Regular ArticleGlycosylation in Human Thyroglobulin: Location of the N-Linked Oligosaccharide Units and Comparison with Bovine Thyroglobulin
References (0)
Cited by (58)
Site-specific N-glycosylation analysis of human thyroid thyroglobulin by mass spectrometry-based Glyco-analytical strategies
2022, Journal of ProteomicsCitation Excerpt :Bioinformatics data also shows that Asn1348 is less likely to carry N-glycans (value for Asn1348 is 0.3571). In a study, sixteen N-glycosylation sites of the thyroglobulin protein were characterized, and it was determined that 12 of these regions were filled and four glycosylation sites did not (Asn110, Asn496, Asn1869, and Asn2122) [4]. However, in the data we obtained, except Asn496, the other 3 N-glycosylation sites were occupied by N-glycans (Fig. S9, Table S6).
Structure and genetic variants of thyroglobulin: Pathophysiological implications
2021, Molecular and Cellular EndocrinologyCitation Excerpt :Individual branches in both types of N-glycans are elongated in the Golgi apparatus by addition of galactose, fucose and sialic acid residues catalyzed by galactosyltransferases, fucosyltransferases and sialyltransferases, respectively (Fig. 8a) (Vagin et al., 2009). The cDNA sequence of human TG predicts 20 putative N-linked glycosylation sites (asparagine residues 76, 110, 198, 484, 529, 748, 816, 947,1220, 1348, 1349, 1365, 1716, 1774, 1869, 2013, 2122, 2250, 2295 and 2582), 16 are glycosylated in the mature protein (Yang et al., 1996). Eight sites (asparagine residues 76, 484, 529, 748, 816, 1716, 1774 and 2250) are linked to complex type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine (Yang et al., 1996).
Defects in protein folding in congenital hypothyroidism: Protein folding in congenital hypothyroidism
2020, Molecular and Cellular EndocrinologyA capture and release method based on noncovalent ligand cross-linking and facile filtration for purification of lectins and glycoproteins
2020, Journal of Biological ChemistryCitation Excerpt :Our previous study (31) showed that CSA and CSC were multivalent ligands of Gal-3. Tg contains 18 complex-type glycans per molecule (nine per subunit) (32). Thus, its interaction with Gal-3 is also multivalent (33).
N-glycan profiling of papillary thyroid carcinoma tissues by MALDI-TOF-MS
2019, Analytical BiochemistryThyroglobulin represents a novel molecular architecture of vertebrates
2016, Journal of Biological ChemistryCitation Excerpt :During its complex trafficking, Tg undergoes many post-translational modifications critical for its biological function (23). In mammals, newly synthesized Tg is first glycosylated at many sites (24) and folded via the formation of numerous intradomain disulfide bonds. Spacing between the cysteine residues has allowed for the identification of distinct Tg repeat domains controlling proper folding of the protein (11).