The N-glycome of human embryonic stem cells

Satomaa, Tero; Heiskanen, Annamari; Mikkola, Milla; Olsson, Cia; Blomqvist, Maria; Tiittanen, Minna; Jaatinen, Taina; Aitio, Olli; Olonen, Anne; Helin, Jari; Hiltunen, Jukka; Natunen, Jari; Tuuri, Timo; Otonkoski, Timo; Saarinen, Jyrki; Laine, Jarmo

doi:10.1186/1471-2121-10-42

Cited by 97 publications

(125 citation statements)

References 54 publications

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“…4A). These results are consistent with both the lectin cell surface studies by Wearne et al (12) and the glycomic profile of whole hESC by Satomaa et al (25). The major difference between this study and the previous two is that we enrich plasma membrane and determine the glycosylation specifically from the membrane.…”

Section: Discussionsupporting

confidence: 82%

“…Furthermore, we quantitate the relative contribution of each glycan types as well as specific isomers on the cell surface. These experiments differ from those by Wearne et al (12) and Satomaa et al (25) in that those were performed on whole cell lysates. The cell surface glycosylation were inferred indirectly using lectins, which are not quantitative when comparing different glycan types.…”

Section: Discussioncontrasting

confidence: 49%

“…In addition, they also found a number of common antigens including T, Tn, and sialyl-Tn. A more structurally intensive study of whole stem cell glycosylation was reported by Satomaa et al (25). The cell surface studies were limited to lectins, which cannot be used quantitatively.…”

mentioning

confidence: 99%

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Extensive Determination of Glycan Heterogeneity Reveals an Unusual Abundance of High Mannose Glycans in Enriched Plasma Membranes of Human Embryonic Stem Cells

Gip

Kim

et al. 2012

Molecular & Cellular Proteomics

100

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Glycosylation is the process by which oligosaccharides, termed glycans, are appended onto membrane and secreted proteins and lipids. It is the most common and complex form of post-translational modification, with ϳ50% of all eukaryotic proteins glycosylated (1, 2). A majority of glycans are found on the cell surface, where they are optimally poised to be the first cellular components encountered by approaching cells, pathogens, antibodies, or other molecules, as well as advertise information about the internal state and homeostasis of the cell (3, 4). Therefore, glycans play an essential role in many biological processes, including cell development and differentiation, cell-cell or cell-matrix communication, and pathogen-host recognition (3,(5)(6)(7). In fact, differences in glycan profiles between healthy and diseased states are utilized for clinical diagnosis (7), providing targets for many novel classes of therapeutics including cancer chemotherapy, diabetes treatment, and antibiotic and anti-viral medicine (5, 8). Glycans are highly heterogeneous in nature, varying in the composition of individual monosaccharide building blocks, the positions with which these building blocks link to each other, and the stereochemical disposition of the linkages (␣ or ␤). This complexity has presented a significant challenge for obtaining structural information about glycans at the molecular From the

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Section: Discussionsupporting

confidence: 82%

Section: Discussioncontrasting

confidence: 49%

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Extensive Determination of Glycan Heterogeneity Reveals an Unusual Abundance of High Mannose Glycans in Enriched Plasma Membranes of Human Embryonic Stem Cells

Gip

Kim

et al. 2012

Molecular & Cellular Proteomics

100

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“…It has recently been demonstrated that the cell surface glycan heparan sulfate (HS) contributes to self-renewal and differentiation of mESCs by regulating BMP, Wnt, and FGF signaling [21,[27][28][29]. The expression patterns of several other cell surface glycans have now been described in undifferentiated and differentiated mESCs and hESCs [30][31][32][33][34]. However, although these glycans may be involved in the regulation of the signaling required for ESC self-renewal, with the exception of HS, their functional roles have not been demonstrated.…”

Section: Introductionmentioning

confidence: 99%

LacdiNAc (GalNAcβ1-4GlcNAc) Contributes to Self-Renewal of Mouse Embryonic Stem Cells by Regulating Leukemia Inhibitory Factor/STAT3 Signaling

et al. 2011

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Self-renewal of mouse embryonic stem cells (mESCs) is maintained by leukemia inhibitory factor (LIF)/signal transducer and activator of transcription (STAT3) signaling. However, this signaling control does not function in neither mouse epiblast stem cells (mEpiSCs) nor human ESCs (hESCs) or human induced pluripotent stem cells (hiPSCs). To date, the underlying molecular mechanisms that determine this differential LIF-responsiveness have not been clarified. Here, we show that the cell surface glycan LacdiNAc (GalNAcb1-4GlcNAc) is required for LIF/ STAT3 signaling. Undifferentiated state mESCs expressed LacdiNAc at a higher level than differentiated state cells. Knockdown of b4GalNAc-T3 reduced LacdiNAc expression and caused a decrease in LIF/STAT3 signaling that lessened the rate of self-renewal of mESCs. A biochemical analysis showed that LacdiNAc expression on LIF receptor (LIFR) and gp130 was required for the stable localization of the receptors with lipid raft/caveolar components, such as caveolin-1. This localization is required for transduction of a sufficiently strong LIF/STAT3 signal. In primed state pluripotent stem cells, such as hiPSCs and mEpiSC-like cells produced from mESCs, LacdiNAc expression on LIFR and gp130 was extremely weak and the level of localization of these receptors on rafts/caveolae was also low. Furthermore, knockdown of b4GalNAc-T3 decreased LacdiNAc expression and reduced the efficiency of reversion of primed state mEpiSC-like cells into naïve state mESCs. These findings show that the different LIF-responsiveness of naïve state (mESCs) and primed state (mEpiSCs, hESCs, and hiPSCs) cells is dependent on the expression of LacdiNAc on LIFR and gp130 and that this expression is required for the induction and maintenance of the naïve state. STEM CELLS 2011;29:641-650 Disclosure of potential conflicts of interest is found at the end of this article.

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“…In human stem cells, the major pluripotency-specific N-glycosylation is made up of a high mannose-type and a biantennary complex-type core structure as determined with MALDI-TOF mass spectrometry NMR spectroscopy (61), flow cytometry and immunohistochemistry, (58, 64,65) and fluorescein labeled lectin staining (59). Upon induction of pluripotency, the occurrence of a significant increase in the high mannose-type N-gly-Karacali S. Cell Surface Sialylated N-Glycan Alterations cans (66,67) indicate that it is in an immature stage of N-glycoproteins (68,69).…”

Section: Embryonic Stem Cell Sialylated N-glycansmentioning

confidence: 99%

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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The N-glycome of human embryonic stem cells

Cited by 97 publications

References 54 publications

Extensive Determination of Glycan Heterogeneity Reveals an Unusual Abundance of High Mannose Glycans in Enriched Plasma Membranes of Human Embryonic Stem Cells

Extensive Determination of Glycan Heterogeneity Reveals an Unusual Abundance of High Mannose Glycans in Enriched Plasma Membranes of Human Embryonic Stem Cells

LacdiNAc (GalNAcβ1-4GlcNAc) Contributes to Self-Renewal of Mouse Embryonic Stem Cells by Regulating Leukemia Inhibitory Factor/STAT3 Signaling

Cell Surface Sialylated N-Glycan Alterations during Development

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