[38] α1-Acid glycoprotein

Arnaúd, Philippe; Miribel, Laurent; Roux, Anne Françoise

doi:10.1016/0076-6879(88)63040-0

Cited by 12 publications

(7 citation statements)

References 53 publications

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“…The lipocalin AGP (or orosomucoid) is an abundant plasma protein [105,106]. It is a positive APP ; after induction by turpentine injection, AGP becomes one of the dominant proteins expressed by the liver and is known to accumulate at sites of inflammation.…”

Section: Immune Modulationmentioning

confidence: 99%

“…AGP has shown many immunoregulatory properties : the ability to inhibit platelet aggregation [107], an involvement in wound healing (possibly through its interaction with collagen), the inhibition of neutrophil activation, inhibition of phagocytosis, and it possesses non-specific immunosuppressive properties [105,108]. AGP has an unusually high carbohydrate content of 40 % and is consequently unusually acidic and soluble [106] ; several studies show that the deglycosylated protein demonstrates little or none of AGP's immunosuppressive properties. The characteristic glycosylation of AGP changes during the acute-phase response, with concomitant effects on its immunomodulatory properties : for example acute inflammation leads to a large increase in sialyl-Lewis-X-substituted AGP, which may inhibit selectin-mediated granulocyte invasion of inflamed endothelium [109].…”

Section: Immune Modulationmentioning

confidence: 99%

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The lipocalin protein family: structure and function

Flower¹

1996

Biochemical Journal

1,541

1,278

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The lipocalin protein family is a large group of small extracellular proteins. The family demonstrates great diversity at the sequence level ; however, most lipocalins share three characteristic conserved sequence motifs, the kernel lipocalins, while a group of more divergent family members, the outlier lipocalins, share only one. Belying this sequence dissimilarity, lipocalin crystal structures are highly conserved and comprise a single eight-stranded continuously hydrogen-bonded antiparallel β-barrel, which encloses an internal ligand-binding site. Together with two other families of ligand-binding proteins, the fatty-acid-binding proteins (FABPs) and the avidins, the lipocalins form part of an overall structural superfamily : the calycins. Members of the lipocalin family are characterized by several common molecular-

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Section: Immune Modulationmentioning

confidence: 99%

Section: Immune Modulationmentioning

confidence: 99%

The lipocalin protein family: structure and function

Flower¹

1996

Biochemical Journal

1,541

1,278

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“…disease had higher ovacid glycoprotein concentrations than all other groups (P < 0.01); patients with hepatocellular carcinoma had higher concentrations than cirrhotics (P < 0.01) (Bonferronfs test for pairwise comparisons). Table 2 shows the results of the multiple regression analysis, taking serum o^-acid glycoprotein as the dependent variable, and C-reactive protein, oci-antiproteinase, cholinesterase, 1 ) γ-glutamyltransferase 1 ) and iron serum concentrations as predictor variables. The analysis was performed for the subjects as a single collective, as well as by groups.…”

Section: Discussionmentioning

confidence: 99%

“…It has a relative molecular mass of about 41000 and is characterized by the presence of five glycosylation sites (1,2). a r Acid glycoprotein has long been recognized as an acute phase reactant (3).…”

Section: Introductionmentioning

confidence: 99%

Increase of Serum α1-Acid Glycoprotein Despite the Decline of Liver Synthetic Function in Cirrhotics with Hepatocellular Carcinoma

Falleti¹,

Pirisi²,

Fabris³

et al. 1993

Clinical Chemistry and Laboratory Medicine

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Summary: α,-Acid glycoprotein, an acute phase reactant synthesised by the liver, has been reported to be increased in neoplastic conditions and reduced in chronic liver disease. We measured serum a r acid glycoprotein by a nephelometric method in 186 subjects (112 males, 74 females): 55 had mild chronic liver disease (chronic hepatitis and steatofibrosis), 45 cirrhosis, 38 hepatocellular carcinoma, 15 extra-hepatic malignant disease; 33 healthy subjects were used as controls. Analysis of variance demonstrated a significant variability among groups (F = 17.08, P = 0.0000). Higher concentrations of ocj-acid glycoprotein were detected in malignant extra-hepatic disease than in all other groups (P < 0.01); concentrations of o^-acid glycoprotein were higher in hepatocellular carcinoma than in cirrhosis (P < 0.01). Multiple regression analysis by groups (dependent variable = αϊ-acid glycoprotein; group 1 = mild chronic liver disease + cirrhosis; group 2 = hepatocellular carcinoma) showed a significant correlation for both group 1 (r = 0.6264, F = 8.005, P = 0.0000) and group 2 (r = 0.8947, F = 13.643, P = 0.0000). The significant standardised regression coefficients were: cholinesterase, C-reactive protein, γ-glutamyltransferase and iron (negative) for regression upon group 1; C-reactive protein, aj-antiproteinase, γ-glutamyltransferase, iron (negative) for regression upon group 2. A difference between the 2 regression equation coefficients was detected (F = 5.209, P = 0.0002). In conclusion, a raised a r acid glycoprotein concentration was found in patients with malignancies, both hepatic and extra-hepatic; however, patients with hepatocellular carcinoma had a lower aj-acid glycoprotein concentration than patients with malignant extra-hepatic disease. In hepatocellular carcinoma, a good correlation existed between a r acid glycoprotein and other serum indices of the acute phase response. In some patients with hepatocellular carcinoma, a t -acid glycoprotein was increased, despite the decrease of liver function.

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“…AGP belongs to the class of acute phase proteins that are known to be induced in the liver in response to a wide variety of physiological stresses, including inflammation, infection, pregnancy, and malignancy (22,23). It is distinct from other serum proteins by its high carbohydrate content (over 40% by weight) and high acidity.…”

Section: Discussionmentioning

confidence: 99%

Binding of thalidomide to alpha1-acid glycoprotein may be involved in its inhibition of tumor necrosis factor alpha production.

Turk

Jiang

Liu

1996

Proc. Natl. Acad. Sci. U.S.A.

111

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In addition to its well known sedative and teratogenic effects, thalidomide also possesses potent immunomodulatory and antiinflammatory activities, being most effective against leprosy and chronic graft-versus-host disease. The immunomodulatory activity of thalidomide has been ascribed to the selective inhibition of tumor necrosis factor ai from monocytes. The molecular mechanism for the immunomodulatory effect of thalidomide remains unknown. To elucidate this mechanism, we synthesized an active photoaffinity label of thalidomide as a probe to identify the molecular target of the drug. Using the probe, we specifically labeled a pair of proteins of 43-45 kDa with high acidity from bovine thymus extract. Purification of these proteins and partial peptide sequence determination revealed them to be al-acid glycoprotein (AGP). We show that the binding of thalidomide photoaffinity label to authentic human AGP is competed with both thalidomide and the nonradioactive photoaffinity label at concentrations comparable to those required for inhibition of production oftumor necrosis factor a from human monocytes, suggesting that AGP may be involved in the immunomodulatory activity of thalidomide.Thalidomide has a relatively simple chemical architecture (Fig.

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[38] α1-Acid glycoprotein

Cited by 12 publications

References 53 publications

The lipocalin protein family: structure and function

The lipocalin protein family: structure and function

Increase of Serum α1-Acid Glycoprotein Despite the Decline of Liver Synthetic Function in Cirrhotics with Hepatocellular Carcinoma

Binding of thalidomide to alpha1-acid glycoprotein may be involved in its inhibition of tumor necrosis factor alpha production.

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