Presence of β-linked GalNAc residues on N-glycans of human thyroglobulin

Takeya, Akira; Hosomi, Osamu; Nishijima, Hironori; Ohe, Yoshihide; Sugahara, Kunio; Sagi, Morihisa; Yamazaki, Kentaro; Hayakawa, Hideyuki; Takeshita, Hiroshi; Sasaki, Chizuko; Kogure, Tadahisa; Mukai, Toshiji

doi:10.1016/j.lfs.2006.10.004

Cited by 13 publications

(4 citation statements)

References 44 publications

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“…The polypeptide chain of human Tg (hTg) contains 20 putative N -glycosylation sites, of which 16 Asn are glycosylated [ 34 ]. The main types of hTg oligosaccharides are high-mannose and diantennary complex-type structures ( Figure 2 ) [ 37 ]. Eight of the N -glycans are fucosylated and galactosylated complex-type, five N -glycosylation sites contain high-mannose oligosaccharides, two of them were identified as hybrid- or complex-type without Fuc, and one N -glycosylation site was occupied by a variety of N -oligosaccharide structures [ 34 ].…”

Section: Glycosylation Of Proteins Involved In Thyroid Functioningmentioning

confidence: 99%

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Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders

Ząbczyńska

Kozłowska

Pocheć

2018

IJMS

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The key proteins responsible for hormone synthesis in the thyroid are glycosylated. Oligosaccharides strongly affect the function of glycosylated proteins. Both thyroid-stimulating hormone (TSH) secreted by the pituitary gland and TSH receptors on the surface of thyrocytes contain N-glycans, which are crucial to their proper activity. Thyroglobulin (Tg), the protein backbone for synthesis of thyroid hormones, is a heavily N-glycosylated protein, containing 20 putative N-glycosylated sites. N-oligosaccharides play a role in Tg transport into the follicular lumen, where thyroid hormones are produced, and into thyrocytes, where hyposialylated Tg is degraded. N-glycans of the cell membrane transporters sodium/iodide symporter and pendrin are necessary for iodide transport. Some changes in glycosylation result in abnormal activity of the thyroid and alteration of the metabolic clearance rate of hormones. Alteration of glycan structures is a pathological process related to the progression of chronic diseases such as thyroid cancers and autoimmunity. Thyroid carcinogenesis is accompanied by changes in sialylation and fucosylation, β1,6-branching of glycans, the content and structure of poly-LacNAc chains, as well as O-GlcNAcylation, while in thyroid autoimmunity the main processes affected are sialylation and fucosylation. The glycobiology of the thyroid gland is an intensively studied field of research, providing new data helpful in understanding the role of the sugar component in thyroid protein biology and disorders.

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Section: Glycosylation Of Proteins Involved In Thyroid Functioningmentioning

confidence: 99%

“…TSHR contains high-mannose and complex-type structures [ 33 ]. High-mannose structures as well as galactosylated, fucosylated, and sialylated hybrid-type and complex-type N -glycans have been identified on Tg [ 34 , 37 , 38 ].…”

Section: Figurementioning

confidence: 99%

Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders

Ząbczyńska

Kozłowska

Pocheć

2018

IJMS

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“…O. tesota PF1 and PF3 lectins are inhibited by free monosaccharides and/or by complex carbohydrates of fetuin, thyroglobulin, immunoglobulin, mucine and ovalbumin, whereas PF2 is only inhibited by the intact glycoprotein [5]. Although glycan structures present in glycoproteins are known to have N and O linked oligosaccharides, desialylation of the glycan can result in an increase or decrease in lectin binding affinity [70]. The galactose residues found in glycosylated proteins are often capped with sialic acid, a characteristic that may alter the interaction with lectins, as is seen for Amaranthus caudatus and Abrus pulchellus [71,72].…”

Section: Specificity Of Legume Lectinsmentioning

confidence: 99%

Legume Lectins: Proteins with Diverse Applications

Lagarda-Díaz

Guzmán-Partida

Vázquez–Moreno

2017

IJMS

136

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Lectins are a diverse class of proteins distributed extensively in nature. Among these proteins; legume lectins display a variety of interesting features including antimicrobial; insecticidal and antitumor activities. Because lectins recognize and bind to specific glycoconjugates present on the surface of cells and intracellular structures; they can serve as potential target molecules for developing practical applications in the fields of food; agriculture; health and pharmaceutical research. This review presents the current knowledge of the main structural characteristics of legume lectins and the relationship of structure to the exhibited specificities; provides an overview of their particular antimicrobial; insecticidal and antitumor biological activities and describes possible applications based on the pattern of recognized glyco-targets.

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“…Fetuin has a triantennary structure with terminal Galβ1-4GlcNAc and three O-linked structure (Townsend et al 1986). Thyroglobulin contains mainly diantennary Gal1-4GlcNAc N-glycans (Takeya et al 2007). Mucin contains several Galβ1-3GalNAcα1 O-glycans.…”

Section: Properties Of Hml As a Lectinmentioning

confidence: 99%

Purification and characterization of a lectin from the mushroom Hypsizigus marmoreus

et al. 2015

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HML (Hypsizigus marmoreus lectin) was isolated from the mushroom Hypsizigus marmoreus using CM cation exchange, bovine submaxillary gland mucin affinity column and TSK-GEL G3000SW gel filtration chromatography. The results of SDS-PAGE, MALDI-TOF MS and gel filtration analysis of HML indicated that the lectin was a dimer with each subunit of 9.5 kDa. The partial amino acid sequences of HML were determined by N-terminal sequencing of peptides obtained by trypsin or Glu-C endopeptidase digest of the lectin. In the hemagglutination inhibition assay, HML did not bind to any mono-or oligo-saccharides tested. Among the glycoproteins examined, asialo-fetuin was the strongest inhibitor.

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Presence of β-linked GalNAc residues on N-glycans of human thyroglobulin

Cited by 13 publications

References 44 publications

Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders

Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders

Legume Lectins: Proteins with Diverse Applications

Purification and characterization of a lectin from the mushroom Hypsizigus marmoreus

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