The abundance of additional N-acetyllactosamine units in N-linked tetraantennary oligosaccharides of human Tamm-Horsfall glycoprotein is a donor-specific feature

Rooijen, Johannes J.M. van; Kamerling, Johannis P.; Vliegenthart, Johannes F.G.

doi:10.1093/glycob/8.11.1065

Cited by 24 publications

(12 citation statements)

References 43 publications

(60 reference statements)

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“…A wide range of different kinds of terminal epitopes occurs, including minor Gal3S(β1-4)GlcNAc, GalNAc4S(β1-4), and Neu5Ac(α2-3)[GalNAc(β1-4)]Gal(β1-4)GlcNAc elements [28,30,31]. Depending on the donor, relative to the total carbohydrate content, 1-20% high-mannose-type N-linked glycans can be present.…”

Section: Tamm Horsfall Glycoprotein (Thp)mentioning

confidence: 99%

A lectin array-based methodology for the analysis of protein glycosylation

Rosenfeld¹,

Bangio²,

Gerwig³

et al. 2007

Journal of Biochemical and Biophysical Methods

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Glycosylation is the most versatile and one of the most abundant protein modifications. It has a structural role as well as diverse functional roles in many specific biological functions, including cancer development, viral and bacterial infections, and autoimmunity. The diverse roles of glycosylation in biological processes are rapidly growing areas of research, however, Glycobiology research is limited by the lack of a technology for rapid analysis of glycan composition of glycoproteins. Currently used methods for glycoanalysis are complex, typically requiring high levels of expertise and days to provide answers, and are not readily available to all researcher.We have developed a lectin array-based method, Qproteome™ GlycoArray kits, for rapid analysis of glycosylation profiles of glycoproteins. Glycoanalysis is performed on intact glycoproteins, requiring only 4-6 h for most analysis types. The method, demonstrated in this manuscript by several examples, is based on binding of an intact glycoprotein to the arrayed lectins, resulting in a characteristic fingerprint that is highly sensitive to changes in the protein's glycan composition. The large number of lectins, each with its specific recognition pattern, ensures high sensitivity to changes in the glycosylation pattern. A set of proprietary algorithms automatically interpret the fingerprint signals to provide a comprehensive glycan profile output.

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Section: Tamm Horsfall Glycoprotein (Thp)mentioning

confidence: 99%

A lectin array-based methodology for the analysis of protein glycosylation

Rosenfeld¹,

Bangio²,

Gerwig³

et al. 2007

Journal of Biochemical and Biophysical Methods

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“…Polylactosamine type sequences are also attached to some of the N-glycans associated with THP (28). However, this expression is a donor-specific feature not found on all samples of this glycoprotein (25).…”

Section: Discussionmentioning

confidence: 95%

Pregnancy-associated Changes in the Glycosylation of Tamm-Horsfall Glycoprotein

Easton¹,

Patankar²,

Clark³

et al. 2000

Journal of Biological Chemistry

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Tamm-Horsfall glycoprotein (THP) is a major glycoprotein associated with human urine that binds proinflammatory cytokines and also inhibits in vitro T cell proliferation induced by specific antigens. THP derived from human pregnancy urine (designated uromodulin) has previously been shown to be 13-fold more effective as an inhibitor of antigen-induced T cell proliferation than THP obtained from other sources. Structural analysis of human THP and uromodulin has for the first time revealed that these glycoproteins are O-glycosylated. THP from nonpregnant females and males expresses primarily core 1 type O-glycans terminated with either sialic acid or fucose but not the sialyl Lewis x epitope. By contrast, the O-glycans linked to uromodulin include unusual core 2 type glycans terminated with one, two, or three sialyl Lewis x sequences. The specific association of these unusual carbohydrate sequences with uromodulin could explain its enhanced immunomodulatory effects compared with THP obtained from males and nonpregnant females. Analysis of THP from one of the pregnant females 2 months postpartum showed a reversion of the O-glycan profile to that found for a nonpregnant female. These data suggest that the glycosylation state of uromodulin could be under the regulation of steroidal hormones produced during pregnancy. The significant physiological implications of these observations are discussed. Tamm-Horsfall glycoprotein (THP)1 is the most abundant glycoprotein in human urine (1, 2). The precise physiological role of THP remains enigmatic, despite considerable investigation of this glycoprotein over the past 50 years. THP was shown to block hemagglutination induced by influenza, mumps, and Newcastle disease viruses (1, 2). THP has been postulated to be essential for protecting the kidneys from bacterial infections (3, 4). THP has also been implicated as a potential component necessary for maintenance of the electrolyte balance in the nephron (5). In addition, THP may also play a significant role in several pathological conditions involving the kidney, including acute renal failure, urinary tract infection, stone formation, and interstitial nephritis (6).In 1973, two studies (7, 8) suggested that human chorionic gonadotropin isolated from pregnancy urine suppressed specific immune activities in vitro. However, this immunosuppressive activity turned out to be due to a contaminant of the human chorionic gonadotropin preparation (9, 10). Muchmore and Decker (11) later used lectin affinity chromatography, gel separation, and isoelectric focusing to purify a glycoprotein from human pregnancy urine that mediated this immunosuppressive activity. They designated this glycoprotein "uromodulin" to account for its origin and its immunomodulatory activities. Amino acid sequence analysis (12, 13) revealed that uromodulin represented THP glycoforms produced during pregnancy.Uromodulin was initially shown to inhibit antigen-induced T cell proliferation at relatively low concentrations (11). Subsequent investigations by Muchmore and ...

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“…The synthesis of the repeats and the structures of the oligosaccharides containing N-acetyllactosamine repeats have been extensively studied [25,27,42,43]. In N-linked oligosaccharides, the N-acetyllactosamine repeats are preferentially located on the complex multiantennary (>3) structures [25,28,31,32,43,44], although the repeats can occur in biantennary oligosaccharides [28,33,45]. In the N-linked oligosaccharides of glycoproteins from CHO cells, the preferred branching (from the two mannoses) for the N-acetyllactosamine repeats (3Gal b1±4Glc Nacb1) n is the 2,6-branched mannosyl residue, which links to the core-mannose through a1±6(core man)b1 linkage [27,46].…”

Section: Discussionmentioning

confidence: 99%

Structural characterization of oligosaccharides in recombinant soluble human interferon receptor 2 using fluorophore-assisted carbohydrate electrophoresis

Frado¹,

Strickler²

2000

Electrophoresis

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The N-linked oligosaccharide profiles (banding patterns in gels) and structures of recombinant soluble human interferon receptor 2 (r-shIFNAR2) were determined using fluorophore-assisted carbohydrate electrophoresis (FACE, Glyko, Novato, CA). The method involves releasing N-linked oligosaccharide moieties from a glycoprotein by digestion with peptide-N glycanase (PNGase F), labeling the released oligosaccharides with the fluorescent dye 8-aminonaphthalene-1,3,6-trisulfonate (ANTS), and separating the labeled oligosaccharides by gel electrophoresis. The isolated oligosaccharides in the bands from the profiling gels can then be sequenced using exoglycosidases to reveal the oligosaccharide structures. The oligosaccharide profile of r-shIFNAR2 consists of at least nine oligosaccharide bands. The relative amount of oligosaccharide in each band can vary, depending on the culture conditions of the source cells. FACE structural analysis shows that r-shIFNAR2 contains only core-fucosylated N-linked oligosaccharides, most of which are fully sialylated (approximately 92%). The major types and relative amounts of the oligosaccharides from a representative sample are: disialylated, galactosylated, biantennary (15%); trisialylated, galactosylated, triantennary (19%), tetrasialylated, galactosylated, tetraantennary (30%), and N-acetyllactosamine-containing higher-order oligosaccharides including tri-, tetra-, and pentaantennary (28%). The remaining oligosaccharides are not fully sialylated and/or not fully galactosylated di-, tri-, and tetraantennary structures (approximately 5%) and unidentified structures (approximately 3%). A method for determining the types and structures of the N-acetyllactosamine containing oligosaccharides is also reported in this study.

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The abundance of additional N-acetyllactosamine units in N-linked tetraantennary oligosaccharides of human Tamm-Horsfall glycoprotein is a donor-specific feature

Cited by 24 publications

References 43 publications

A lectin array-based methodology for the analysis of protein glycosylation

A lectin array-based methodology for the analysis of protein glycosylation

Pregnancy-associated Changes in the Glycosylation of Tamm-Horsfall Glycoprotein

Structural characterization of oligosaccharides in recombinant soluble human interferon receptor 2 using fluorophore-assisted carbohydrate electrophoresis

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