Eukaryotic protein glycosylation: a primer for histochemists and cell biologists

Corfield, Anthony P.

doi:10.1007/s00418-016-1526-4

Cited by 110 publications

(85 citation statements)

References 357 publications

(241 reference statements)

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“…The N-linked glycosylation of proteins is initiated in the endoplasmic reticulum (ER) with the en bloc transfer of a preformed oligosaccharide structure to the consensus sequence Asn-X-Ser/Thr. This structure is subsequently processed by glycosidases and glycosyltransferases in the ER and Golgi [reviewed in Moremen et al (2012)] (please see the articles by Corfield (2017) and Roth and Zuber (2017) in this theme issue for a review of this process). While the glycosylation enzymes in the Golgi are localized in the cisternae essentially in the order in which they act to modify the new glycans, there is distinct overlap (Rabouille et al 1995).…”

Section: The Biosynthesis Of Sialylated N-glycans In the Golgimentioning

confidence: 99%

Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Bhide

Colley

2016

Histochem Cell Biol

178

144

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Sialylated N-glycans play essential roles in the immune system, pathogen recognition and cancer. This review approaches the sialylation of N-glycans from three perspectives. The first section focuses on the sialyltransferases that add sialic acid to N-glycans. Included in the discussion is a description of these enzymes' glycan acceptors, conserved domain organization and sequences, molecular structure and catalytic mechanism. In addition, we discuss the protein interactions underlying the polysialylation of a select group of adhesion and signaling molecules. In the second section, the biosynthesis of sialic acid, CMP-sialic acid and sialylated N-glycans is discussed, with a special emphasis on the compartmentalization of these processes in the mammalian cell. The sequences and mechanisms maintaining the sialyltransferases and other glycosylation enzymes in the Golgi are also reviewed. In the final section, we have chosen to discuss processes in which sialylated glycans, both N- and O-linked, play a role. The first part of this section focuses on sialic acid-binding proteins including viral hemagglutinins, Siglecs and selectins. In the second half of this section, we comment on the role of sialylated N-glycans in cancer, including the roles of β1-integrin and Fas receptor N-glycan sialylation in cancer cell survival and drug resistance, and the role of these sialylated proteins and polysialic acid in cancer metastasis.

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Section: The Biosynthesis Of Sialylated N-glycans In the Golgimentioning

confidence: 99%

Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Bhide

Colley

2016

Histochem Cell Biol

178

144

View full text Add to dashboard Cite

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“…These diseases showed fluctuating expression for many glycogenes (Figure 2) and structural changes in glycans may be involved in them. Structural changes in O-glycans in inflammatory bowel disease were recently reported, [42] whereas changes in N-glycans can be inferred from our PCA results. Taking these findings together, structural changes in O-glycans and N-glycans may be common to these diseases.…”

Section: Identification Of Commonalities Among Different Diseasesmentioning

confidence: 55%

Omics‐based Identification of Glycan Structures as Biomarkers for a Variety of Diseases

Akiyoshi

Iwata

Berenger

et al. 2019

Molecular Informatics

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Glycans play important roles in cell communication, protein interaction, and immunity, and structural changes in glycans are associated with the regulation of a range of biological pathways involved in disease. However, our understanding of the detailed relationships between specific diseases and glycans is very limited. In this study, we proposed an omics-based method to investigate the correlations between glycans and a wide range of human diseases. We analyzed the gene expression patterns of glycogenes (glycosyltransferases and glycosidases) for 79 different diseases. A biological pathway-based glycogene signature was constructed to identify the alteration in glycan biosynthesis and the associated glycan structures for each disease state. The degradation of N-glycan and keratan sulfate, for example, may promote the growth or metastasis of multiple types of cancer, including endometrial, gastric, and nasopharyngeal. Our results also revealed that commonalities between diseases can be interpreted using glycogene expression patterns, as well as the associated glycan structure patterns at the level of the affected pathway. The proposed method is expected to be useful for understanding the relationships between glycans, glycogenes, and disease and identifying disease-specific glycan biomarkers.

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“…Just as an intricate synthetic apparatus ensures to have a broad panel of 'code words' available (3)(4)(5)(6)(7)(8), the same is true for reaching diversity on the level of 'readers' of the sugar code: more than a dozen protein folds have developed the ability to specifically bind glycans (9)(10)(11)(12)(13)(14). Among them, the β-sandwich motif is a (15)(16)(17)(18)(19)(20)(21)(22)(23).…”

Section: A Introductionmentioning

confidence: 99%

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 1. Galectin-Related Inter-Fiber Protein (GRIFIN)

Caballero¹,

Manning²,

Ludwig³

et al. 2018

TIGG

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Systematic databank-based sequence comparisons with the cDNA sequence for a lens-specific rat protein localized between lens fiber cells disclosed its similarity to galectins. In mammals, two sequence changes occur within the seven positions of amino acids commonly engaged in contacts to the β-galactoside core of glycans. Taking the compilation of GRIFIN genes to the level of diverse vertebrates revealed an exceptional variability: mammals shared alteration at two sites, birds and reptiles at only one site and amphibians and fish presented complete reconstitution. The homodimeric (proto-type) GRIFINs of chicken and zebrafish thus are active lectins. Crystallographical information for chicken GRIFIN illustrates the contact profile to lactose without one otherwise conserved site due to the Arg-to-Val substitution. That GRIFIN is enormously stable in vertebrate lenses, can act like a glue (or a bridge) due to its structure and interacts with α-crystallin (shown for murine GRIFIN) suggests a role in well-ordered packing of lens proteins. Referring to a likely analogy in plants, oligomeric leguminous lectins, β-sandwich proteins as galectins, are also assumed to participate in depositing and spatially organizing cell contents, here storage proteins in protein bodies and their contact to the membrane in carbohydrate-dependent and -independent manners, a likely case of structural and functional convergence. A. IntroductionThe realization of the unsurpassed capacity of glycans to store

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Eukaryotic protein glycosylation: a primer for histochemists and cell biologists

Cited by 110 publications

References 357 publications

Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Sialylation of N-glycans: mechanism, cellular compartmentalization and function

Omics‐based Identification of Glycan Structures as Biomarkers for a Variety of Diseases

Members of the Galectin Network with Deviations from the Canonical Sequence Signature. 1. <i>G</i>alectin-<i>R</i>elated <i>I</i>nter-<i>F</i>iber Prote<i>in</i> (GRIFIN)

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