Biosynthesis of Complex Mucin-Type O-Glycans

Brockhausen, Inka

doi:10.1016/b978-008045382-8.00643-2

Cited by 12 publications

(19 citation statements)

References 264 publications

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“…This suggests that C2GnT1 is expressed in HEK293 cells and that OE-E6/E7 cells, in addition, express low levels of C2GnT2. 37 Thus both cell types can efficiently synthesize O-glycan core 1 and 2 structures, and lack the enzyme activity that synthesizes O-glycan core 3 which is the precursor for the synthesis of core 4 structure. However, the MS data suggest that there may be a very small amount of core 3 and/or core 4 structures in rhOVGP1 which remains to be confirmed.…”

Section: Resultsmentioning

confidence: 99%

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Structures and biosynthesis of the N- and O-glycans of recombinant human oviduct-specific glycoprotein expressed in human embryonic kidney cells

Yang

Tao

Orlando

et al. 2012

Carbohydrate Research

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Oviduct-specific glycoprotein (OVGP1) is a major mucin-like glycoprotein synthesized and secreted exclusively by non-ciliated secretory cells of mammalian oviduct. In vitro functional studies showed that OVGP1 plays important roles during fertilization and early embryo development. We have recently produced recombinant human oviduct-specific glycoprotein (rhOVGP1) in human embryonic kidney 293 (HEK293) cells. The present study was undertaken to characterize the structures and determine the biosynthetic pathways of the N- and O-glycans of rhOVGP1. Treatment of the stable rhOVGP1-expressing HEK293 cells with either GalNAcα-Bn to block O-glycan extension, tunicamycin to block N-glycosylation, or neuraminidase increased the electrophoretic mobility of rhOVGP1. A detailed analysis of O- and N-linked glycans of rhOVGP1 by mass spectrometry showed a broad range of many simple and complex glycan structures. In order to identify the enzymes involved in the glycosylation of rhOVGP1, we assayed glycosyltransferase activities involved in the assembly of O- and N-glycans in HEK293 cells, and compared these to those from the immortalized human oviductal cells (OE-E6/E7). Our results demonstrate that HEK293 and OE-E6/E7 cells exhibit a similar spectrum of glycosyltransferase activities that can synthesize elongated and sialylated O-glycans with core 1 and 2 structures, as well as complex multiantennary N-glycans. It is anticipated that the knowledge gained from the present study will facilitate future studies of the role of the glycans of human OVGP1 in fertilization and early embryo development.

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Section: Resultsmentioning

confidence: 99%

“…However, oviductal cells exhibit the levels of enzymes typical for a secretory type of cell that can O-glycosylate secreted glycoproteins and mucins. 37 …”

Section: Resultsmentioning

confidence: 99%

Structures and biosynthesis of the N- and O-glycans of recombinant human oviduct-specific glycoprotein expressed in human embryonic kidney cells

Yang

Tao

Orlando

et al. 2012

Carbohydrate Research

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“…About 75% of the mucin weight is carbohydrate. Typically, O-glycans are densely attached to Ser/Thr residues in tandem repeat sequences [6,19,20]. N-glycosylation sites (Asn-x-Ser/Thr) and N-glycans have also been found in mucins [21,22] and the cell surface-bound MUC1 associates with Tyr-kinase receptors that are N-glycosylated [13,14].…”

Section: Introductionmentioning

confidence: 99%

“…Both N-and O-glycans of glycoproteins can carry sulfate esters, and mucins from bronchial, intestinal and reproductive tissues have been shown to be sulfated [20]. Sulfotransferases are ubiquitously expressed and selected sulfotransferases play a role in inflammation.…”

Section: Introductionmentioning

confidence: 99%

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Glycosylation pathways of human corneal and conjunctival epithelial cell mucins

Brockhausen

Elimova

Woodward

et al. 2018

Carbohydrate Research

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Mucin glycoproteins on the ocular surface are rich in O-glycans and have important roles in the protection from physical, chemical and microbial impact. In this work, we have cultured human corneal and conjunctival epithelial cells to examine the glycosyltransferase activities that synthesize the O-glycans of mucins. The results indicate that ocular surface epithelial cells have active enzymes that synthesize O-glycans with sialylated core 1, Galβ1–3GalNAcα, and core 2, GlcNAcβ1–6(Galβ1–3)GalNAcα structures which corresponds to previous structural studies. Eye cells also have enzymes that synthesize complex N-glycans that are found on mucins. Results from treatment of eye cells with TNFα suggest that epithelial O-glycosylation changes in a dynamic fashion during inflammatory stimuli of the eye surface.

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Mucin‐Type Glycopeptide Structure in Solution: Past, Present, and Future

Barchi

2013

Biopolymers

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Mucins are very high molecular weight glycoproteins that form a "mucus" barrier at the surface of epithelial cells. They are heavily glycosylated with O-linked glycans that are involved in myriad cellular functions, including protection from external changes in pH, ion flux and reactive oxygen species. Aberrations in mucin expression and their glycan constitution have been associated with many disease states including gastritis, pulmonary disorders and cancer. High resolution structural information on mucins is lacking due to their complexity, in particular their large size and the many variants of O-linked glycans produced in their biosynthesis. This review discusses the structures of glycopeptides that contain "mucin-type" glycosylation, and concentrates primarily on data obtained by NMR spectroscopy. The effect of the glycan on the peptide backbone, the features that have shown to be common to this type of glycosylation and the differences of glycosylation at serine and threonine residues are the major topics of discussion.

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Biosynthesis of Complex Mucin-Type O-Glycans

Cited by 12 publications

References 264 publications

Structures and biosynthesis of the N- and O-glycans of recombinant human oviduct-specific glycoprotein expressed in human embryonic kidney cells

Structures and biosynthesis of the N- and O-glycans of recombinant human oviduct-specific glycoprotein expressed in human embryonic kidney cells

Glycosylation pathways of human corneal and conjunctival epithelial cell mucins

Mucin‐Type Glycopeptide Structure in Solution: Past, Present, and Future

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