Structural studies on the carbohydrate portion of fetuin.

Nilsson, Bo; Nordén, Nils E.; Svensson, Sigfrid

doi:10.1016/s0021-9258(17)30046-7

Cited by 341 publications

(41 citation statements)

References 15 publications

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“…20 For the Fet 'parent' glycoform, these structures are all sialylated to different degrees. [19][20][21] (Fig. 1) Fet desialylated by mild acid hydrolysis (ASFA) was included in the glycoform group to demonstrate characteristics of a completely desialylated glycoform.…”

Section: Glycoform Generationmentioning

confidence: 99%

“…[16][17][18] Bovine fetuin (Fet) is a well-characterized model glycoprotein which typically has three asparagines modied with complextype N-linked glycans and at least three serine or threanine residues modifed with O-linked oligosaccharides of either core type 1 or core type 2. [19][20][21] Both the N-and O-linked structures are normally terminated with sialic acid (N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc)) in either a(2 / 3) or a(2 / 6) linkages (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

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Microarray evaluation of the effects of lectin and glycoprotein orientation and data filtering on glycoform discrimination

2014

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Silver stain visualization of SDS-PAGE mass shifts resulting from removal of monosaccharide constituents of bovine fetuin (Fet). Lines indicate uppermost position of each glycoform relative to the M r standards. Fet (Fet, Lane 1). Products of 5 h incubation of Fet with Vibrio cholerae sialidase (ASFE, Lane 2) or sialidase and bovine testes β-galactosidase combined (ASGF, Lane 3). Asialofetuin produced by acid hydrolysis of sialic acid termini (ASFA, Lane 4). Approximately 1 μg of each glycoform loaded per well (by Bradford estimation).

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Section: Glycoform Generationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Microarray evaluation of the effects of lectin and glycoprotein orientation and data filtering on glycoform discrimination

2014

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“…The recombinant enzyme efficiently mediated the transfer of sialic acid residues to O-linked oligosaccharides of fetuin (Table 1), which is known to contain three core 1 O-linked oligosaccharides, one of them being a disialylated tetrasaccharide, Neu5Acα2-3Galβ1-3[Neu5Acα2-6]GalNAc, and the other two the monosialylated trisaccharide Neu5Acα2-3Galβ1-3GalNAc [33]. The two GalNAc residues of native fetuin unsubstituted in position-6 can therefore serve as an acceptor for hST6GalNAc IV.…”

Section: Table 2 Determination Of the Kinetic Parameters Of Hst6galnac IVmentioning

confidence: 99%

Cloning, expression and gene organization of a human Neu5Acα2‒3Galβ1‒3GalNAc α2,6-sialyltransferase: hST6GalNAc IV

et al. 2000

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On the basis of the detection of expressed sequence tag ('EST') similar to the rat N-acetylgalactosamine alpha2,6-sialyltransferase (ST6GalNAc) III cDNA, we have identified a novel member of the human ST6GalNAc family. We have isolated a cDNA clone containing an open reading frame that codes for a type II membrane protein of 302 amino acids with a seven-amino-acid cytoplasmic domain, an 18-amino-acid transmembrane domain and the smallest described catalytic domain of 277 amino acids. This predicted sialyltransferase sequence is similar to the rat ST6GalNAc III (46.6%), but was found to be even more similar to the recently reported mouse ST6GalNAc IV (88.1%) on the basis of amino acid sequence identity. Northern-blot analysis showed that the newly identified gene is expressed constitutively in various adult human tissues as a 2.2kb transcript, but was also found to be expressed at lower levels in brain, heart and skeletal muscle as a 2.5kb transcript. Expression of the hST6GalNAc IV gene was investigated by reverse transcription PCR in various human cancer cells, and was found to be present in the majority of cell types with the exception of the carcinoma cell line T47D and pro-monocyte THP cells. The transient expression in COS-7 cells of the full-length cDNA led to the production of an active enzyme sharing the acceptor specificity of the ST6GalNAc family towards Neu5Ac alpha 2-3Gal beta 1-3GalNAc alpha-O-R (where 'R' denotes H, benzyl, or a peptidic chain). Detailed analysis in vitro of substrate specificity revealed that the enzyme required the trisaccharide Neu5Ac alpha 2-3Gal beta1-3GalNAc found on O-glycans and arylglycosides. In addition, we have clarified the genomic organization of ST6GalNAc IV gene.

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“…Fetuin contains 3 N-linked glycosylation sites (at 81Asn, 138Asn, and 158Asn) and at least 3 O-linked glycosylation sites [58]. The structures of both the D-linked [59,60] and N-linked oligosaccharides attached to fetuin have been extensively studied [61,62,63,64,65]. The N-linked glycosylation sites cannot be isolated into convenient small glycopeptides by digestion with trypsin alone; therefore, a subsequent digestion with Staph.…”

Section: Screening For Glycopeptides In Proteolytic Digest Mixtures Of Glycoproteins By Lc/cid/msmentioning

confidence: 99%

The determination of glycopeptides by liquid chromatography/mass spectrometry with collision-induced dissociation

Conboy

Henion

1992

J. Am. Soc. Mass Spectrom.

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Glycopeptides derived from ribonuclease B and ovomucoid have been subjected to collisioninduced dissociation (CID) in the second quadrupole of a triple quadrupole mass spectrometer. Doubly charged parent ions gave predictable fragmentation that yielded partial sequence information of the attached oligosaccharide as Hex and HexNAc units. Common oxonium ions are observed in the product ion mass spectra of the glycopeptides that correspond to HexNAc(+) (m/z 204) and HexHexNAc(+) (m/z 366). A strategy for locating the glycopeptides in the proteolytic digest mixtures of glycoproteins by ions spray liquid chromatography mass spectrometry (LC/MS) is described by utilizing CID in the declustering region of the atmospheric pressure ionization mass spectrometer to produce these characteristic oxonium ions. This LC/CID/MS approach is used to identify glycopeptides in proteolytic digest mixtures of ovomucoid, asialofetuin, and fetuin. LC/CID/MS in the selected ion monitoring mode may be used to identify putative glycopeptides from the proteolytic digest of fetuin.

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Structural studies on the carbohydrate portion of fetuin.

Cited by 341 publications

References 15 publications

Microarray evaluation of the effects of lectin and glycoprotein orientation and data filtering on glycoform discrimination

Microarray evaluation of the effects of lectin and glycoprotein orientation and data filtering on glycoform discrimination

Cloning, expression and gene organization of a human Neu5Acα2‒3Galβ1‒3GalNAc α2,6-sialyltransferase: hST6GalNAc IV

The determination of glycopeptides by liquid chromatography/mass spectrometry with collision-induced dissociation

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