Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics

Taniguchi, Naoyuki; Korekane, Hiroaki

doi:10.5483/bmbrep.2011.44.12.772

Cited by 106 publications

(94 citation statements)

References 92 publications

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“…GnT-III catalyzes the formation of β1-4 glycosidic linkage by transferring GlcNAc to the first Man residue on the core (Figure 2). The formation of a bisecting GlcNAc prevents subsequent processing and elongation of N-glycans (90) which inhibits the catalytic activity of the GnT-II, GnT-IV, GnT-V and FUT8 enzymes that are responsible for branching of the core structure in vitro (89,91).…”

Section: Differentiated Cell Sialylated N-glycansmentioning

confidence: 99%

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Cell Surface Sialylated N-Glycan Alterations during Development

Karaçalı¹

2017

Eur J Biol

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This brief survey focuses on the comparison of sialylated N-glycans of embryonic stem cells (ESCs), induced pluripotent stem cells (iPSCs), mesenchymal stem cells (MSCs) and of differentiated cells. In addition, the impact of sialic acid (Sia) deficiency on cell surfaces during development is summarized. The most common Sia is N-acetylneuraminic acid (Neu5Ac). The branched structures of complex-and hybrid-type N-glycans are the carrier for Sia. Transmembrane adhesive proteins, voltage-gated ion channels and many ligand-activated receptors are some examples of heavily sialylated N-glycan bearing membrane proteins. Their oligosaccharide extensions provide an important contribution to glycocalyx glycans. ESCs and iPSCs are characterized with high mannose-type and biantennary complex-type core structures. Two branches terminate with α2,6-linked Sia. MSCs contain high mannose, hybrid-and complex-type N-glycans. Linear poly-N-acetyllactosamine (poly-Galβ1-4GlcNAc, poly-LacNAc) chains are the characteristic structures. Both α2,3-and α2,6-linked Sias are seen in a species-specific manner in MSCs. α2,6-linked Sia is probably a marker associated with the multipotency of human MSCs. Differentiated healthy cells contain the most abundant 2-branched complex structures. The bisecting branch on the core structure appears as a differentiation marker. poly-LacNAc chains are terminated with α2,3-and α2,6-linked Sia, with the former being higher. poly-LacNAc sequences have a high affinity for β-galactoside recognizing lectin and galectin. Galectin forms a lattice structure with the N-glycans of glycoproteins anchored to the plasma membrane. The impact of N-glycangalectin complexes in cell biology is summarized. Finally, the effect of reduced Sia on clearance of aged cells is explained. Experimental evidence for the masking role of Sia in the regulation of histolysis in aged cells is revealed.

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Section: Differentiated Cell Sialylated N-glycansmentioning

confidence: 99%

“…Sequential activity rules for the GnTs were established by Brockhausen Karacali S. Cell Surface Sialylated N-Glycan Alterations et al (89). These enzymes are responsible for the branching of the core structure in vitro (90)(91)(92)(93)(94).…”

Section: Differentiated Cell Sialylated N-glycansmentioning

confidence: 99%

Cell Surface Sialylated N-Glycan Alterations during Development

Karaçalı¹

2017

Eur J Biol

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“…A significant relationship between the alteration of cell-surface glycan profiles and cancer progress has been described (Borzym-Kluczyk et al, 2012;Saldova et al, 2013a;Zhang et al, 2014). The modifications of cell-surface glycosylation are responsible for the behavioral changes of tumor cells, including invasion and metastasis Kang et al, 2011;Taniguchi and Korekane, 2011;Tian and Zhang, 2013;Zhang et al, 2013;Christiansen et al, 2014;Häuselmann and Borsig, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…GnT-I is required for the conversion from the high-mannose type (with 5 Man residues) to the hybrid and complex types (with 3 Man residues) of N-glycans (Yip et al, 1997;Chen et al, 2002;Taniguchi and Korekane, 2011). It catalyzes the formation of β1-2 linkage by transferring a GlcNAc sugar to the Man residue on the α1-3 arm of the core structure with 5 mannoses (Figure 4).…”

Section: Introductionmentioning

confidence: 99%

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Glycosylation changes leading to the increase in size on the common core of N-glycans, required enzymes, and related cancer-associated proteins

Karaçalı¹,

İzzetoğlu²,

Deveci³

2014

Turk J Biol

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Glycan parts of glycoconjugates on the surfaces of cells regulate many kinds of interactions between the cells and their immediate environments. Alterations in glycosylation on the cancer-associated glycoproteins are responsible for changes in their molecular interactions and biological functions. Glycosylation changes occur in the core and/or at the nonreducing end of the oligosaccharide chains of N-glycans. In this review, we focus on the branching of the common core structure of N-glycans, the responsible enzyme, and the extensions of some of the branches causing size increases on the surface of tumor cells. Abnormal branching, elongation of the branches, and increasing size of the common core of N-glycans are the typical features of these changes and are related with malignant transformations. Seven N-acetylglucosaminyltransferases (GnTs) (GnT-I, GnT-II, GnT-III, GnT-IV, GnT-V, GnT-VI, and GnT-IX) and α1,6-fucosyltransferase (FUT8) initiate the new branches on the core. GnT-IV, GnT-V, and GnT-IX initiate the branches available for poly-LacNAc extensions, which are responsible for tumor progression and metastasis. GnT-III prevents the catalytic activity of GnT-II, GnT-IV, GnT-V, and FUT8 to form branching and elongation of the branches. The contributions of GnT-III and the other enzymes to the cancer progression are in conflict with each other. While GnT-III prevents cancer, the others increase metastasis. The function of FUT8 is related to signal transduction and its activity is higher in tumor tissue than in healthy tissue. The impact of glycosylation changes on some of the cancer-associated proteins (growth factor receptors, adhesion and signal molecules, CD147, TIMP-1, and matriptase) is also summarized.

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Glyco‐engineering in plants to produce human‐like N‐glycan structures

Castilho

Steinkellner

2012

Biotechnology Journal

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It is now possible to produce complex human proteins, largely correctly folded and N-glycosylated, in plants. Much effort has been invested in engineering expression technologies to develop products with superior characteristics. The results have begun to show success in controlling important posttranslational modifications such as N-glycosylation. With the emerging data increasingly indicating the significance of proper N-glycosylation for the efficacy of a drug, glyco-engineering has become an important issue not only for academia but also for the biopharmaceutical industry. Plants have demonstrated a high degree of tolerance to changes in the N-glycosylation pathway, allowing recombinant proteins to be modified into human-like structures in a specific and controlled manner. Frequently the results are a largely homogeneously glycosylated product, currently unrivalled by that of any other expression platforms. This review provides a comprehensive analysis of recent advances in plant N-glyco-engineering in the context of the expression of therapeutically relevant proteins, highlighting both the challenges and successes in the application of such powerful technologies.

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Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics

Cited by 106 publications

References 92 publications

Cell Surface Sialylated N-Glycan Alterations during Development

Cell Surface Sialylated N-Glycan Alterations during Development

Glycosylation changes leading to the increase in size on the common core of N-glycans, required enzymes, and related cancer-associated proteins

Glyco‐engineering in plants to produce human‐like N‐glycan structures

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