Glycosylation of .ALPHA.1-Acid Glycoprotein(Orosomucoid) in Health and Disease: Occurrence, Regulation and Possible Funtional Implications.

Dijk, W. van; Linden, Els C.M. Brinkman-Van der; Havenaar, Ellen C.

doi:10.4052/tigg.10.235

Cited by 44 publications

(34 citation statements)

References 7 publications

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“…[43]). A masking effect of selectins was already proposed for the strongly fucosylated and sialyl Lewis X -containing AGP glycoform present in acute-phase plasma [12,13]. Indeed, studies in an ischemiareperfusion model in rats support this notion [14].…”

Section: Discussionsupporting

confidence: 61%

“…A minor fraction of AGP was detected at 41-43 kD, the apparent molecular weight generally found for human plasma AGP (Fig. 1) [10,13]. Both AGP variants appeared to be present as soluble proteins in PMN, as they were recovered almost completely in the 100,000 g supernatant of cells that were lysed by repeated freezing and thawing (Fig.…”

Section: Characteristics Of Pmn Agpmentioning

confidence: 94%

“…The hepatic acute-phase response induces an increased ␣3-fucosylation of these glycans, resulting in the occurrence of AGP glycoforms rich in sialyl Lewis x groups in plasma during inflammation [12]. It is interesting that these AGP glycoforms, by binding to E-selectin [13] and by amelioration of complement-induced damage [14], possibly counteract the influx of PMN in inflamed tissue.…”

Section: Introductionmentioning

confidence: 99%

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Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Poland¹,

Vallejo²,

Niessen

et al. 2005

Journal of Leukocyte Biology

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␣ 1 -Acid glycoprotein (AGP) is a major acute-phase protein present in human plasma as well as in polymorphonuclear leukocytes (PMN). In this report, we show that PMN synthesize a specific glycoform of AGP, which is stored in the specific and azurophilic granules. Activation of PMN results in the rapid release of soluble AGP. PMN AGP exhibits a substantially higher apparent molecular weight than plasma AGP (50 -60 kD vs. 40 -43 kD), owing to the presence of strongly fucosylated and sialylated polylactosamine units on its five Nlinked glycans. PMN AGP is also released in vivo from activated PMN, as appeared from studies using well-characterized myocard slices of patients that had died within 2 weeks after an acute myocardial infarction. AGP was found deposited transiently on damaged cardiomyocytes in areas with infiltrating PMN only. It is interesting that this was inversely related to the deposition of activated complement C3. Strongly fucosylated and sialylated AGP glycoforms have the ability to bind to E-selectin and to inhibit complement activation. We suggest that AGP glycoforms in PMN provide an endogenous feedback-inhibitory response to excessive inflammation. J. Leukoc. Biol. 78: 453-461; 2005.

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Section: Discussionsupporting

confidence: 61%

Section: Characteristics Of Pmn Agpmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 99%

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Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Poland¹,

Vallejo²,

Niessen

et al. 2005

Journal of Leukocyte Biology

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“…Acute phase reaction may lead to other alterations than concentration changes in heavily glycosylated proteins such as AGP, for example changes in glycan composition as shown for AGP in other species [32,33]. To the best of our knowledge, only one paper is available reporting the differences in glycosylation patterns of boAGP from bovines of different ages [14] and this aspect should be investigated further.…”

Section: Discussionmentioning

confidence: 99%

Identification of the bovine α1-acid glycoprotein in colostrum and milk

et al. 2005

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-α1-acid glycoprotein (AGP) is an immunomodulatory protein expressed by hepatocytes in response to the systemic reaction that follows tissue damage caused by inflammation, infection or trauma. This paper presents the detection of bovine AGP (boAGP) in mammary secretions (colostrum and milk) and mammary gland tissue. Bovine AGP was detected by Western blotting in all the samples analysed, and could be quantified in colostrum at 162 (± 63.7) µg/mL and 114.5 (± 67.8) µg/mL during the first 12 h and 24 h respectively. In mature milk, the boAGP concentration clearly decreased and was no longer detectable using the Radial Immunodiffusion (RID) technique. The concentration of mature milk boAGP was therefore semi-quantified using an anion-exchange chromatographic procedure that allowed the concentration of the protein to be determined. The presence of AGP in bovine milk was confirmed by the internal sequence analysis performed following purification to homogeneity of the protein from milk. The concentration of AGP in bovine milk with low SCC (< 250 000) was very similar to that from bovine milk with high SCC (> 250 000). In order to investigate the origin of AGP in bovine milk, a search for mRNA was carried out in somatic cells and mammary gland tissue: mRNA expression of the boAGP gene was detected in mammary gland tissue, but not in somatic cells. Finally, the cDNA sequence of the boAGP was determined, and is hereby presented. α1-acid glycoprotein / mastitis / colostrum / milk

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“…[13][14][15] The glycans of AGP are reported to influence its biological activities and to modulate cell-to-cell interactions and cellular signaling. 9,17 During the inflammatory process the sialylated and fucosylated glycotopes of AGP are reported to be involved in anti-inflammatory and immunomodulatory reactions. Van Dijk et al 17 have suggested that AGP molecules carrying sialyl-Lewis x glycotopes may interfere with leukocyteendothelial interactions by binding to E-or P-selectin and possess anti-inflammatory properties.…”

Section: Introductionmentioning

confidence: 99%

Lactation Stage-Related Expression of Sialylated and Fucosylated Glycotopes of Human Milk α-1-Acid Glycoprotein

Orczyk-Pawiłowicz

Hirnle

Berghausen-Mazur

et al. 2014

Breastfeeding Medicine

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Background: Because terminal sugars of a-1-acid glycoprotein (AGP) are reported to be involved in antiinflammatory and immunomodulatory processes, their expressions might have an influence on the proper function of immune system of newborns. Here, relative amounts of sialylated and fucosylated glycotopes on human milk AGP over normal lactation were investigated. Materials and Methods: AGP concentration and relative amounts of its sialylated and fucosylated glycovariants were analyzed in early colostrum, colostrum, and transitional and mature milk samples of 127 healthy mothers by lectin-AGP enzyme-linked immunosorbent assay using a2,3-and a2,6-sialic acid and a1,2-, a1,3-, and a1,6-fucose specific biotinylated Maackia amurensis, Sambucus nigra, Ulex europaeus, Tetragonolobus purpureus, and Lens culinaris lectins, respectively. Results: AGP concentration in human milk was about 30 times lower than in plasma of lactating mothers and decreased gradually over lactation. Milk AGP showed significantly higher expression of sialylated and fucosylated glycotopes in comparison with those of plasma AGP. Milk AGP glycovariants containing a2,6-sialylated and a1,6-and a1,2-fucosylated glycotopes showed the highest relative amounts in early colostrums. With progression of lactation, the expressions of glycotopes a1,2-fucosylated decreased starting from Day 4 and those of a2,6-sialylated and a1,6-fucosylated from Day 8 of lactation, whereas the level of a2,3-sialyl-glycotope was almost constant over 45 days of lactation. In contrast, the expression of a1,3-linked fucose on AGP was low in colostrums and significantly higher in transitional and mature milk. Conclusions: The relative amounts of sialylated and fucosylated glycovariants of human hindmilk AGP significantly varied between Days 2 and 45 of normal lactation.

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Glycosylation of .ALPHA.1-Acid Glycoprotein(Orosomucoid) in Health and Disease: Occurrence, Regulation and Possible Funtional Implications.

Cited by 44 publications

References 7 publications

Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Activated human PMN synthesize and release a strongly fucosylated glycoform of α1-acid glycoprotein, which is transiently deposited in human myocardial infarction

Identification of the bovine α1-acid glycoprotein in colostrum and milk

Lactation Stage-Related Expression of Sialylated and Fucosylated Glycotopes of Human Milk α-1-Acid Glycoprotein

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