Sulfated di‐, tri‐ and tetraantennary N‐glycans in human Tamm‐Horsfall glycoprotein

Abstract

The primary structures of 32 sulfated di-, tri-and tetraantennary N-glycans of human Tamm-Horsfall glycoprotein (THP) have been determined. THP was isolated from the urine of one healthy male donor. The intact carbohydrate chains were released by PNGase-F and fractionated via FPLC on Resource Q, HPLC on LiChrosorb-NH 2 , and high-pH anion-exchange chromatography on CarboPac PA-1. Characterizations were performed using 500-MHz and 600-MHz 1 H-NMR spectroscopy, in combination with sialidase treatments. The type of characterized N-glycans ranged from monosulfated to trisulfated N-glycans, whereby the sulfate groups were present as 3-O-sulfated Gal (Gal3S) and 4-O-sulfated GalNAc (GalNAc4S). A compilation of the established structures is shown below.

Uromodulin, an Emerging Novel Pathway for Blood Pressure Regulation and Hypertension

“…36 In the urine, uromodulin is mainly present as a high-molecular-weight polymer (M r , 1-10×10 6 Da) that appears on electron microscopy analysis as a matrix of fibrils, with a width of ≈100 Å and an average length of 25 000 Å. Uromodulin is a polyanionic macromolecule attributable to extensive sialylation and sulfated N-linked glycans. 37 In solution, uromodulin aggregates with gel-like properties when NaCl and CaCl 2 concentrations are ≈100 mmol/L and ≈1 mmol/L, respectively. 38,39 The released protein forms a slowly moving polyanionic gel interacting or associating with plasma membrane-anchored uromodulin molecules.…”

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

“…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.…”

Molecular Cloning and Characterization of a Novel Human Galactose 3-O-Sulfotransferase That Transfers Sulfate to Galβ1→3GalNAc Residue in O-Glycans

“…The SO 3 Ϫ 33Gal structure in O-linked and N-linked glycans has been found in various glycoproteins including thyroglobulin (4 -6), meconium glycoproteins (7), respiratory mucous glycoproteins from patients with cystic fibrosis (8 -10) and chronic bronchitis (11), an ovarian cystadenoma glycoprotein (12), LS174T-HM7 colon carcinoma mucin (13), Tamm-Horsfall glycoprotein (14), sulfomucins (15), and oviducal mucins (16). Sulfated residues in these glycoproteins are attached to C-3Ј of Gal␤133/4GlcNAc, Gal␤133GalNAc, or Gal␤133Gal structure.…”