scholarly journals Clinical Significance of Serum Apolipoprotein H (β2-glycoprotein I) in NIDDM

1987 ◽  
Vol 15 (1) ◽  
pp. 241-247
Author(s):  
Kazunaga TAKAMATSU ◽  
Masui KAWADA ◽  
Tadashi SUEHIRO ◽  
Nobukazu YASUOKA ◽  
Kenzo YOSHIDA ◽  
...  
Keyword(s):  
Clinical Significance ◽  
Glycoprotein I ◽  
Apolipoprotein H

β 2 -Glycoprotein I (Apolipoprotein H) Modulates Uptake and Endocytosis Associated Chemiluminescence in Rat Kupffer Cells

2002 ◽  
Vol 36 (7) ◽  
pp. 741-747 ◽  
Author(s):  
L.F. Gomes ◽  
L.M. Gonçalves ◽  
F.L.A. Fonseca ◽  
C.M. Celli ◽  
L.A. Videla ◽  
...  
Keyword(s):  
Kupffer Cells ◽  
Glycoprotein I ◽  
Apolipoprotein H

Excretion of beta 2-glycoprotein I (apolipoprotein H) in renal tubular disease

1991 ◽  
Vol 37 (1) ◽  
pp. 74-77 ◽  
Author(s):  
A G W Norden ◽  
L M Fulcher ◽  
M Lapsley ◽  
F V Flynn
Keyword(s):  
Multiple Forms ◽  
Bence Jones Protein ◽  
Major Urinary Protein ◽  
Glycoprotein I ◽  
Apolipoprotein H ◽  
Beta 2 ◽  
Renal Tubular ◽  
Renal Tubular Disease ◽  
Urine Proteins ◽  
Tubular Proteins

Abstract beta 2-Glycoprotein I (beta 2GI) was identified as a major urinary protein excreted by patients with several renal tubular diseases, including adult Fanconi syndrome, nephrocalcinosis associated with autoimmune diseases, Lowe's syndrome, and Dent's disease (a familial renal tubular disease). Sixteen patients excreted between 2 and 40 mg of beta 2GI per millimole of creatinine. In contrast, 18 healthy controls had undetectable amounts of beta 2GI in urine. Isoelectric focusing followed by immunoblotting demonstrated multiple forms of beta 2GI with pls between 6.4 and 8.2. These pls are higher than for several other "tubular proteins"; beta 2GI may therefore be less retarded than more-anionic proteins by the glomerular charge-barrier. This could explain why large quantities of beta 2GI are excreted despite its relatively high molecular mass (50 kDa). Excretion of beta 2GI was easily demonstrated by routine electrophoresis of urine proteins. beta 2GI migrates in the beta-gamma region and may be confused with Bence Jones protein. beta 2GI is stable for at least two years in urine frozen at -25 degrees C.

β2-Glycoprotein I: Target Antigen for Autoantibodies in the ‘Antiphospholipid Syndrome’

Lupus ◽  
1996 ◽  
Vol 5 (5) ◽  
pp. 381-385 ◽  
Author(s):  
DA Kandiah ◽  
YH Sheng ◽  
SA Krilis
Keyword(s):  
Clinical Significance ◽  
Protein C ◽  
Binding Proteins ◽  
Protein S ◽  
Target Antigen ◽  
Major Protein ◽  
Neurological Sequelae ◽  
Foetal Loss ◽  
Lupus Anticoagulants ◽  
Glycoprotein I

‘Antiphospholipid’ (aPL) antibodies are of important clinical significance because of their association with thrombosis both arterial and venous, recurrent foetal loss, specific neurological sequelae like seizures and chorea, cardiac valvular abnormalities and thrombocytopenia.1 Traditionally these autoantibodies have been assayed using phospholipid (PL) dependent tests and are classified as lupus anticoagulants (LA) and anticardiolipin (aCL) antibodies based on the method of detection.2 The antibodies thus, had been thought to bind PLs but it has now become clear that the true antigens are PL-binding proteins. The major protein consistently found as the target antigen for these autoantibodies is β2-glycoprotein I (β2-GPI).3 Other candidate PL-binding proteins have also been investigated including prothrombin, protein C and protein S4 but thus far appear to play less important roles in the binding of these antibodies.

Crystallization and preliminary X-ray crystallographic studies on apolipoprotein H (β2-glycoprotein-I) from human plasma

1998 ◽  
Vol 54 (6) ◽  
pp. 1450-1452 ◽  
Author(s):  
Ajay Saxena ◽  
Anna Gries ◽  
Robert Schwarzenbacher ◽  
Gerhard M. Kostner ◽  
Peter Laggner ◽  
...  
Keyword(s):  
Human Plasma ◽  
Free Form ◽  
Data Sets ◽  
Asymmetric Unit ◽  
Orthorhombic Space Group ◽  
X Ray ◽  
Human Plasma Protein ◽  
Glycoprotein I ◽  
Apolipoprotein H ◽  
Cell Dimensions

Apolipoprotein-H (Apo-H, Mw ≃ 50 kDa) is a carbohydrate-rich human-plasma protein which exists in blood serum in the free form as well as distributed between several classes of lipoproteins. Single crystals of apo-H have been obtained and crystallographic data sets have been collected. The crystals belong to the orthorhombic space group C2221, with cell dimensions a = 158.47, b = 169.25, c = 113.28 Å (at 100 K). The data indicate that the crystallographic asymmetric unit contains one tetramer of the protein.

Genetic variation in the apolipoprotein H (β2-glycoprotein I) gene affects plasma apolipoprotein H concentrations

1999 ◽  
Vol 105 (1-2) ◽  
pp. 63-71 ◽  
Author(s):  
H. Mehdi ◽  
C.E. Aston ◽  
D.K. Sanghera ◽  
R.F. Hamman ◽  
M.I. Kamboh
Keyword(s):  
Genetic Variation ◽  
Glycoprotein I ◽  
Apolipoprotein H ◽  
Plasma Apolipoprotein ◽  
I Gene

Anti-β2-glycoprotein I Antibody: Specificity and Clinical Significance

Lupus ◽  
1996 ◽  
Vol 5 (5) ◽  
pp. 378-380 ◽  
Author(s):  
T Koike ◽  
E Matsuura
Keyword(s):  
Conformational Change ◽  
Clinical Significance ◽  
Clinical Course ◽  
Oxidized Ldl ◽  
Anticardiolipin Antibody ◽  
Antibody Specificity ◽  
Glycoprotein I ◽  
Cryptic Epitopes ◽  
Oxygen Atoms

Cardiolipin binding of IgG-class anticardiolipin antibody (aCL) depends on the existence of β2-glycoprotein I (β2-GPI). We developed an EIA system that enables detection of antibodies against β2-GPI, without the presence of cardiolipin. This system involves use of irradiated polystyrene plates, in which oxygen atoms are introduced onto the surfaces of the plates. β2-GPI bound to the surface of these plates is assumed to undergo a conformational change that exposes normally cryptic epitopes. Anti-β2-GPI antibody measured using this EIA system showed good correlation with aCL measured by conventional EIA methods and may prove useful in evaluating the risk of thrombosis and monitoring the clinical course in patients with SLE. Utilizing this EIA system and β2-GPI-deleted mutants, we found that the fourth domain of β2-GPI is involved in expression of one of the cryptic epitopes recognized by aCL. We also found that oxidized LDL are sequentially targeted by β2-GPI and aCL.

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