Structural Domains of Apolipoprotein(a) and Its Interaction with Apolipoprotein B-100 in the Lipoprotein(a) Particle

Biochemistry ◽  
1994 ◽  
Vol 33 (11) ◽  
pp. 3335-3341 ◽  
Author(s):  
Thierry Huby ◽  
Chantal Doucet ◽  
Hans Dieplinger ◽  
John Chapman ◽  
Joelle Thillet
Keyword(s):  
Apolipoprotein B ◽  
Structural Domains ◽  
Lipoprotein A ◽  
Apolipoprotein A

The unique lipoprotein(a): properties and immunochemical measurement

1990 ◽  
Vol 36 (12) ◽  
pp. 2019-2026 ◽  
Author(s):  
J J Albers ◽  
S M Marcovina ◽  
M S Lodge
Keyword(s):  
Rapid Development ◽  
Structural Complexity ◽  
Structural Domains ◽  
Lipoprotein A ◽  
Apolipoprotein A ◽  
High Amino Acid ◽  
Multiple Copies ◽  
High Concentrations ◽  
Size Heterogeneity ◽  
Genetically Determined

Abstract Lipoprotein (a) [Lp(a)] represents a class of lipoprotein particles defined by the presence of apolipoprotein(a), a unique glycoprotein linked by a disulfide bond to apolipoprotein B-100 to form a single macromolecule. Apolipoprotein(a) is formed by three different structural domains having high amino acid sequence homology with plasminogen. One of the domains, called kringle 4, is present in multiple copies, the number of which varies and is genetically determined. This accounts for the size heterogeneity of apolipoprotein(a) and thus of Lp(a). Because high concentrations of Lp(a) are associated with atherosclerotic cardiovascular and cerebrovascular disease and may inhibit fibrinolysis, interest in measuring Lp(a) has increased considerably, leading to a rapid development of commercially available immunoassays for the measurement of Lp(a) in human plasma. However, the immunochemical measurement of Lp(a) has several peculiar problems in addition to those encountered by the measurements of other apolipoproteins. The major problems that need to be carefully evaluated are (a) the structural complexity and heterogeneity of Lp(a), (b) the homology of apolipoprotein(a) with plasminogen, (c) the lack of standardization of the methods, and (d) the lack of a common means of expressing the Lp(a) values.

Mo-P4:282 Apolipoprotein A-1, apolipoprotein B and lipoprotein (A) levels at patients with ischemic stroke

2006 ◽  
Vol 7 (3) ◽  
pp. 108
Author(s):  
D. Agapakis ◽  
G. Ntaios ◽  
E. Massa ◽  
C. Savopoulos ◽  
G. Kaiafa ◽  
...  
Keyword(s):  
Ischemic Stroke ◽  
Apolipoprotein B ◽  
Lipoprotein A ◽  
Apolipoprotein A

The linkage with apolipoprotein (a) in lipoprotein (a) modifies the immunochemical and functional properties of apolipoprotein B

Biochemistry ◽  
1988 ◽  
Vol 27 (22) ◽  
pp. 8474-8481 ◽  
Author(s):  
Zbigniew Zawadzki ◽  
Francois Terce ◽  
Leo J. Seman ◽  
Richard T. Theolis ◽  
W. Carl Breckenridge ◽  
...  
Keyword(s):  
Functional Properties ◽  
Apolipoprotein B ◽  
Lipoprotein A ◽  
Apolipoprotein A

The Efficacy of Electroacupuncture Therapy for Weight Loss Changes Plasma Lipoprotein A, Apolipoprotein A and Apolipoprotein B Levels in Obese Women

2008 ◽  
Vol 36 (06) ◽  
pp. 1029-1039 ◽  
Author(s):  
Mehmet T. Cabioglu ◽  
Nimet Gündoǧan ◽  
Neyhan Ergene
Keyword(s):  
Weight Reduction ◽  
Apolipoprotein B ◽  
Plasma Lipoprotein ◽  
The Body ◽  
Control Group ◽  
Obese Women ◽  
Diet Restriction ◽  
Lipoprotein A ◽  
Apolipoprotein A ◽  
Placebo Acupuncture

In the present study, we aimed to investigate the effects of electroacupuncture treatment on lipoprotein A, apolipoprotein A and apolipoprotein B levels in obese subjects. Fifty-eight women were studied in 3 groups as follows: 1) Placebo acupuncture (n = 15; mean age = 41.47 ± 4.61, and mean body mass index {BMI} = 33.43 ± 3.10); 2) Electroacupuncture (EA) (n = 20; mean age = 40.55 ± 5.30, and BMI = 35.65 ± 3.84) and 3) Diet restriction groups (n = 23; mean age = 42.91 ± 4.02, and BMI = 34.78 ± 3.29). EA was performed using the ear points, Hungry, Shen Men and Stomach the body points, Hegu (LI 4), Quchi (LI 11), Tianshu (St 25), Zusanli (St 36), Neiting (St 44) and Taichong (Liv 3) for 20 days. Intragroup comparisons were made by using paired samples t-test whereas intergroup differences were investigated by the two-way variation analysis and LSD test. There was a 4.7% (p < 0.001) weight reduction in patients with electroacupuncture application, whereas patients in diet restriction had a 2.9% (p < 0.001) weight reduction. There were significant decreases in lipoprotein A (p < 0.05) and apolipoprotein B (p < 0.05) levels in the EA compared to the control group and no changes in apolipoprotein A levels was observed in EA, diet and placebo acupuncture groups. EA therapy may be a useful approach for the treatment of obesity for both losing weight and lowing the risk factors for cardiovascular disease associated with obesity, since this application may decrease the plasma lipoprotein A and apolipoprotein B levels.

Plasma concentration levels of apolipoprotein A-I, apolipoprotein B and lipoprotein (a) in Greenland Inuit (Eskimos)

1992 ◽  
Vol 231 (6) ◽  
pp. 623-625 ◽  
Author(s):  
L. U. GERDES ◽  
E. B. SCHMIDT ◽  
I. C. KLAUSEN ◽  
S. D. KRISTENSEN ◽  
E. ERNST ◽  
...  
Keyword(s):  
Plasma Concentration ◽  
Apolipoprotein B ◽  
Lipoprotein A ◽  
Apolipoprotein A ◽  
Concentration Levels

scholarly journals The apolipoprotein B3304–3317 peptide as an inhibitor of the lipoprotein (a):apolipoprotein B-containing lipoprotein interaction

1995 ◽  
Vol 307 (1) ◽  
pp. 17-22 ◽  
Author(s):  
V N Trieu ◽  
U Olsson ◽  
W J McConathy
Keyword(s):  
Coronary Artery Disease ◽  
Risk Factor ◽  
Coronary Artery ◽  
Binding Site ◽  
Apolipoprotein B ◽  
Proline Residue ◽  
Lipoprotein A ◽  
Apolipoprotein A ◽  
Artery Disease ◽  
Competitive Nature

Lipoprotein (a) [Lp(a)] is a risk factor for coronary artery disease. It is characterized by apolipoprotein (a) [apo(a)] disulphide linked to apolipoprotein B (apoB), by Cys4057 of apo(a) and possibly Cys3734 of apoB. We call this the covalent apo(a):apoB-Lp interaction, to distinguish it from the non-covalent Lp(a):apoB-Lp interaction, mediated by the proline-binding kringle-4-like domain(s) of Lp(a). The Lp(a):apoB-Lp interaction was inhibited by an apoB peptide spanning residues 3304-3317. This peptide was found by a computerized search for sites on apoB similar to the plasminogen's kringle-4-binding site of alpha 2-antiplasmin. It probably constitutes part of the Lp(a)-binding site on apoB because: (1) it corresponds to the alpha 2-antiplasmin minimum binding domain for plasminogen's kringle-4; (2) the competitive nature of inhibition [KI = (1.5 +/- 0.7) x 10(-4) M, n = 5] suggested that it and apoB-Lp bound to Lp(a) by the same mechanism at the same site; and (3) it specifically bound Lp(a) and not apoB-Lp, and the bound Lp(a) was dissociated by inhibitors of the Lp(a):apoB-Lp interaction, 6-aminohexanoic acid and L-proline. Inhibition was independent of its proline residue, suggesting that proline in the context of a peptide is not a ligand for the kringle(s) which mediated the binding of Lp(a) to apoB-Lp.

Quantification of lipoprotein(a) particles containing various apolipoprotein(a) isoforms by a monoclonal anti-apo(a) capture antibody and a polyclonal anti-apolipoprotein B detection antibody sandwich enzyme immunoassay

1993 ◽  
Vol 39 (7) ◽  
pp. 1382-1389 ◽  
Author(s):  
W C Taddei-Peters ◽  
B T Butman ◽  
G R Jones ◽  
T M Venetta ◽  
P F Macomber ◽  
...  
Keyword(s):  
Apolipoprotein B ◽  
Low Density Lipoprotein ◽  
Sandwich Elisa ◽  
Density Lipoprotein ◽  
Low Density ◽  
Linear Calibration ◽  
Lipoprotein A ◽  
Apolipoprotein A ◽  
Assay Format ◽  
Capture Antibody

Abstract A quantitative sandwich ELISA for lipoprotein(a) [Lp(a)], utilizing a monoclonal capture antibody that recognizes human and rhesus monkey apolipoprotein(a) [apo(a)] isoforms in combination with a polyclonal anti-apolipoprotein B-peroxidase conjugate was developed. This assay generates a linear calibration curve from 31.2 to 1000 mg/L, is highly reproducible (intra- and interassay CV of &lt; 5% and &lt; or = 12%, respectively), and shows no interference from plasminogen (1 g/L), low-density lipoprotein (6.00 g/L), triglycerides (27.00 g/L from chylomicrons and 10.00 g/L from very-low-density lipoprotein), hemoglobin (5 g/L), or bilirubin (30 mg/L). This assay format quantifies the concentration of Lp(a) on an equal molar basis regardless of apo(a) isoform. In contrast, a commercially available ELISA [Macra Lp(a)] method with a monoclonal anti-apo(a) capture antibody and a polyclonal anti-apo(a) conjugate was found to underestimate the Lp(a) concentrations of individuals with lower-M(r) apo(a) isoforms--whether quantifying the Lp(a) in plasma or the purified lipoprotein. This demonstrates the importance of assay format selection in quantifying Lp(a).

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