BIOMAT Database Logo BIOMAT Database Logo

Human very low density lipoprotein structure: interaction of the C apolipoproteins with apolipoprotein B-100. 1993

C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Department of Medicine, Baylor College of Medicine, Houston, TX 77030.

Very low density lipoproteins (VLDL) are a heterogenous population of particles differing in size and composition. Heparin-Sepharose chromatography yields three VLDL subfractions. Two subfractions, VLDLNR-1 and VLDLNR-2, which are not retained by heparin, contain little or no detectable apolipoprotein (apo)E. According to negative stain electron microscopy, VLDLNR-1 is slightly larger than VLDLNR-2. The third fraction, VLDLR, is composed of smaller particles that are retained by the heparin-Sepharose and contain apoE. The C apolipoproteins of the respective VLDL subfractions transfer to 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC) single bilayer vesicles giving three subfractions designated VLDLNR-1-C, VLDLNR-2-C, and VLDLR-C. The protein, phospholipid, and cholesterol (free + esterified) contents decrease in the order VLDLR > VLDLNR-2 > VLDLNR-1. Triglyceride content decreases in the opposite order. POPC treatment of each VLDL subfraction increases the phospholipid and decreases the protein, triglyceride, and cholesteryl ester contents, while free cholesterol remains unchanged. According to immunological analysis of each subfraction with well-characterized monoclonal antibodies, the accessibility of some epitopes of apoB-100 on VLDL is changed by POPC treatment. Electron-microscopic analysis of POPC-treated VLDL subfraction reveals vacancies on the surfaces of each particle. VLDLNR-1, VLDLNR-2, and VLDLR are resistant to thrombin cleavage, whereas the lipoproteins lacking C apolipoproteins are not. Thrombin cleavage (8 h) of apoB-100 of VLDLNR-2-C and VLDLR-C gives two fragments, T1 and T2, that are converted to smaller fragments only after prolonged treatment. In contrast, apoB-100 of VLDLNR-1-C is converted into small fragments after 8 h thrombin treatment. These results suggest that removal of apoCs affects the accessibility and conformation of apoB-100 in the individual VLDL subfractions in the region near residue 3249, which is the primary thrombin cleavage site and the epitope of monoclonal antibody 4C11.

UI MeSH Term Description Entries
D008079 Lipoproteins, VLDL 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. Pre-beta-Lipoprotein,Prebeta-Lipoprotein,Prebeta-Lipoproteins,Very Low Density Lipoprotein,Very-Low-Density Lipoprotein,Very-Low-Density Lipoproteins,Lipoprotein VLDL II,Lipoproteins, VLDL I,Lipoproteins, VLDL III,Lipoproteins, VLDL1,Lipoproteins, VLDL2,Lipoproteins, VLDL3,Pre-beta-Lipoproteins,Lipoprotein, Very-Low-Density,Lipoproteins, Very-Low-Density,Pre beta Lipoprotein,Pre beta Lipoproteins,Prebeta Lipoprotein,Prebeta Lipoproteins,VLDL Lipoproteins,VLDL1 Lipoproteins,VLDL2 Lipoproteins,VLDL3 Lipoproteins,Very Low Density Lipoproteins
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D002845 Chromatography Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts. Chromatographies
D004797 Enzyme-Linked Immunosorbent Assay An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed. ELISA,Assay, Enzyme-Linked Immunosorbent,Assays, Enzyme-Linked Immunosorbent,Enzyme Linked Immunosorbent Assay,Enzyme-Linked Immunosorbent Assays,Immunosorbent Assay, Enzyme-Linked,Immunosorbent Assays, Enzyme-Linked
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001055 Apolipoproteins B 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. Apo-B,Apo B,ApoB,Apoprotein (B),Apoproteins B
D001056 Apolipoproteins C 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. Apo-C,Apo C,ApoC,Apoprotein (C),Apoproteins C
D013917 Thrombin An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN. Thrombase,Thrombin JMI,Thrombin-JMI,Thrombinar,Thrombostat,alpha-Thrombin,beta,gamma-Thrombin,beta-Thrombin,gamma-Thrombin,JMI, Thrombin
D053299 Apolipoprotein B-100 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. Apo B-100,Apo-B-100,ApoB-100,Apo B 100,ApoB 100,Apolipoprotein B 100

Related Publications

C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Apolipoproteins C-III and A-V as predictors of very-low-density lipoprotein triglyceride and apolipoprotein B-100 kinetics.
March 2006, Arteriosclerosis, thrombosis, and vascular biology,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Metabolism of very-low-density lipoprotein and low-density lipoprotein containing apolipoprotein C-III and not other small apolipoproteins.
February 2010, Arteriosclerosis, thrombosis, and vascular biology,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Increased hepatic secretion of very-low-density lipoprotein apolipoprotein B-100 in NIDDM.
August 1995, Diabetologia,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
The binding of very low density lipoprotein remnants to the low density lipoprotein receptor in familial defective apolipoprotein B-100.
August 1993, Atherosclerosis,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the low density lipoprotein-receptor interaction.
August 1992, Journal of lipid research,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Binding of thyroxine to human plasma low density lipoprotein through specific interaction with apolipoprotein B (apoB-100).
February 1989, Biochimie,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Very low density lipoprotein apolipoprotein B metabolism in humans.
August 1988, Klinische Wochenschrift,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Determinants of the kinetics of very low-density lipoprotein apolipoprotein B-100 in non-obese men.
August 1997, Clinical and experimental pharmacology & physiology,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
Acute hyperinsulinemia decreases the hepatic secretion of very-low-density lipoprotein apolipoprotein B-100 in NIDDM.
September 1995, Diabetes,
C Y Yang, and Z W Gu, and N Valentinova, and H J Pownall, and B Lee, and M Yang, and Y H Xie, and J R Guyton, and T N Vlasik, and J C Fruchart
The affinity of low-density lipoproteins and of very-low-density lipoprotein remnants for the low-density lipoprotein receptor in homozygous familial defective apolipoprotein B-100.
June 1995, Atherosclerosis,
Copied contents to your clipboard!