Human α 1-acid glycoprotein-exposed macrophages release interleukin 1 inhibitory activity

Bories, Phuong Nhi; Guenounou, Moncef; Féger, Jeanne; Kodari, E.; Agneray, J; Durand, Geneviève

doi:10.1016/0006-291x(87)90988-0

Cited by 30 publications

(15 citation statements)

References 14 publications

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“…It can be calculated, however, that the total amount of sialic acid per molecule of AGP-A is higher than of AGP-C, as a result of the increase in branching. This is in agreement with the higher sialic acid content of 'ConA-unreactive' (AGP-A) relative to 'ConA-reactive' AGP (AGP-B plus -C) as published by Durand and co-workers [29], and with the lower isoelectric point observed for AGP-A than for AGP-C by Wells et al [4].…”

Section: Variety Of Glycan Chains In Agp-a -B and -Csupporting

confidence: 91%

Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A

Bierhuizen

Wit

Govers

et al. 1988

European Journal of Biochemistry

115

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Human al-acid glycoprotein (AGP) was separated into a non-bound (AGP-A; 46%), a retarded (AGP-B; 39%) and a bound fraction (AGP-C; 150/,) using concanavalin A (ConA) -Sepharose chromatography. The apparent molecular masses, as determined by SDS-PAGE, of the three fractions were 43.5, 42.3 and 41.2 kDa, respectively.The occurrence of N-linked di-, tri-and tetraantennary glycans on these three molecular forms (AGP-A, -B, and -C) was studied by sequential lectin-affinity chromatography of the 14C-labelled glycopeptides. These were obtained by extensive pronase treatment followed by N-[14C]acetylation of the peptide moieties.The glycopeptides of AGP-A did not bind to ConA-Sepharose whereas for AGP-B and AGP-C 18% and 44%, respectively, of the glycopeptides were bound as diantennary structures. Glycopeptide fractions of all three forms of AGP which were not bound to ConA-Sepharose were shown to contain equal amounts of both tri-and tetraantennary glycans by chromatography with Phaseolus vulgaris leukoagglutinating lectin (L-PHA).With the assumption that each molecule contains five glycosylation sites, it could be shown that AGP-A contains no diantennary structures whereas AGP-B and AGP-C contain one and two diantennary structures, respectively. In addition each of the molecular forms contains equal amounts of tri-and tetraantennary structures on the remaining glycosylation sites. The results of this study, therefore, exclude a uniformity of glycan chains in the three molecular forms of AGP.The degree of sialylation of each of the molecular forms was investigated by chromatography on L-PHAagarose and Ricinus communis agglutinin-I -agarose both before and after desialylation of the glycopeptides. It was shown that about 90% of the biantennary glycans of both AGP-B and AGP-C were disialylated while the remainder were monosialylated. The degree of sialylation of the tri-and tetraantennary glycans was identical for the three molecular forms. In each case, one or more terminal galactose residues occurred on at least 20% of the tri-and 65% of the tetraantennary chains.It is suggested that the decrease in the exposure of galactose residues from AGP-A to AGP-C is related to the concomittant decrease in branching of the glycans of the three molecular forms. The relevance of these findings to studies on the function of AGP during inflammatory and liver diseases is discussed. Abbreviations. AGP, ccl-acid glycoprotein; ConA, concanavalin A; L-PHA, Phaseolus vulgaris leukoagglutinating lectin; RCAI, Ricinus communis agglutinin I; CO, LO, RO, non-retarded or nonbound, and Cn, Ln, Rn (n = 1-4) retarded or bound glycopeptide fractions on ConA-Sepharose, L-PHA-agarose and RCA,-agarose, respectively. The fraction names are sometimes used sequentially, e.g. COLlR3, which indicates the fraction of glycopeptides that was not bound on ConA-Sepharose but retarded sequentially on position L1 of L-PHA-agarose and bound on position R3 of RCAI-agarose. Use of the prefix 'a' denotes that the fraction is desialylated by mild acid hydrolysis. fini...

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Section: Variety Of Glycan Chains In Agp-a -B and -Csupporting

confidence: 91%

Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A

Bierhuizen

Wit

Govers

et al. 1988

European Journal of Biochemistry

115

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“…4,5 In the same time monocytes/macrophages tre ated with AGP release interleukin-1 inhibitory factor. 6,7 These data confirm the role of AGP as an element of cytokine network. Immunomodulating properties of AGP depend on microheterogeneity of carbohydrate chains.…”

Section: Introductionsupporting

confidence: 84%

Immunomodulating activities of a natural α₁ ‐acid glycoprotein and its carbohydrate chains attached to the Protein‐Free Polymer

Pukhalsky

Shyian

Калашникова

et al. 1998

Mediators of Inflammation

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Immunomodulating effects of a neoglycoconjugate created on the basis of alpha1-acid glycoprotein (AGP) carbohydrate chains and synthetic protein-free carrier have been investigated. It was demonstrated that this pseudo-AGP suppressed PHA- or anti-CD3 antibody-induced lymphocyte proliferation in a dose-dependent manner. Pseudo-AGP revealed a similar antiproliferative effect as the natural AGP samples. Stimulation of the LPS-induced proinflammatory cytokine production by mononuclear cells treated with both natural and pseudo-AGP has been also demonstrated. These data show that carbohydrate chains of AGP play a crucial role in the studied biological effect realization.

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“…For example con A-unreactive AGP (i.e. the tri-and the tetra-antennary isoforms) are more effective that the con A-reactive AGP (diantennary) glycoforms on the induction of inhibitors of IL-1 activity [149]. Moreover, the glycoforms containing the maximal number of diantennary chains stimulate the expression of LPS-induced production of TNF and IL-1 cytokines by mononuclear cells.…”

Section: Glycan Pattern Modification Of Agp During Diseasementioning

confidence: 98%

The Acute Phase Protein α1-Acid Glycoprotein: A Model for Altered Glycosylation During Diseases

Ceciliani¹,

Pocacqua²

2007

CPPS

192

200

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Glycosylation is one of the most important post-translational modifications of proteins, and has been widely acknowledged as one of the most important ways to modulate both protein function and lifespan. The acute phase proteins are a major group of serum proteins whose concentration is altered during various pathophysiological conditions. The aim of this paper is to review the structure and functions of the alpha1-acid glycoprotein (AGP). AGP belongs to the subfamily of immunocalins, a group of binding proteins that also have immunomodulatory functions. One of the most interesting features of AGP is that its glycosylation microheterogeneity can be modified during diseases. This aspect is particularly remarkable, since both the immunomodulatory and the binding properties of AGP strongly depend on its carbohydrate composition. For these reasons, AGP can be considered an outstanding model for the study of glycan pattern modification during diseases. This review is focused on the most recent studies on the occurrence of different glycoforms in plasma and tissues and how the appearance of different oligosaccharide patterns during systemic inflammation or diseases can influence AGP's biological functions. The first part of the review will describe the structure of AGP and the several biological functions identified so far for this protein. The second part will be devoted to the post-translational modifications of the oligosaccharides micro-heterogeneity of AGP caused by pathological states. A critical evaluation of the impact of different AGP glycoforms on both its transport and anti-inflammatory features, and how the modifications of the glycan pattern can be utilized in clinical biochemistry, is also discussed.

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Human α 1-acid glycoprotein-exposed macrophages release interleukin 1 inhibitory activity

Cited by 30 publications

References 14 publications

Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A

Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A

Immunomodulating activities of a natural α₁ ‐acid glycoprotein and its carbohydrate chains attached to the Protein‐Free Polymer

The Acute Phase Protein α1-Acid Glycoprotein: A Model for Altered Glycosylation During Diseases

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Human α 1-acid glycoprotein-exposed macrophages release interleukin 1 inhibitory activity

Cited by 30 publications

References 14 publications

Glycosylation of three molecular forms of human α1‐acid glycoprotein having different interactions with concanavalin A

Glycosylation of three molecular forms of human α1‐acid glycoprotein having different interactions with concanavalin A

Immunomodulating activities of a natural α1 ‐acid glycoprotein and its carbohydrate chains attached to the Protein‐Free Polymer

The Acute Phase Protein &#945;1-Acid Glycoprotein: A Model for Altered Glycosylation During Diseases

Contact Info

Product

Resources

About

Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A

Glycosylation of three molecular forms of human α₁‐acid glycoprotein having different interactions with concanavalin A

Immunomodulating activities of a natural α₁ ‐acid glycoprotein and its carbohydrate chains attached to the Protein‐Free Polymer

The Acute Phase Protein α1-Acid Glycoprotein: A Model for Altered Glycosylation During Diseases