Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02749 (beta2-glycoprotein I)
 836 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fifteen serum proteins were estimated by linear immunodiffusion in blood samples from children with acute hepatitis. Blood was drawn at the beginning of the disease and three weeks later. The results were compared with results obtained from a group of age-matched normal children. At the beginning of the disease prealbumin and beta-2-glycoprotein I were depressed, whereas alpha-1-acid-glycoprotein, alpha-1-antitrypsin, cerloplasmin and alpha-2-HS-glycoprotein were found to be elevated. Alpha-2-macroglobulin, transferrin and beta-lipoprotein showed a significant elevation after three weeks. Beta-1-A/C, IgM and IgG remain elevated during time of observation. Albumin, haptoglobin and IgA were similar in patients and controls and did not change during the period of observation.
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PMID:Quantitative determination of single serum proteins during acute hepatitis in childhood. 7 48

The synthesis of various products by a human mammary cell line (BT 20) was studied by incorporation of 14C-labeled amino acids, choline, glucosamine, or galactosamine into nondialyzable materials. These products had molecular weights ranging from less than 12,300 daltons to more than 200,000 daltons. They were analyzed by immunoelectrophoresis and double diffusion in agar. Among the synthesized products, the following proteins were identified: beta2-glycoprotein I, alpha2HS-glycoprotein, alpha2-lipoprotein, actin, beta2-microglobulin, carcinoembryonic antigen, three oncofetal-associated antigens, and various erythrocyte membrane-associated antigens (namely, glycophorin). Synthesis of milk proteins was not detectable. Only the protein moiety of the glycophorin molecule seemed to be synthesized. The beta2-microglobulin was synthesized in an unbound state as well as bound to a glycoprotein whose relationship with the transplantation or tumor antigens must be determined. The three oncofetal-associated antigens were also synthesized in vitro by human fetal tissues and neoplastic and dysplastic human mammary tissues.
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PMID:Antigens of a human breast carcinoma cell line (BT 20). I. Synthesis of serum proteins, membrane-associated antigens, and oncofetal-associated antigens. 35 46

A serum protein named agglutinin is able to induce mitochondria to agglutinate. The protein has been purified from human serum by chromatography on DE-52. Sephadex G-200 and immunoglobulin-Sepharose 4B columns. Agglutinin is a glycoprotein that migrates electrophoretically as a gamma-globulin. Its molecular weight was determined to be 50,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Monospecific antiserum prepared against the agglutinin was found to be identical with anti-beta 2-glycoprotein I and agglutinating activity could be adsorbed on anti-beta 2-glycoprotein I-Sepharose 4B columns. Thus, the agglutinin has been identified as beta 2-glycoprotein I. The reaction between mitochondria and agglutinin shows positive cooperativity, which is independent on the stage of purification of agglutinin. The agglutinating activity could be diminished (inhibited) by acidic non-soluble lipids such as oleic acid, phosphatidic acid, phosphatidyl serine and phosphatidyl inositol.
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PMID:Purification, characterization and identification of an agglutinin in human serum. 53 52

In 92 patients with multiple myeloma and IgG monoclonal proteinemia concentrations of seventeen different serum proteins were specifically determined. Prealbumin, albumin, alpha, HS-glycoprotein, alpha-macroglobulin, transferrin and immunoglobulins IgA, IgM and IgD were significantly decreased in patients with IgG myeloma. On the contrary the means found for the typical acute phase proteins i.e. haptoglobin, orosomucoid and CRP were significantly elevated. No significant differences were demonstrated for less typical acute phase protients, i.e. alpha1-antitrypsin, ceruloplasmin and C3-component as well as for hemopexin and beta2-glycoprotein I. CRP values were strongly elevated in some sera, however in majority of patients they were within the normal limits. Negative correlation was found between monoclonal IgG and the most of the studied proteins inclusive immunoglobulins IgA, IgM and IgD. No correlation was demonstrated between the monoclonal IgG and the triad of typical acute phase proteins. Positive correlation was found between monoclonal IgG and the total serum protein and further among the proteins negatively correlated with monoclonal IgG as well as among the individual acute phase proteins. Explanation of the correlations reported has been suggested.
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PMID:Individual serum proteins and acute phase reactants in monoclonal immunoglobulinopathies (a study in patients with IgG myeloma). 64 23

Anions with strong electro-negative charges, like sulphuric esters of polysaccharides (heparin, dextran sulphate M.W. 15 00), the sodium salt of polyanethol sulfonic acid (liquoid, Roche), anionic detergents (sodium dodecylsulphate, sodium oleate, sodium deoxycholate), and the sodium salt of phosphotungstic acid were added to human serum or citrated plasma. For each compound several final concentrations were adopted, the highest being 4%. By using microimmunoelectrophoresis and numerous specific antisera against human plasma proteins, it was demonstrated that at pH 8.60 anions increase electrophoretic mobility of the following antigens: lipoproteins alpha and beta; fibrinogen; beta 2-glycoprotein I; beta 2-glycoprotein II ; antithrombin III. All reagents utilized do not react with all these proteins; for instance, only detergents accelerate the migration rate of a lipoproteins. Besides, depending on the protein, this or that reagent may be the most active. Thus, in the polysulphate group, heparin has the highest affinity for antithrombin III, liquoid for fibrinogen and dextran sulphate for beta 2-glycoprotein I.
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PMID:[Polysulfates, anionic detergents, sodium phosphotungstate and electrophoretic mobility of plasmatic proteins]. 67 30

Analyses of mucoproteins, orcin-positive protein sugar, sialic acid of the alpha2-macroglobulin, alpha1-glycoprotein, alpha1-antitrypsin, alpha2-HS-glycoprotein and beta2-glycoprotein I were carried out in 302 diabetics. In creases of concentration could be proved for alpha2-macroglobulin, alpha2-HS-glycoprotein, orcin-positive protein sugar and sialic acid. In diabetics with retinopathies the alpha2-macroglobulin concentration is significantly increased compared with diabetics without retinopathies.
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PMID:[Glycoproteins in diabetes mellitus]. 108 92

Beta 2-GPI is a single chain, 50 kd glycoprotein made up of 326 amino-acids, present in human plasma at concentrations of about 200 micrograms/ml. It has been shown to represent the "serum cofactor" important in determining the binding of aCL to phospholipids both in fluid and in solid phase assays. Its cofactor activity is demonstrable for aPL antibodies from patients with autoimmune but not with infectious diseases. It is immunogenic in heterospecific models, and immunization with beta 2-GPI seems to be able to induce the production not only of anti-beta 2-GPI but also of aPL antibodies. Most probably its binding to CL changes the configuration of phospholipids to a more immunogenic one. The various characteristics of beta 2-GPI are summarized in Table I. beta 2-GPI has been recognized as a natural anticoagulant protein, but its possible role in the pathogenesis of the APLS remains to be determined.
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PMID:The beta-2-glycoprotein I and antiphospholipid antibodies. 150 19

The clinical and serological features of 38 aCL-positive patients were compared to those of 45 aCL-negative patients. A significantly higher incidence of thrombophlebitis and livedo reticularis was found in aCL-positive patients. There were 13 aCL positive patients with thrombophlebitis and/or arterial thromboses and these 13 patients were designated as having the antiphospholipid syndrome (APS) while the remaining 70 patients were diagnosed as having Systemic Lupus Erythematosus (SLE). APS patients also had a high incidence of arterial occlusions, recurrent abortions and strokes compared to SLE patients. Patients with high levels of IgG-aCL were more likely to have APS, while patients with low levels of IgG-aCL or IgM-aCL only were more likely to have SLE without the clinical features of APS. Since aCL antibodies have recently been shown to interact with a phospholipid-binding plasma protein beta 2-glycoprotein-I (beta 2-GPI), we measured the beta 2-GPI levels in these patients and found that beta 2-GPI levels are significantly higher in APS compared to SLE patients negative for aCL antibodies. Since beta 2-GPI is known to exert multiple effects on coagulation processes the interaction of aCL antibodies with this glycoprotein may play a pathogenic role in APS.
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PMID:Patients with anticardiolipin antibodies with and without antiphospholipid syndrome: their clinical features and beta 2-glycoprotein-I plasma levels. 151 96

Autoimmune aPL are associated with a well-defined clinical syndrome of vascular thromboses, recurrent fetal loss, thrombocytopenia, livedo reticularis, and valvular and neurologic abnormalities. A clinical diagnosis of SLE need not be present, and aPL syndrome in the absence of other well-defined autoimmune disease is termed PAPS. A positive test for aPL is defined by enzyme-linked immunoassay (aCL) or by functional coagulation assay (LAC). Anticardiolipin antibody and LAC are similar but probably not identical antibodies. The false-positive test for syphilis is less closely associated with clinical complications than are aCL and LAC. The mechanism of action of aPL is not yet known, although many theories have been advanced. Recent identification of beta 2-glycoprotein I, a serum glycoprotein, as an aPL cofactor suggests that inhibition of this protein's anticoagulant activity may be important. Autoimmune aPL differ from infection-induced aPL in important antibody characteristics, including IgG subclass, light chain preference, antibody avidity, and cofactor requirement. Both recognize negatively charged phospholipids, but various physical characteristics of the phospholipids alter the recognition patterns. Treatment of the aPL syndrome is not well defined. Anticoagulation with heparin, coumadin, or aspirin are currently widely used. Although corticosteroid, immunosuppressive therapy, and plasmapheresis may be used for severe, fulminant thrombosis, the efficacy of this treatment has yet to be proved.
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PMID:Antiphospholipid antibody syndrome. 156 40

C-reactive protein (CRP) is thought to play an important role in immunomodulation. The exact biologic function of this pentraxin protein is, however, still unclear. Here we report experiments designed to further characterize the binding properties of CRP. Using purified human CRP it could be shown that CRP immobilized onto polystyrene surfaces or onto latex beads binds distinct plasma glycoproteins including IgG, asialofetuin, asialo-beta 2-glycoprotein I and, likewise, synthetic glycoproteins as a lectin, exhibiting binding specificity for terminal galactosyl residues of the glycoprotein glycans. Binding of CRP to IgA, IgM, IgG, asialofetuin, asialo-beta 2-glycoprotein I and to synthetic glycoproteins requires immobilization onto surfaces of both CRP and the ligand. Fibronectin and fibrinogen are bound by surface-immobilized CRP also in soluble phase. Comparing various mono-, di-, and trisaccharides as competitive inhibitors of the lectin binding activity of CRP, only beta-D-Gal-(1-3)-D-GalNAc, beta-D-Gal-(1-4)-D-GalNAc, and beta-D-Gal-(1-4)-beta-D-Gal-(1-4)-D-GlcNAc had significant inhibitory power at a concentration of 8 mmol/liter. Binding activity of CRP was pH-dependent with an optimum at pH 5 to 6 and was reduced by 90% when pH was shifted from 6 to the physiologic pH value of 7.4. CRP exhibited lectin-like properties with binding specificity for galactosyl residues also when bound to K-562 erythroleukemia cells. It is therefore suggested that CRP immobilized onto surfaces exhibits lectin activity toward galactosyl groups preferentially in a mildly acidic environment as present at sites of inflammation.
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PMID:Lectin specificity and binding characteristics of human C-reactive protein. 162 92


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