Regulation of dolichol-linked glycosylation

Welti, Michael

doi:10.1007/s10719-012-9417-y

Cited by 33 publications

(22 citation statements)

References 53 publications

(51 reference statements)

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“…It is possible that the unique N ‐acetylglucosamine (GlcNAc) end of LNT2 is responsible for this protective effect. The process of N ‐glycosylation starts with the synthesis of precursor oligosaccharides and formation of a dolichol‐linked GlcNAc sugar . The GlcNAc end of LNT2 might serve as a substrate for the N ‐glycosylation and therefore prevent Tm‐induced decline of mucus synthesis genes.…”

Section: Discussionmentioning

confidence: 99%

Human Milk Oligosaccharides Differently Modulate Goblet Cells Under Homeostatic, Proinflammatory Conditions and ER Stress

Cheng

Kong

Walvoort

et al. 2019

Molecular Nutrition Food Res

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Scope Human milk oligosaccharides (hMOs) have beneficial effects on intestinal barrier function, but the mechanisms of action are not well understood. Here, the effects of hMOs on goblet cells, which indicate that some hMOs may enhance mucus barrier function through direct modulation of goblet cell function, are studied. Methods and results The modulatory effects of 2′‐fucosyllactose (2′‐FL), 3‐fucosyllactose (3‐FL), lacto‐N‐triaose II (LNT2), and galacto‐oligosaccharides (GOS) on the expression of goblet cell secretory related genes MUC2, TFF3, and RETNLB, and the Golgi‐sulfotransferase genes CHST5 and GAL3ST2 of LS174T are determined by real‐time quantitative RT‐PCR. 3‐FL, LNT2, and GOS‐modulated LS174T gene expression profiles in a dose‐ and time‐dependent manner. In addition, the upregulation of MUC2 is confirmed by immunofluorescence staining. Effects of 2′‐FL, 3‐FL, LNT2, and GOS on gene transcription of LS174T are also assessed during exposure to TNF‐α, IL‐13, or tunicamycin. During TNF‐α challenge, 3‐FL and LNT2 enhance MUC2 and TFF3 gene expression. After IL‐13 exposure, 2′‐FL, 3‐FL, and LNT2 all show upregulating effects on MUC2; 3‐FL and LNT2 also enhance TFF3 expression. LNT2 significantly reverses Tm‐induced downregulation of TFF3, RETNLB, and CHST5. Conclusion The findings indicate that hMOs may enhance mucus barrier function through direct modulation of intestinal goblet cells. Effects are structure‐ and stressor‐dependent.

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Section: Discussionmentioning

confidence: 99%

Human Milk Oligosaccharides Differently Modulate Goblet Cells Under Homeostatic, Proinflammatory Conditions and ER Stress

Cheng

Kong

Walvoort

et al. 2019

Molecular Nutrition Food Res

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“…Dolichol is synthesized by cis-prenyltransferase, starting from farnesylpyrophosphate and the sequential addition of C 5 isoprenoid units [7,8]. Alterations in dolichol biosynthesis severely affect the N-glycosylation process [9] and can result in a recently described class of congenital disorders of glycosylation (CDG) [10].…”

Section: Dolichol the Lipid Carrier In Er Glycosylationmentioning

confidence: 99%

N-linked protein glycosylation in the ER

Aebi

2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

607

516

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N-linked protein glycosylation in the endoplasmic reticulum (ER) is a conserved two phase process in eukaryotic cells. It involves the assembly of an oligosaccharide on a lipid carrier, dolichylpyrophosphate and the transfer of the oligosaccharide to selected asparagine residues of polypeptides that have entered the lumen of the ER. The assembly of the oligosaccharide (LLO) takes place at the ER membrane and requires the activity of several specific glycosyltransferases. The biosynthesis of the LLO initiates at the cytoplasmic side of the ER membrane and terminates in the lumen where oligosaccharyltransferase (OST) selects N-X-S/T sequons of polypeptide and generates the N-glycosidic linkage between the side chain amide of asparagine and the oligosaccharide. The N-glycosylation pathway in the ER modifies a multitude of proteins at one or more asparagine residues with a unique carbohydrate structure that is used as a signalling molecule in their folding pathway. In a later stage of glycoprotein processing, the same systemic modification is used in the Golgi compartment, but in this process, remodelling of the N-linked glycans in a protein-, cell-type and species specific manner generates the high structural diversity of N-linked glycans observed in eukaryotic organisms. This article summarizes the current knowledge of the N-glycosylation pathway in the ER that results in the covalent attachment of an oligosaccharide to asparagine residues of polypeptide chains and focuses on the model organism Saccharomyces cerevisiae. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum.

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“…S1C) (Cantagrel & Lefeber, 2011;Helenius & Aebi, 2004;Larkin & Imperiali, 2011;Schwarz & Aebi, 2011;Welti, 2013). This review will focus on the enzymes in eukaryotes and prokaryotes that generate the monophosphorylated lipid carrier either through phosphorylation of the alcohol or dephosphorylation of the pyrophosphate polyisoprenoid moiety, with the latter being coupled to de novo synthesis of the lipid carrier or through a recycling pathway.…”

Section: Introductionmentioning

confidence: 99%

Conservation of the PTEN catalytic motif in the bacterial undecaprenyl pyrophosphate phosphatase, BacA/UppP

Bickford

Nick

2013

Microbiology

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Isoprenoid lipid carriers are essential in protein glycosylation and bacterial cell envelope biosynthesis. The enzymes involved in their metabolism (synthases, kinases and phosphatases) are therefore critical to cell viability. In this review, we focus on two broad groups of isoprenoid pyrophosphate phosphatases. One group, containing phosphatidic acid phosphatase motifs, includes the eukaryotic dolichyl pyrophosphate phosphatases and proposed recycling bacterial undecaprenol pyrophosphate phosphatases, PgpB, YbjB and YeiU/LpxT. The second group comprises the bacterial undecaprenol pyrophosphate phosphatase, BacA/UppP, responsible for initial formation of undecaprenyl phosphate, which we predict contains a tyrosine phosphate phosphatase motif resembling that of the tumour suppressor, phosphatase and tensin homologue (PTEN). Based on protein sequence alignments across species and 2D structure predictions, we propose catalytic and lipid recognition motifs unique to BacA/UppP enzymes. The verification of our proposed active-site residues would provide new strategies for the development of substratespecific inhibitors which mimic both the lipid and pyrophosphate moieties, leading to the development of novel antimicrobial agents.

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Regulation of dolichol-linked glycosylation

Cited by 33 publications

References 53 publications

Human Milk Oligosaccharides Differently Modulate Goblet Cells Under Homeostatic, Proinflammatory Conditions and ER Stress

Human Milk Oligosaccharides Differently Modulate Goblet Cells Under Homeostatic, Proinflammatory Conditions and ER Stress

N-linked protein glycosylation in the ER

Conservation of the PTEN catalytic motif in the bacterial undecaprenyl pyrophosphate phosphatase, BacA/UppP

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