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| 1 | No image | b-lipoprotein |
low density lipoprotein |
TLP1001 | Kazuo Kondo |
LDL |
Definition LDL is defined as the lipoprotein fraction with the density range of 1.019 to 1.063 g/ml.(Ref. 1001) |
1.019-1.063 g/ml |
Physical properties Particle weight 2.5  106 , Diameter(nm) 19-25 Relative weight Composition (%) Protein 20-25 Phospholipid 20-25 Free cholesterol 6-10 Cholesteryl ester 35-45 Triglyceride6-12 Apolipoproteincontribution (%) apo B 90-95 apo C Trace apo E Trace(Ref. 1006) |
LDL in Agarose Gel Electrophoresis In agarose gel electrophoresis LDL migrates at the same position as b-globulins, thus LDL is designated b-lipoprotein. Fig.1 through 4: Electrophorograms above electrophoretic patterns of anodically migrating lipoprotein fractions. Fig.1: Red 7B stained lipoproteins. Fig.2: Formazan dye developed cholesterol fractions. Fig.3: Formazan dye developed triglyceride fractions Fig.4: Fig.2 and Fig.3 superimporsed. Demonstrate relative positions and enabling ratio assessment of all triglyceride and choresterol fractions, including Lp(a), Lipo X, slowa, IDL, and b-VLDL. [Chromatogram 1001] |
Structure and Composition of LDL LDL is a spherical particle and in normal individuals ranges 20.0 to 23.0 nm in diameter. The average molecular weight is 2.3 106. Compared with other lipoproteins, LDL particles are relatively homogeneous in size and composition, however, LDL particles can be separated into several subfractions of increasing density and decreasing size. LDL consists of protein (20-25%), phospolipid (20-25%), free cholesterol (6-10% ), cholesterol ester (35-45%) and triglyceride (6-12%). Apo B-100 is the sole constituent apolipoprotein on LDL. It is presumed that the cholesteryl esters and triglycerides form the hydrophobic core, which is surrounded by a surface coat of apolipoprotein B, free cholesterol and polar phospholipid components oriented toward the aqueous medium.[Table 2001] (Ref. 1001/1002/1003/1004/1005/1006/1007/1015/1207) |
Metabolism of LDL LDL particles are mainly derived from the catabolism of VLDL. Lipoprotein lipase(LPL) hydrolyzes most of triglycerides of VLDL. Concequently, VLDL is converted into IDL. A portion of IDL particles are removed to the liver via LDL receptor. Moreover, triglycerides of the remainder of IDL particles are hydrolyzed by hepatic triglycerides lipase (HTGL) and IDL is converted into LDL. LDL is taken in cells via LDL receptor on peripheral tissues and supplies cholesterols to cells. LDL is cleared from plasma via LDL receptor, predominantly in the liver.(Ref. 1001/1007/1013/1014/1015/1207) |
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| 2 | No image | a- lipoprotein |
high density lipoprotein |
TLP1201 | Kazuo Kondo |
HDL |
Biological Activity HDL Approximately 25% of the total cholesterol in plasma is contained in HDL particles.HDL particles transport cholesterol from peripheral cells to other lipoproteins and the liver.Many epidemiological studies have shown an inverse relationship between the prevalence of coronary heart disease(CHD) and the level of HDL cholesterol.(Ref. 1208/1209/1210/1211) |
Definition of HDL High density lipoprotein (HDL) is defined as the lipoprotein fraction with a density range between 1.063 to 1.21 g/ml. The HDL fraction comprises two major fractions : HDL2 (1.063-1.125 g/ml) and HDL3 (1.125-1.21 g/ml).(Ref. 1001) |
HDL2 : 1.063-1.125 g/ml, HDL3 : 1.125-1.210 g/ml |
Physical properties Particle weight HDL2: 3.6 105, HDL3: 1.75105, Diameter (nm) HDL2 : 8-11, HDL3 : 6-9Relative weight composition (%) HDL2 : Protein 35-40 Phospholipid 30-40 Free cholesterol 4-6 Cholesteryl ester 15-20 Triglyceride 3-6, HDL3 : Protein 45-55 Phospholipid 25-35 Free cholesterol 1-3 Cholesteryl ester 8-15 Triglyceride 3-6 Apolipoprotein contribution (%) HDL2 : apo A-I 65 apo A-II 10 apo C 10-15 apo E 3-5, HDL3 : apo A-I 62 apo A-II 23 apo A-IV Trace apo C 5 apo E 1 (Ref. 1006) |
HDL in agarose gel electrophoresis In agarose gel electrophoresis HDL migrates at the same position as a-globulins; thus HDL is designated a-lipoprotein. Fig.1 through 4: Electrophorograms above electrophoretic patterns of anodically migrating lipoprotein fractions. Fig.1: Fat Red 7B stained lipoproteins. Fig.2: Formazan dye developed cholesterol fractions. Fig.3: Formazan dye developed triglyceride fractions Fig.4: Fig.2 and Fig.3 superimporsed. Demonstrate relative positions and enabling ratio assessment of all triglyceride and choresterol fractions, including Lp(a), Lipo X, slowa,IDL,andb-VLDL. [Chromatogram 1001] |
Classification of HDL The HDL fraction consists of heterogeneous particles differentiated by particle size, chemical composition and physicochemical properties and are separated into three main subfractions differentiated by density: HDL1 (1.055-1.085 g/ml), HDL2 (1.063-1.125 g/ml) and HDL3 (1.125-1.21 g/ml). HDL2 and HDL3 are major fractions. HDL1 is a minor fraction and contains apolipoprotein E (apo E) as its main protein component and is mainly observed in humans who have ingested a high-cholesterol diet for several weeks. These subfractions are separated into other subclasses according to size by polyacrylamide gradient gel electrophoresis (GGE). Two have migration distances (RF values) in the range associated with HDL2 and three in the RF range of HDL3. Mean hydrated densities and particle sizes of these subfractions are 1.085 g/ml and 10.57 nm for (HDL2b)gge, 1.115 g/ml and 9.16 nm for (HDL2a)gge, 1.136 g/ml and 8.44 nm for (HDL3a)gge, 1.154 g/ml and 7.97 nm for (HDL3b)gge, and 1.171 g/ml and 7.62 nm for (HDL3c)gge. HDL can be fractionated into LpA-I and LpA-I/A-II, differentiated by the constituent apolipoproteins using affinity columns containing antibodies specific for apo A-I and apo A-II. LpA-I contains apolipoprotein A-I (apo A-I) but not apolipoprotein A-II (apo A-II) and LpA-I/A-II contains both apo A-I and apo A-II. Some evidences suggests that LpA-I can promote cholesterol efflux from cells but LpA-I/A-II is less effective. Pre-b-HDL is a minor fraction of LpA-I, migrating in the pre-b position on agarose gel electrophoresis. Pre-b-HDL is considered the initial acceptor of cellular cholesterol.(Ref. 1201/1202/1203/1204/1205) |
Composition and Structure of HDL The average molecular weight of HDL2 is 3.6 105 and consists of protein (35-40%), phospholipid (30-40%), free cholesterol (4-6%), cholesteryl ester (15-20%) and triglyceride (3-6%). The average molecular weight of HDL3 is 1.75105 and consists of protein (45-55%),phospholipid (25-35%), free cholesterol (1-3%), cholesteryl ester (8-15%) and triglyceride (3-6%). The ratio of phosphatidyl choline to sphingomyelin and that of free to estetified cholesterol is greater for HDL2 than for HDL3.Approximately 90% of the constituent apolipoproteins on HDL2 and HDL3 are apolipoprotein A-I (apo A-I) and apolipoprotein A-II (apoA-II) .Apolipoprotein C (apo C),apo E and apolipoprotein A-IV (apo A-IV) are found in small quantities. The relative proportion of apoA-I and apo A-II varies in the HDL subfractions .Preparation by zonal ultracentrifugation shows an apo A-I/apo A-II molar ratio of 9:1 in the HDL2 fraction and 2:1 in the HDL3 fraction. HDL particles are secreted as discoidal particles or small spherical particles. Discoidal HDL consists of phospholipid and some unesterified cholesterol organized as a lipid bilayer associated with apo A-I.The discoidal particles are designated nascent HDL, and are transformed into spherical particles by lecithin:cholesterol acyl transferase (LCAT) reaction.In all of the sub fractions , HDL exists as spherical particles which contain the same chemical constituents,but differ in particle size, density and stoichiometry.The structure of HDL is presumed to comprise cholesteryl esters and triglycerides in the hydrophobic core, surrounded by a surface coat of apo A-I,apo A-II ,phosphatidyl choline and sphingomyelin oriented toward the aqueous medium. [Table 2001] (Ref. 1001/1003/1005/1006/1206/1207) |
Metabolism of HDL HDL precursors are secreted from the liver and intestine, or derived from surface fragments originating by lipolysis of chylomicrons and VLDL. These particles consists of phospholipid and some unesterified cholesterol organized as a lipid bilayer associated with apo A-I. Apo A-I is an activator of the lecithin:cholesterol acyl transferase (LCAT). HDL precursors acquire unesterified cholesterol from cell membranes, incorporate cholesteryl esters into their cores by the LCAT reaction, and become mature HDL particles ( HDL precursors  HDL3HDL2). Cholesteryl esters of HDL are transferred to apo B containing lipoproteins by the cholesteryl ester transfer protein (CETP), and exchanged for their triglycerides. Then triglycerides of HDL are hydrolyzed by hepatic lipase, the HDL particles become smaller, more dense particles that are donors for further transfer of cholesteryl esters.These processes are part of the Reverse Cholesterol Transport system. Cholesteryl esters transferred to apo B containing lipoproteins are endocytosed with those particles in the liver by receptor-mediated processes involving the LDL and chylomicron remnant receptors. Moreover it appears that another pathway exists for the transport of cholesteryl ester to liver: HDL particles transport cholesterol directly to hepatocyte by receptor-mediated endocytosis. It is postulated that HDLwith apo E is ultimately taken up into the liver via an apo E receptor (remnant receptor), and HDL without apo E is ultimately taken up via the HDL receptor. Cholesterol taken up into the liver is finally made available for the synthesis of bile acids.(Ref. 1001/1006/1207) |
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| 3 | No image | pre b lipoprotein |
very low density lipoprotein |
TLP1301 | Kazuo Kondo |
VLDL |
Biological activities VLDL is the major vehicle in the plasma which carries triacylglycerol synthesized in the liver to peripheral tissues for utilization. . (Ref. 1307) |
Definition VLDL is defined as the lipoprotein fraction with the density range of 0.93 to1.006 g/ml. (Ref. 1301) |
0.93 to1.006 g/ml (Ref. 1301) |
Physical properties Particle weight 8 107 Diameter nm 30-80 Relative weght Composition (%) of Human Plasma Lipoproteins Protein 10% Phospholipid 19% Free cholesterol 7.3% Cholesterol ester 4.6% Triglyceride 56% Apolipoprotein contribution% apoB 37 apoC 50 apoE13 (Ref. 1301) |
VLDL on agarose gel electrophoresis In agarose gel electrophoresis, VLDL migrate at the same position of preb-globulins, thus VLDL is designated preb-lipoprotein. |
Structure of VLDL VLDL is spherical particle and in normal individuals ranges 30 to 80 nm in diameter. The molecular weight is 10 to 8 107. Compare with LDL particles, VLDL particles are heterogeneous in size and composition. VLDL particls can be separated in Sf 20-60 and Sf60-400. VLDL consists of protein 10%, phospholipid 19%, free cholesterol 7%, cholesterol ester 10% and triglycerides 56%. Apolipoprotein contribution% apoB 37 apoC 50 apoE 13 Apo B-48 is the sole constituent apolipoprotein on VLDL.It is presumed that the cholesteryl esters and triglycerides form the hydrophobic core, which is surrounded by a surface coat of apolipoprotein B, free cholesterol and polar phospholipid components oriented toward the aqueous medium.(Ref. 1301/1302/1303/1304/1305/1306) |
Metabolism of VLDL VLDL is syncesized by the liver. VLDL is the major vehicle in the plasma which carries triacylglycerol synthesized in the liver to peripheral tissues for utilization. VLDL is catabolized by lipoprotein lipase. Concequently,VLDL is converted into IDL. The VLDL remnants are taken up into the liver via the LDL receptor and the LDL receptor-related protein. (Ref. 1301/1307) |
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| 4 | No image | Chylomicrons |
Chylomicrons |
TLP1401 | Kazuo Kondo |
chylos |
Biological activities Chylomicrons transport dietary triglyceride from the intestine to peripheral tissues and cholesterol to the liver. (Ref. 1406) |
Defination Chylomicrons is defined as the lipoprotein fraction with the density below 0.93 (Ref. 1401) |
below 0.93 g/ml (Ref. 1401) |
Physical properties Particle weight below 4 108 Diameter nm 75-1200 Relative weght Composition (%) of Human Plasma Lipoproteins Protein 1-2% Phospholipid 19% Free cholesterol 1.6% Cholesterol ester 1.4% Triglyceride % Apolipoprotein contribution% apoB 5-20 apoC 70-80 apo E4 (Ref. 1401) |
Chylomicrons on agarose gel electrophoresis In agarose gel electrophoresis Chylomicrons remains at origin. |
Structure of Chylomicrons Chylomicrons is a spherical particle and in normal individuals ranges 75 to 1200 nm in diameter. The average molecular weight is below 4 108 .Compared with other lipoproteins , Chylomicrons particles are relatively heterogeneous in size and composition . Chylomicrons consists of Protein 1-2% Phospholipid 19% Free cholesterol 1.6% Cholesterol ester 1.4% Triglyceride 88% Apolipoprotein contribution% apoB 5-20 (mainly apoB48) apoC 70-80 apoE 4 on Chylomicrons. It is presumed that the cholesteryl esters and triglycerides form the hydrophobic core, which is surrounded by a surface coat of apolipoprotein B48, free cholesterol and polar phospholipid components oriented toward the aqueous medium. (Ref. 1401/1402/1403/1404/1405) |
Metabolism of Chylomicrons Chylomicrons are formed in the intestine and transport dietary triglyceride to peripheral tissues and cholesterol to the liver. The enzyme lipoprotein lipase, with apolipoprotein (apo)C-II as a co-factor, hydrolyzes chylomicron triglyceride allowing the delivery of free fatty acids to muscle and adipose tissue. As a result, a new particle called a chylomicron remnant is formed.The chylomicron remnants are rapidly taken up into the liver via the LDL receptor and the LDL receptor-related protein. (Ref. 1401/1406/1407) |
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| 5 | No image | remnant like particles |
TLP2001 | Kazuo Kondo |
RLP |
Definition RLP is an abbreviation given to remnant like lipoprotein particles,which do not bind to the anti apo A-I monoclonal antibody (H-12), anti apo B-100 monoclonal antibody (JI-H) conjugated Sepharose-4B. |
Physical properties main Diameter nm 30-80 Relative weight composition % Protein 7-10 Phospholipid 17-21 Free cholesterol 6-8 Cholesteryl ester 6-23 Triglyceride 41-61 Apolipoprotein contribution % apoB 3-6 apoCIII 13-19 apo E 29-32 |
Characterization RLP is an abbreviation given to rremnant like lipoprotein particles, which do not bind to the anti apo A-I monoclonal antibody (H-12), anti apo B-100 monoclonal antibody (JI-H) conjugated Sepharose-4B. Greater than 97% of the LDL and HDL were removed from the serum by the antibodies. Most VLDL are also removed from the serum but chylomicron-derived particles containing apo B-48 remain in the supernatant, together with a minor fraction of VLDL particles containing apo B-100. Both of these particles populations have been shown to be enriched in apo E. The epitope of the apo B-100 monoclonal antibody has been localized to an amphipathic helical region of apo B-100 encompassing residues 2291-2318, i.e., at about B-51. The serum concentrations of remnant-like particles are routinely determined in the supernate as RLP-cholesterol and RLP-triglycerides.RLP-cholesterol and RLP-triglycerides increase in patients with atherosclerotic diseases. An increase of RLP-cholesterol in blood is a risk factor for atherosclerosis. [Table 2001] (Ref. 2006) |
Remnant like Particles (RLP) Remnant like particles are isolated almost free of low density lipoprotein (LDL) and high density lipoprotein (HDL) by use of an immunoafinity matrix in which Monoclonal antibody (Mab) JI-H and a Mab to apo A-I are bound to agarose beads. Mab (JI-H) recognizes an epitope in the region of apo B-51. Mab (JI-H) binds to LDL and most Triglyceride-rich lipoproteins (TRL), but not to a minor fraction of TRL particles containing apo B-100 that is enriched in apo E. The RLP is enriched in apo E and contain more cholesterol esters and free cholesterol than those bind to Mab JI-H. The electrophoretic mobility of RLP is reduced, as compared with the bound very low density lipoprotein (VLDL). In normolipidemic human subjects, the RLP account for about 15% of the total apo B in TRL. The particles are homogeneous in size (30-80 nm) and composition.RLP reflect chyromocron remnants and VLDL remnants. (Ref. 2001) |
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| 6 | No image | lipoprotein (a) |
TLP3001 | Kazuo Kondo |
Lp(a) |
Biological activities There is substantial evidence for an association between serum Lp(a) concentration and myocardial infarction. Most of this evidence is from case control rather than prospective studies. There is also evidence that serum Lp(a) is related to the extent of coronary artery disease assessed angiographically. It is often stated that Lp(a) is a strong independent indicator of coronary heart disease risk. (Ref. 3009/3010/3011) |
Physical properties Mean Diameter 21-26 nm Relative weight composition % Protein30.9}0.8 Phospholipid 19.0}0.2 Free cholesterol 7.9}1.8 Cholesterol ester 37.1}1.6 Triglyceride 8.0}5.3 Density 1.05-1.21g/mL(Ref. 3005) |
Characterization Lp(a) particles, first identified in human plasma by K. Berg in 1963(Ref. 3006), are similar to low-density lipoproteins (LDL), containing apolipoprotein B-100 (apo B-100) and a similar lipid content. In addition, Lp(a) contains the glycoprotein apolipoprotein(a) (apo (a)), which is disulfide-linked to apo B-100(Ref. 3001). |
Structure Lp(a) is made up of a low-density lipoprotein-like structure in which apolipoprotein B-100, the protein moiety of authentic low-density lipoprotein, is covalently linked to a glycoprotein, apolipoprotein (a) ,which is the specific marker of Lp (a) that exhibits a striking similarity to plasminogen. The dominant structural motif of apo (a) is the kringle, a three-disulfide, triple-loop structure named for its resemblance to a Danish pretzel. Kringle 4 is repeated 13 to 37 times, whereas there is only one kringle 5. It is now established that the size of each apo (a) isoform is under strict genetic control and determined by the number of kringles that it contains. Usually, there is 1 mol of apo (a) and 1 mol of apo B-100 in each Lp(a) particle. However, species of Lp (a) having one copy of apo B-100 and 2mol of apo (a) have been reported. Composition Lp(a) is heterogeneous, both within and among individuals, and this heterogeneity may at least partly be accounted for by differences in the size of apo (a). The Mr of apo (a) varies among individuals, and no fewer than six isoforms with Mr ranging from 450,000 to 1,000,000 Da have been observed.(Ref. 3007) Synthesis The primary site of synthesis of Lp (a) appears to be the hepatocyte, although apo (a) mRNA has also been identified in testes and brain.(Ref. 3008) Synthesis of apo (a) in liver is hardly surprising given that the hepatocyte is also the primary site of the synthesis of apo B-100. |
Metabolism Lp(a) contains an LDL component having an apo B-100 moiety, early studies addressed the access of Lp (a) to LDL receptor pathways. Several groups have demonstrated that Lp (a) binds to the classic LDL receptor in cultured fibroblasts, although with a lower affinity than LDL itself; the estimated apparent Kd for Lp (a) is 9.5 nM compared with 7.8 nM for LDL, according to Krempler and colleagues. |
The cDNA for apo (a) predicted a protein consisting of tandemly repeated plasminogen kringle-four-like domains followed by a single plasminogen kringle-five-like and protease domain. It is postulated that the differences in the sizes of the isoforms is a result of allelic variation in the number of kringle-four repeats. The apo (a) gene has been localized to the long arm of chromosome 6 (q26-27) where it is closely linked to the plasminogen gene.(Ref. 3012) |
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| 7 | No image | apolipoprotein A-I |
TLP4101 | Kazuo Kondo |
apo A-I |
Molecular weight:28,016 Isoelectric point:5.4-5.05(Ref. 4101) |
The number of amino acid residues :243 |
Amino acid compositions (Ref. 4113) |
Amino acid sequences:In 1975, the primary structure of apo AI was clarified by Baker et al., and the full-length cDNA was cloned by Brewer et al. in 1984. |
Structure: The secondary structure of apo AI consists of 11 a-helices (55%),2 b-turns (8%), and 2 b-turns (37%). |
Method of purification HDL was initially purified and separated by ultracentrifugation, and the sample containing apo AI was dialyzed against 0.16 M NaCl-1 mM EDTA solution (pH 8.0), then lyophilized. Subsequently, fat was removed from the sample by ether/ethanol (2/3), and the sample was dissolved in 0.01 M Tris-6 M urea solution (pH 8.6) for purification by gel filtration chromatography. |
Existing condition and distribution of lipoprotein In blood, apo AI binds to lipids and exists as a component of chylomicron and HDL.(Ref. 4103) |
Sites of synthesis:The liver and the small intestine. The rate of synthesis:11mg/kg/day |
Metabolism Apo AI is synthesized in the liver and samll intestine. Apo AI is initially contained in chylomicron in blood, then produces nascent HDL in combination with phospholipids. Subsequently, nascent HDL is altered to mature HDL by LCAT and taken up in the liver and other organs. Half life:4.3 days(Ref. 4111) |
Standard range:122 - 161 mg/dl (in human sera) Diseases and drugs that induce abnormal levels of apo A-I.:Hypoalphalipoproteinemia, LCAT deficiency, and abetalipoproteinemia. Analytical methods:TIA,ELISA,Nephelometry,SRIDetc. |
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| 8 | No image | apolipoprotein A-II |
TLP4201 | Kazuo Kondo |
apo A-II |
The number of amino acid residues :77 2molecules |
Amino acid compositions (Ref. 4113) |
Amino acid sequences:Further investigations are required. |
Structure:Apo AII consists of 2 polypeptide molecules, and the 6th cysteine molecules are bound by the disulfide bond. The secondary structure of apo AII consists of a-helix (35%), b-structure (13%), and irregular structure (52%). |
Method of purification HDL was initially purified and separated by ultracentrifugation, and the sample containing apo AII was dialyzed against 0.16 M NaCl-1 mM EDTA solution (pH 8.0), then lyophilized. Subsequently, fat was removed from the sample using ether/ethanol (2/3), and dissolved in 0.01 M Tris-6 M urea (pH 8.6) for purification by gel filtration chromatography. |
Existing condition and distribution of lipoprotein In blood, apo AII binds to lipids, and exists as a component of chylomicron and HDL.(Ref. 4204) |
Sites of synthesis:The liver and the small intestine. The rate of synthesis:2.8mg/kg/day |
Metabolism After transport from chylomicron to HDL, apo AII is taken up in the liver. Half life:5.0 days(Ref. 4207) |
Standard range:25.1-34.5 mg/dl (in human sera) Diseases and drugs that induce abnormal levels of apo A-II. LCAT deficiency, and abetalipoproteinemia. Analytical methods:TIA,ELISA,Nephelometry SRID,RIA etc. |
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| 9 | No image | apolipoprotein B |
TLP4301 | Kazuo Kondo |
apo B |
Function (1) Apo B is a structural element of chylomicron, VLDL, IDL, and LDL.(2) Apo B binds to lipids to synthesize chylomicron or VLDL, which is secreted into lymphatic and blood vessels. Apo B accelerates absorption of dietary lipids, especially triglycerides. (3)Apo B binds to cell surface receptors to supply lipids into the cell.(Ref. 4304/4305/4306) |
Molecular weight: 549,000(Ref. 4301) |
The number of amino acid residues : |
Amino acid sequences: The primary structure of apo B is repetitive. |
Structure: The secondary structure consists of a-helices (25%), b-structures (37%), and disordered structures (37%). However, the secondary structure of apo B varies depending on binding lipids and temperatures. |
Method of purification A fraction containing apo B (1.030 - 1.050 g/ml) was purified by ultracentrifugation, which was defatted by ether/ethanol. |
Existing condition and distribution of lipoprotein In blood, apo B binds to lipids, and is a structural element of LDL and VLDL. |
Sites of synthesis: liver The rate of synthesis:14.4mg/kg/day |
Metabolism Apo B is synthesized in the liver and secreted as VLDL. When LPL acts on VLDL, VLDL is converted to LDL, which is incorporated into LDL receptors. In addition, a part of apo B is denatured, and is processed by incorporation into the scavenger receptor pathway. Half life:2.2days(Ref. 4307) |
Genetic information Gene locus:There are 4 loci for the alpha globulin (Ag) gene on the short arm of chromosome 2. Gene arrangement (DNA)(Ref. 4309/4310/4311) :Information of genetic diseases: Ten allotypes (Aga1, c, d, g, h, l, t, x, y, and z) have been discovered.Information of genetic diseases (abetalipoproteinemia, hypobetalipoproteinemia). Phenotypes:Further investigations are required.(Ref. 4308) |
Standard range:69-105mg/dl (in human sera) Diseases and drugs that induce abnormal levels of apo B. Hyperlipoproteinemia (type IIa, IIb), familial LCAT deficiency, abetalipoproteinemia, and hypobetalipoproteinemia. Analytical methods:TIA,ELISA,Nephelometry ,SRIDetc. |
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| 10 | No image | apolipoprotein C-II |
TLP4401 | Kazuo Kondo |
apo C-II |
Molecular weight:8,837 Isoelectric point:4.9(Ref. 4401) |
The number of amino acid residues :79 |
Amino acid compositions (Ref. 4408) |
Amino acid sequences:Further investigations are required. |
Structure:The primary structure of apo C-II is comprised of single-stranded polypeptides. Amphiphilic helix structures are observed in segments 13-22, 28-38, and 43-51. Hydrophobic peptides in segments 66-78, 60-78, 55-78, and 50-78 do not bind to phospholipids, while the segment 43-49 is highly hydrophobic and has a helix structure, thus being involved in lipid binding. |
Method of purification After centrifugation, VLDL was separated from plasma by ultracentrifugation, which was defatted after dialysis. |
Existing condition and distribution of lipoprotein In blood, apo C-II binds to lipids, and is a structural element of VLDL and HDL |
Sites of synthesis:The liver and the small intestine. The rate of synthesis:1.6mg/kg/day |
Standard range:1.6- 4.2mg/dl (in human sera) Diseases and drugs that induce abnormal levels of apo C-II.:Apo C-II deficiency Analytical methods:TIA,ELISA,Nephelometry ,SRIDetc. |
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| 11 | No image | apolipoprotein C-III |
TLP4501 | Kazuo Kondo |
apo C-III |
The number of amino acid residues :79 |
Amino acid compositions (Ref. 4408) |
Amino acid sequences::Further investigations are required. |
Structure:The primary structure of apo C -III is comprised of single-stranded polypeptides. Threonine74 binds to one molecule each of galactose, mannose and galactosamine, in addition to 0 or several molecules of sialic acid. The secondary structure consists of a-helices (17.7%), b-structures (17.7%), b-turns (30.4%), and random structures (34.2%). The secondary structure of apo C III forms amphiphilic helices, and polar amino acids distributed on the opposite side of the structure are involved in lipid binding. |
Method of purification After centrifugation, VLDL was separated from plasma by ultracentrifugation, which was defatted after dialysis. |
Existing condition and distribution of lipoprotein In blood, apo C-III binds to lipids, and is a structural element of VLDL and HDL. |
Sites of synthesis:The liver and the small intestine. The rate of synthesis:5.2mg/kg/day |
Standard range:5.5- 9.5 mg/dl (in human sera) Diseases and drugs that induce abnormal levels of apo C-III. Apo C III deficiency Analytical methods:TIA,ELISA,Nephelometry,SRID etc. |
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| 12 | No image | apolipoprotein E |
TLP4601 | Kazuo Kondo |
apo E |
Function (1) Apo E transits among lipoproteins, thus being involved in regulation of lipoprotein metabolism. (2) Apo E is involved in lipoprotein uptake via cell receptors as well as in the catabolism of lipids and proteins.(Ref. 4604) |
Molecular weight:3,3000-3,9000 Isoelectric point:5,7-6.0(Ref. 4601) |
The number of amino acid residues :299 |
Amino acid compositions (Ref. 4611) |
Amino acid sequences:Further investigations are required. |
Structure:Arginine accounts for a relatively large proportion of structural amino acids (10 - 12 mol%). When the secondary structure of apo E is examined, 62% of structural amino acids form 11 a-helix segment, 11% of structural amino acids form 8 b-turns, 9% of structural amino acids form 3 short sheets, and the remaining amino acids form random coils which are mainly located at the region between the 164th and 202nd amino acid residues. |
Method of purification Lipoproteins are initially separated by ultracentrifugation. After defatting, apoproteins are separated and purified by column chromatography. |
Existing condition and distribution of lipoprotein In blood, apo E is bound to lipids, and accounts for 15% of apoproteins in VLDL. A small amount of apo E is also contained in chylomicron, chylomicron remnant, HDL, and LDL. |
Sites of synthesis:The liver The rate of synthesis:5.2mg/kg/day |
Metabolism Apo E is synthesized in the liver, and contained in VLDL and nascent HDL. When lipoprotein lipase acts on VLDL, a part of apo E in VLDL is released and transferred to HDL. When LCAT acts on HDL, apo E in HDL is transferred to VLDL. The respective lipoproteins are taken up after being bound to LDL receptors, chylomicron remnant receptors, and apo E receptors. Half life:0.4days(Ref. 4605/4606/4607) |
Genetic information Gene locus:19; Gene arrangement (DNA)(Ref. 4612) Information of gene aberration:Apo E3 is a wild type of apo E. In apo E2 and E4, mutual replacement occurs between arginine and cysteine at the 112th and 158th amino acid residues of apo E3, respectively. Information of genetic diseases :apo E2 homozygote Phenotypes:E1,E2,E3,E4,E5,E7(Ref. 4608/4609/4610) |
Standard range:2.8- 4.6mg/dl (in human sera) Diseases and drugs that induce abnormal levels of apo E. Congenital apo E abnormalities (dyslipoproteinemia caused by apo E2 homozygote, apo E deficiency, b-lipoprotein abnormalities demonstrating E3/3) and risk factors for Alzheimer's disease (apo E4). Analytical methods:TIA,ELISA,Nephelometry,SRID etc. |
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| AUTHOR | : | Gotto,A.M. Jr., Pownall,H.J., and Havel,R.J. (1986) Introduction to the Plasma Lipoproteins, in Methods in Enzymology vol.128 (Segrest,J.P. and Albers,J.J., eds),pp3-41, Academic Press, London |
| TITLE | : | |
| JOURNAL | : | |
| VOL | : | PAGE : - () |
| AUTHOR | : | Lee, D. M., and Alaupovic, P. |
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