. It plays a crucial role in the metabolism and transport of lipids, particularly cholesterol, within the body. ApoA-I facilitates the formation of HDL particles, which are involved in the reverse transport of cholesterol from peripheral tissues to the liver for excretion. This process is known as reverse cholesterol transport and helps maintain appropriate cholesterol levels in the body. Low levels of ApoA-I or dysfunctional ApoA-I have been associated with an increased risk of developing cardiovascular diseases.

'NK Cell Lectin-Like Receptor Subfamily A' refers to a group of activating receptors expressed on natural killer (NK) cells, which are a type of immune cell. These receptors are named for their similarity in structure to lectins, which are proteins that bind to carbohydrates.

The NK Cell Lectin-Like Receptor Subfamily A includes several different receptors, such as NKp46, NKp44, and NKp30, that play important roles in the immune response. These receptors recognize specific molecules on the surface of infected or damaged cells, triggering the activation of NK cells and the release of cytotoxic substances that can kill the target cells.

The activation of NK cells through these receptors helps to control infections and prevent the development of cancer. However, abnormal activation of NK cells can also contribute to autoimmune diseases and other conditions. Therefore, understanding the function of NK Cell Lectin-Like Receptor Subfamily A members is important for developing new therapies and treatments for a variety of diseases.

NK cell lectin-like receptors are a type of receptor found on natural killer (NK) cells, which are a type of immune cell that plays a role in the body's defense against viruses and cancer. These receptors are characterized by their ability to bind to specific carbohydrate structures on the surface of infected or abnormal cells.

The lectin-like receptors include several different types, such as the natural cytotoxicity receptors (NCRs), the C-type lectin-like receptors (CLRs), and the immunoglobulin-like transcript (ILT) receptors. These receptors recognize and bind to specific ligands on the surface of target cells, which can trigger NK cell activation and the release of cytotoxic granules that kill the target cell.

The lectin-like receptors play an important role in NK cell function and regulation, and dysregulation of these receptors has been implicated in various diseases, including cancer and autoimmune disorders.

Apolipoprotein E (ApoE) is a protein involved in the metabolism of lipids, particularly cholesterol. It is produced primarily by the liver and is a component of several types of lipoproteins, including very low-density lipoproteins (VLDL) and high-density lipoproteins (HDL).

ApoE plays a crucial role in the transport and uptake of lipids in the body. It binds to specific receptors on cell surfaces, facilitating the delivery of lipids to cells for energy metabolism or storage. ApoE also helps to clear cholesterol from the bloodstream and is involved in the repair and maintenance of tissues.

There are three major isoforms of ApoE, designated ApoE2, ApoE3, and ApoE4, which differ from each other by only a few amino acids. These genetic variations can have significant effects on an individual's risk for developing certain diseases, particularly cardiovascular disease and Alzheimer's disease. For example, individuals who inherit the ApoE4 allele have an increased risk of developing Alzheimer's disease, while those with the ApoE2 allele may have a reduced risk.

In summary, Apolipoprotein E is a protein involved in lipid metabolism and transport, and genetic variations in this protein can influence an individual's risk for certain diseases.

Apolipoprotein B-100 (apoB-100) is a large protein component of low-density lipoprotein (LDL), also known as "bad cholesterol." It plays a crucial role in the metabolism and transport of fats and cholesterol in the body. ApoB-100 is responsible for the binding of LDL to specific receptors on cell surfaces, facilitating the uptake of lipoprotein particles by cells. Elevated levels of apoB-100 in the blood are associated with an increased risk of developing cardiovascular diseases, such as atherosclerosis and coronary artery disease.

I'm assuming you are asking for information about "Ly" antigens in the context of human immune system and immunology.

Ly (Lymphocyte) antigens are a group of cell surface markers found on human leukocytes, including T cells, NK cells, and some B cells. These antigens were originally identified through serological analysis and were historically used to distinguish different subsets of lymphocytes based on their surface phenotype.

The "Ly" nomenclature has been largely replaced by the CD (Cluster of Differentiation) system, which is a more standardized and internationally recognized classification system for cell surface markers. However, some Ly antigens are still commonly referred to by their historical names, such as:

* Ly-1 or CD5: A marker found on mature T cells, including both CD4+ and CD8+ subsets.
* Ly-2 or CD8: A marker found on cytotoxic T cells, which are a subset of CD8+ T cells that can directly kill infected or damaged cells.
* Ly-3 or CD56: A marker found on natural killer (NK) cells, which are a type of immune cell that can recognize and destroy virus-infected or cancerous cells without the need for prior activation.

It's worth noting that while these antigens were originally identified through serological analysis, they are now more commonly detected using flow cytometry, which allows for the simultaneous measurement of multiple surface markers on individual cells. This has greatly expanded our ability to identify and characterize different subsets of immune cells and has led to a better understanding of their roles in health and disease.

Apolipoprotein B (ApoB) is a type of protein that plays a crucial role in the metabolism of lipids, particularly low-density lipoprotein (LDL) or "bad" cholesterol. ApoB is a component of LDL particles and serves as a ligand for the LDL receptor, which is responsible for the clearance of LDL from the bloodstream.

There are two main forms of ApoB: ApoB-100 and ApoB-48. ApoB-100 is found in LDL particles, very low-density lipoprotein (VLDL) particles, and chylomicrons, while ApoB-48 is only found in chylomicrons, which are produced in the intestines and responsible for transporting dietary lipids.

Elevated levels of ApoB are associated with an increased risk of cardiovascular disease (CVD), as they indicate a higher concentration of LDL particles in the bloodstream. Therefore, measuring ApoB levels can provide additional information about CVD risk beyond traditional lipid profile tests that only measure total cholesterol, LDL cholesterol, HDL cholesterol, and triglycerides.

Apolipoprotein E (APOE) is a gene that provides instructions for making a protein involved in the metabolism of fats called lipids. One variant of this gene, APOE4, is associated with an increased risk of developing Alzheimer's disease and other forms of dementia.

The APOE4 allele (variant) is less efficient at clearing beta-amyloid protein, a component of the amyloid plaques found in the brains of people with Alzheimer's disease. This can lead to an accumulation of beta-amyloid and an increased risk of developing Alzheimer's disease.

It is important to note that having one or two copies of the APOE4 allele does not mean that a person will definitely develop Alzheimer's disease, but it does increase the risk. Other factors, such as age, family history, and the presence of other genetic variants, also contribute to the development of this complex disorder.

Apolipoprotein E3 (ApoE3) is one of the three major isoforms of apolipoprotein E (ApoE), a protein involved in the metabolism of lipids, particularly cholesterol. ApoE is produced by the APOE gene, which has three common alleles: ε2, ε3, and ε4. These alleles result in three main isoforms of the protein: ApoE2, ApoE3, and ApoE4.

ApoE3 is the most common isoform, found in approximately 77-78% of the population. It has a slightly different amino acid sequence compared to ApoE2 and ApoE4, which can affect its function. ApoE3 is thought to play a neutral or protective role in the risk of developing Alzheimer's disease and cardiovascular diseases, although some studies suggest that it may have a mildly favorable effect on lipid metabolism compared to ApoE4.

Apolipoprotein A-II (ApoA-II) is a protein component of high-density lipoproteins (HDL), often referred to as "good cholesterol." It is one of the major apolipoproteins in HDL and plays a role in the structure, metabolism, and function of HDL particles. ApoA-II is produced primarily in the liver and intestine and helps facilitate the transport of cholesterol from tissues to the liver for excretion. Additionally, ApoA-II has been shown to have anti-inflammatory properties and may play a role in the regulation of the immune response.

Apolipoproteins are a group of proteins that are associated with lipids (fats) in the body and play a crucial role in the metabolism, transportation, and regulation of lipids. They are structural components of lipoprotein particles, which are complexes of lipids and proteins that transport lipids in the bloodstream.

There are several types of apolipoproteins, including ApoA, ApoB, ApoC, ApoD, ApoE, and others. Each type has a specific function in lipid metabolism. For example, ApoA is a major component of high-density lipoprotein (HDL), often referred to as "good cholesterol," and helps remove excess cholesterol from cells and tissues and transport it to the liver for excretion. ApoB, on the other hand, is a major component of low-density lipoprotein (LDL), or "bad cholesterol," and plays a role in the delivery of cholesterol to cells and tissues.

Abnormal levels of apolipoproteins or dysfunctional forms of these proteins have been linked to various diseases, including cardiovascular disease, Alzheimer's disease, and metabolic disorders such as diabetes. Therefore, measuring apolipoprotein levels in the blood can provide valuable information for diagnosing and monitoring these conditions.

Apolipoprotein C-II (ApoC-II) is a type of apolipoprotein, which are proteins that bind to lipids to form lipoprotein complexes. ApoC-II is a component of several lipoproteins, including very low-density lipoproteins (VLDL) and chylomicrons, which are responsible for the transport of fat molecules, such as triglycerides and cholesterol, in the bloodstream.

ApoC-II plays a crucial role in the activation of lipoprotein lipase, an enzyme that breaks down triglycerides in VLDL and chylomicrons into fatty acids, which can then be taken up by cells for energy production or storage. Therefore, ApoC-II deficiency can lead to hypertriglyceridemia, a condition characterized by high levels of triglycerides in the blood.

In addition to its role in lipid metabolism, ApoC-II has been implicated in the development and progression of atherosclerosis, a chronic inflammatory disease that affects the arteries and can lead to serious cardiovascular complications, such as heart attack and stroke.

Apolipoprotein A (apoA) is a type of apolipoprotein that is primarily associated with high-density lipoproteins (HDL), often referred to as "good cholesterol." There are several subtypes of apoA, including apoA-I, apoA-II, and apoA-IV.

ApoA-I is the major protein component of HDL particles and plays a crucial role in reverse cholesterol transport, which is the process by which excess cholesterol is removed from tissues and delivered to the liver for excretion. Low levels of apoA-I have been linked to an increased risk of cardiovascular disease.

ApoA-II is another protein component of HDL particles, although its function is less well understood than that of apoA-I. Some studies suggest that apoA-II may play a role in regulating the metabolism of HDL particles.

ApoA-IV is found in both HDL and chylomicrons, which are lipoprotein particles that transport dietary lipids from the intestine to the liver. The function of apoA-IV is not well understood, but it may play a role in regulating appetite and energy metabolism.

Overall, apolipoproteins A are important components of HDL particles and play a critical role in maintaining healthy lipid metabolism and reducing the risk of cardiovascular disease.

Apolipoprotein B-48 (apoB-48) is a protein component of chylomicrons, which are lipoprotein particles responsible for carrying dietary fat and cholesterol from the intestines to other parts of the body. ApoB-48 is produced in the intestines and is a shorter version of apolipoprotein B-100 (apoB-100), which is a component of low-density lipoproteins (LDL) or "bad cholesterol."

Chylomicrons are assembled and secreted by intestinal cells after a meal, and apoB-48 is essential for the formation and function of these particles. ApoB-48-containing chylomicrons transport dietary lipids to various tissues, including the liver, where they contribute to the maintenance of lipid homeostasis.

Elevated levels of apoB-48 in the blood have been associated with an increased risk of cardiovascular disease, particularly in individuals with familial chylomicronemia syndrome (FCS), a rare genetic disorder characterized by severely elevated triglyceride levels due to impaired clearance of chylomicrons.

Apolipoprotein E2 (ApoE2) is one of the three major isoforms of the apolipoprotein E (ApoE) protein, which is a component of lipoproteins that are involved in the transport and metabolism of cholesterol and other fats in the body. ApoE is produced by the APOE gene, which has three common alleles: ε2, ε3, and ε4.

The ApoE2 protein is encoded by the ε2 allele of the APOE gene. Compared to the other two isoforms (ApoE3 and ApoE4), ApoE2 has a different amino acid at position 112, where it has a cysteine instead of an arginine. This difference affects the protein's ability to interact with other molecules involved in lipid metabolism, such as the low-density lipoprotein receptor (LDLR).

Individuals who inherit two copies of the ε2 allele (ε2/ε2) have a higher risk of developing type III hyperlipoproteinemia, also known as dysbetalipoproteinemia, which is characterized by elevated levels of cholesterol and triglycerides in the blood due to impaired clearance of remnant lipoproteins. However, not all people with the ε2/ε2 genotype develop type III hyperlipoproteinemia, and other genetic and environmental factors may contribute to the development of this condition.

It's worth noting that having one or two copies of the ε2 allele has been associated with a reduced risk of developing Alzheimer's disease, although the mechanism by which ApoE2 protects against Alzheimer's is not fully understood.

High-Density Lipoproteins (HDL) are a type of lipoprotein that play a crucial role in the transportation and metabolism of cholesterol in the body. They are often referred to as "good" cholesterol because they help remove excess cholesterol from cells and carry it back to the liver, where it can be broken down and removed from the body. This process is known as reverse cholesterol transport.

HDLs are composed of a lipid core containing cholesteryl esters and triglycerides, surrounded by a shell of phospholipids, free cholesterol, and apolipoproteins, primarily apoA-I. The size and composition of HDL particles can vary, leading to the classification of different subclasses of HDL with varying functions and metabolic fates.

Elevated levels of HDL have been associated with a lower risk of developing cardiovascular diseases, while low HDL levels increase the risk. However, it is essential to consider that HDL function and quality may be more important than just the quantity in determining cardiovascular risk.

Cholesterol is a type of lipid (fat) molecule that is an essential component of cell membranes and is also used to make certain hormones and vitamins in the body. It is produced by the liver and is also obtained from animal-derived foods such as meat, dairy products, and eggs.

Cholesterol does not mix with blood, so it is transported through the bloodstream by lipoproteins, which are particles made up of both lipids and proteins. There are two main types of lipoproteins that carry cholesterol: low-density lipoproteins (LDL), also known as "bad" cholesterol, and high-density lipoproteins (HDL), also known as "good" cholesterol.

High levels of LDL cholesterol in the blood can lead to a buildup of cholesterol in the walls of the arteries, increasing the risk of heart disease and stroke. On the other hand, high levels of HDL cholesterol are associated with a lower risk of these conditions because HDL helps remove LDL cholesterol from the bloodstream and transport it back to the liver for disposal.

It is important to maintain healthy levels of cholesterol through a balanced diet, regular exercise, and sometimes medication if necessary. Regular screening is also recommended to monitor cholesterol levels and prevent health complications.

Lipoproteins are complex particles composed of multiple proteins and lipids (fats) that play a crucial role in the transport and metabolism of fat molecules in the body. They consist of an outer shell of phospholipids, free cholesterols, and apolipoproteins, enclosing a core of triglycerides and cholesteryl esters.

There are several types of lipoproteins, including:

1. Chylomicrons: These are the largest lipoproteins and are responsible for transporting dietary lipids from the intestines to other parts of the body.
2. Very-low-density lipoproteins (VLDL): Produced by the liver, VLDL particles carry triglycerides to peripheral tissues for energy storage or use.
3. Low-density lipoproteins (LDL): Often referred to as "bad cholesterol," LDL particles transport cholesterol from the liver to cells throughout the body. High levels of LDL in the blood can lead to plaque buildup in artery walls and increase the risk of heart disease.
4. High-density lipoproteins (HDL): Known as "good cholesterol," HDL particles help remove excess cholesterol from cells and transport it back to the liver for excretion or recycling. Higher levels of HDL are associated with a lower risk of heart disease.

Understanding lipoproteins and their roles in the body is essential for assessing cardiovascular health and managing risks related to heart disease and stroke.

Apolipoprotein D (apoD) is a protein that is associated with high-density lipoprotein (HDL) particles in the blood. It is one of several apolipoproteins that are involved in the transport and metabolism of lipids, such as cholesterol and triglycerides, in the body.

ApoD is produced by the APOD gene and is found in various tissues, including the brain, where it is believed to play a role in protecting nerve cells from oxidative stress. It has also been studied for its potential role in Alzheimer's disease and other neurological disorders.

In addition to its role in lipid metabolism and neuroprotection, apoD has been shown to have anti-inflammatory properties and may be involved in the regulation of immune responses. However, more research is needed to fully understand the functions and mechanisms of action of this protein.

Low-density lipoproteins (LDL), also known as "bad cholesterol," are a type of lipoprotein that carry cholesterol and other fats from the liver to cells throughout the body. High levels of LDL in the blood can lead to the buildup of cholesterol in the walls of the arteries, which can increase the risk of heart disease and stroke.

Lipoproteins are complex particles composed of proteins (apolipoproteins) and lipids (cholesterol, triglycerides, and phospholipids) that are responsible for transporting fat molecules around the body in the bloodstream. LDL is one type of lipoprotein, along with high-density lipoproteins (HDL), very low-density lipoproteins (VLDL), and chylomicrons.

LDL particles are smaller than HDL particles and can easily penetrate the artery walls, leading to the formation of plaques that can narrow or block the arteries. Therefore, maintaining healthy levels of LDL in the blood is essential for preventing cardiovascular disease.

Lipids are a broad group of organic compounds that are insoluble in water but soluble in nonpolar organic solvents. They include fats, waxes, sterols, fat-soluble vitamins (such as vitamins A, D, E, and K), monoglycerides, diglycerides, triglycerides, and phospholipids. Lipids serve many important functions in the body, including energy storage, acting as structural components of cell membranes, and serving as signaling molecules. High levels of certain lipids, particularly cholesterol and triglycerides, in the blood are associated with an increased risk of cardiovascular disease.

LDL receptors (Low-Density Lipoprotein Receptors) are cell surface receptors that play a crucial role in the regulation of cholesterol homeostasis within the body. They are responsible for recognizing and binding to LDL particles, also known as "bad cholesterol," which are then internalized by the cell through endocytosis.

Once inside the cell, the LDL particles are broken down, releasing their cholesterol content, which can be used for various cellular processes such as membrane synthesis and hormone production. The LDL receptors themselves are recycled back to the cell surface, allowing for continued uptake of LDL particles.

Mutations in the LDL receptor gene can lead to a condition called familial hypercholesterolemia, which is characterized by high levels of LDL cholesterol in the blood and an increased risk of premature cardiovascular disease.

Atherosclerosis is a medical condition characterized by the buildup of plaques, made up of fat, cholesterol, calcium, and other substances found in the blood, on the inner walls of the arteries. This process gradually narrows and hardens the arteries, reducing the flow of oxygen-rich blood to various parts of the body. Atherosclerosis can affect any artery in the body, including those that supply blood to the heart (coronary arteries), brain, limbs, and other organs. The progressive narrowing and hardening of the arteries can lead to serious complications such as coronary artery disease, carotid artery disease, peripheral artery disease, and aneurysms, which can result in heart attacks, strokes, or even death if left untreated.

The exact cause of atherosclerosis is not fully understood, but it is believed to be associated with several risk factors, including high blood pressure, high cholesterol levels, smoking, diabetes, obesity, physical inactivity, and a family history of the condition. Atherosclerosis can often progress without any symptoms for many years, but as the disease advances, it can lead to various signs and symptoms depending on which arteries are affected. Treatment typically involves lifestyle changes, medications, and, in some cases, surgical procedures to restore blood flow.

HDL (High-Density Lipoprotein) cholesterol is often referred to as "good" cholesterol. It is a type of lipoprotein that helps remove excess cholesterol from cells and carry it back to the liver, where it can be broken down and removed from the body. High levels of HDL cholesterol have been associated with a lower risk of heart disease and stroke.

Arteriosclerosis is a general term that describes the hardening and stiffening of the artery walls. It's a progressive condition that can occur as a result of aging, or it may be associated with certain risk factors such as high blood pressure, high cholesterol, diabetes, smoking, and a sedentary lifestyle.

The process of arteriosclerosis involves the buildup of plaque, made up of fat, cholesterol, calcium, and other substances, in the inner lining of the artery walls. Over time, this buildup can cause the artery walls to thicken and harden, reducing the flow of oxygen-rich blood to the body's organs and tissues.

Arteriosclerosis can affect any of the body's arteries, but it is most commonly found in the coronary arteries that supply blood to the heart, the cerebral arteries that supply blood to the brain, and the peripheral arteries that supply blood to the limbs. When arteriosclerosis affects the coronary arteries, it can lead to heart disease, angina, or heart attack. When it affects the cerebral arteries, it can lead to stroke or transient ischemic attack (TIA). When it affects the peripheral arteries, it can cause pain, numbness, or weakness in the limbs, and in severe cases, gangrene and amputation.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Phosphatidylcholine-Sterol O-Acyltransferase (PCOAT, also known as Sterol O-Acyltransferase 1 or SOAT1) is an enzyme that plays a crucial role in the regulation of cholesterol metabolism. It is located in the endoplasmic reticulum and is responsible for the transfer of acyl groups from phosphatidylcholine to cholesterol, forming cholesteryl esters. This enzymatic reaction results in the storage of excess cholesterol in lipid droplets, preventing its accumulation in the cell membrane and potentially contributing to the development of atherosclerosis if not properly regulated.

Defects or mutations in PCOAT can lead to disruptions in cholesterol homeostasis, which may contribute to various diseases such as cardiovascular disorders, metabolic syndrome, and neurodegenerative conditions. Therefore, understanding the function and regulation of this enzyme is essential for developing therapeutic strategies aimed at managing cholesterol-related disorders.

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Apolipoprotein B100 (apoB100) is a protein that plays a role in moving cholesterol around your body. It is a form of low ... Apolipoprotein B100 (apoB100) is a protein that plays a role in moving cholesterol around your body. It is a form of low ... Apolipoprotein B100 (apoB100) is a protein that plays a role in moving cholesterol around your body. It is a form of low ... Apolipoprotein measurements may provide more detail about your risk for heart disease, but the added value of this test beyond ...
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LBXAPB - Apolipoprotein (B) (mg/dL). Variable Name: LBXAPB. SAS Label: Apolipoprotein (B) (mg/dL). English Text: Apolipoprotein ... LBDAPBSI - Apolipoprotein (B) (g/L). Variable Name: LBDAPBSI. SAS Label: Apolipoprotein (B) (g/L). English Text: Apolipoprotein ... Apolipoprotein B (ApoB_G) Data File: ApoB_G.xpt First Published: January 2014. Last Revised: NA ... Apolipoprotein B is the main protein component of LDL and accounts for approximately 95% of the total protein content of LDL. ...
Macrophage-derived apolipoprotein (apo) E and multimers of a synthetic apo E-peptide display monokine-like functions by ...
Beta apolipoproteins. Beta apolipoproteins are the largest of the apolipoproteins. They are critically important for the ... Apolipoprotein B-100 deficiency. Intestinal steatosis despite apolipoprotein B-48 synthesis. J Clin Invest. 1985 Aug. 76(2):403 ... CMs, VLDL, and LDL carry apolipoproteins on their surface; these apolipoproteins have lipid-soluble segments, the beta ... The 2 beta apolipoproteins are B-100 and B-48. ApoB-100 is carried on VLDL and the lipoproteins derived from its metabolism, ...
Apolipoprotein E4 (apoE4), the major genetic risk factor of Alzheimers disease (AD), is associated with enhanced brain ... Apolipoprotein E4 enhances brain inflammation by modulation of the NF-kappaB signaling cascade Neurobiol Dis. 2005 Dec;20(3): ... Apolipoprotein E4 (apoE4), the major genetic risk factor of Alzheimers disease (AD), is associated with enhanced brain ...
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Apolipoprotein E (APOE) is a lipid-transport protein abundantly expressed in most neurons in the central nervous system. APOE- ... Role of apolipoprotein E in neurodegenerative diseases Vo Van Giau,1 Eva Bagyinszky,1 Seong Soo A An,1 SangYun Kim2 1Department ... Effect of apolipoprotein E variants on plasma lipids and apolipoproteins in the Orang Asli (Aborigines) of Malaysia. Hum ... Apolipoprotein E2-Dunedin (228 Arg replaced by Cys): an apolipoprotein E2 variant with normal receptor-binding activity. J ...
Apolipoprotein E4 Reduction with Antisense Oligonucleotides Decreases Neurodegeneration in a Tauopathy Model. Ann Neurol. 2021 ...
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Bioss Anti-Apolipoprotein E Polyclonal, Catalog # BS-4892R. Tested in Western Blot (WB), Immunocytochemistry (ICC/IF), ... Protein Aliases: Apo-E; ApoE4; Apolipoprotein; Apolipoprotein E; apolipoprotein E3; apolipoprotein E4; Apoprotein; B2G1; BG; ... Cite Apolipoprotein E Polyclonal Antibody. The following product was used in this experiment: Apolipoprotein E Polyclonal ... Apo E (Apolipoprotein E) plays an important role in the metabolism of lipids in the plasma, and is also is a constituent of ...
... *Authors: *Tomohiro Aoki ... Aoki T, Moriwaki T, Takagi Y, Kataoka H, Yang J, Nozaki K and Hashimoto N: The efficacy of apolipoprotein E deficiency in ... Aoki, T., Moriwaki, T., Takagi, Y., Kataoka, H., Yang, J., Nozaki, K., & Hashimoto, N. (2008). The efficacy of apolipoprotein E ... Aoki, T., Moriwaki, T., Takagi, Y., Kataoka, H., Yang, J., Nozaki, K., Hashimoto, N.The efficacy of apolipoprotein E ...
View Mouse/Rat Apolipoprotein H/ApoH Antibody (AF6575) datasheet. ... Background: Apolipoprotein H/ApoH. Apolipoprotein H (ApoH), also known as beta 2‑Glycoprotein I/ beta 2-GPI, is a variably ... Detects mouse and rat Apolipoprotein H/ApoH in Western blots and detects recombinant mouse Apolipoprotein H/ApoH in direct ... Reviews for Mouse/Rat Apolipoprotein H/ApoH Antibody. There are currently no reviews for this product. Be the first to review ...
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Background: The apolipoprotein E (ApoE) polymorphism has been well studied in the adult human population, in part because the ...
Apolipoprotein E genotyping in Alzheimers disease and frontotemporal dementia. *Mark. Gustafson, Lars LU ; Abrahamson, Magnus ... Apolipoprotein E, Isoforms, Alzheimers disease, Frontotemporal dementia. in Dementia and Geriatric Cognitive Disorders. volume ... Apolipoprotein E; Isoforms; Alzheimers disease; Frontotemporal dementia}}, language = {{eng}}, number = {{4}}, pages = {{240-- ... 243}}, publisher = {{Karger}}, series = {{Dementia and Geriatric Cognitive Disorders}}, title = {{Apolipoprotein E genotyping ...
Erratum - Association between Apolipoprotein E Polymorphism and Clinical Outcome after Ischemic Stroke, Intracerebral ... Erratum - Association between Apolipoprotein E Polymorphism and Clinical Outcome after Ischemic Stroke, Intracerebral ... This is an erratum to: Association between Apolipoprotein E Polymorphism and Clinical Outcome after Ischemic Stroke, ... In the article "Association between Apolipoprotein E Polymorphism and Clinical Outcome after Ischemic Stroke, Intracerebral ...

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