BIOMAT Database Logo BIOMAT Database Logo

Isolation and partial characterization of lipoprotein A-II (LP-A-II) particles of human plasma. 1992

E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Lipoprotein and Atherosclerosis Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104.

High density lipoproteins (HDL) consist of a mixture of chemically and functionally distinct families of particles defined by their characteristic apolipoprotein (Apo) composition. The two major lipoprotein families are lipoprotein A-I (LP-A-I) and lipoprotein A-I:A-II (LP-A-I:A-II). This study describes the isolation of a third minor HDL family of particles referred to as lipoprotein A-II (LP-A-II) because it lacks ApoA-I and contains ApoA-II as its main or sole apolipoprotein constituent. Because ApoA-II is an integral protein constituent of three distinct lipoprotein families (LP-A-I:A-II, LP-A-II: B:C:D:E and LP-A-II), LP-A-II particles were isolated from whole plasma by sequential immunoaffinity chromatography on immunosorbers with antisera to ApoA-II, ApoB and ApoA-I, respectively. In normolipidemic subjects, the concentration of LP-A-II particles, based on ApoA-II content, is 4-18 mg/dl accounting for 5-20% of the total ApoA-II not associated with ApoB-containing lipoproteins. The lipid composition of LP-A-II particles is characterized by low percentage of triglycerides and cholesterol esters and a high percentage of phospholipids in comparison with lipid composition of LP-A-I and LP-A-II: A-II. The major part of LP-A-II particles contain ApoA-II as the sole apolipoprotein constituent; however, small subsets of LP-A-II particles may also contain ApoD and other minor apolipoproteins. The lipid/protein ratio of LP-A-II is higher than those of LP-A-I and LP-A-I:A-II. In homozygous ApoA-I and ApoA-I/ApoC-III deficiencies, LP-A-II particles are the only ApoA-containing high density lipoprotein with levels found to be within the same range (7-13 mg/dl) as those of normolipidemic subjects. However, in contrast to normal LP-A-II, their lipid composition is characterized by higher percentages of triglycerides and cholesterol esters and a lower percentage of phospholipids and their apolipoprotein composition by the presence of ApoC-peptides and ApoE in addition to ApoA-II and ApoD. These results show that LP-A-II particles are a minor HDL family and suggest that, in the absence of ApoA-I-containing lipoproteins, they become an efficient acceptor/donor of ApoC-peptides and ApoE required for a normal metabolism of triglyceride-rich lipoproteins. Their other possible functional roles in lipid transport remain to be established in future experiments.

UI MeSH Term Description Entries
D008055 Lipids 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) Lipid
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D001053 Apolipoproteins 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. Apolipoprotein
D016632 Apolipoprotein A-I 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. Apo A-I,Apo A-1,Apo A-I Isoproteins,Apo A1,Apo AI,ApoA-1,ApoA-I,Apolipoprotein A-1,Apolipoprotein A-I Isoprotein-2,Apolipoprotein A-I Isoprotein-4,Apolipoprotein A-I Isoproteins,Apolipoprotein A1,Apolipoprotein AI,Apolipoprotein AI Propeptide,Pro-Apo A-I,Pro-Apolipoprotein A-I,Proapolipoprotein AI,Apo A I Isoproteins,Apolipoprotein A 1,Apolipoprotein A I,Apolipoprotein A I Isoprotein 2,Apolipoprotein A I Isoprotein 4,Apolipoprotein A I Isoproteins,Pro Apo A I,Pro Apolipoprotein A I
D016633 Apolipoprotein A-II 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. Apo A-II,Apo A-2,Apo A-II Isoproteins,Apo A2,Apo AII,ApoA-2,ApoA-II,Apolipoprotein A-2,Apolipoprotein A-II Isoproteins,Apolipoprotein A2,Apolipoprotein AII,Pro-Apo A-II,Pro-Apolipoprotein A-II,Proapolipoprotein A-II,Apo A II Isoproteins,Apolipoprotein A 2,Apolipoprotein A II,Apolipoprotein A II Isoproteins,Pro Apo A II,Pro Apolipoprotein A II,Proapolipoprotein A II

Related Publications

E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Isolation and partial characterization of two abnormal human plasma lipoproteins: LP-X1 and LP-X2.
June 1976, Biochimica et biophysica acta,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Characterization of the Lp(a) lipoprotein in human plasma.
January 1970, Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
[Purification and partial characterization of lipoprotein Lp (a)].
January 1977, Biochimie,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Radioimmunoassay of human plasma Lp(a) lipoprotein.
May 1977, Journal of lipid research,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Isolation and partial characterization of apolipoprotein (a) from human lipoprotein (a).
October 1986, Biochemistry and cell biology = Biochimie et biologie cellulaire,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Immunochemical quantification of human plasma Lp(a) lipoprotein.
January 1974, Lipids,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Isolation and characterization of lipoprotein-X (LP-X) from canine.
December 1973, FEBS letters,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Isolation and partial characterization of intracytoplasmic A particles.
April 1972, Virology,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Isolation and partial characterization of apolipoprotein D: a new protein moiety of the human plasma lipoprotein system.
December 1973, FEBS letters,
E D Bekaert, and P Alaupovic, and C Knight-Gibson, and R A Norum, and M J Laux, and M Ayrault-Jarrier
Protein composition of Lp(a) lipoprotein from human plasma.
April 1983, FEBS letters,
Copied contents to your clipboard!