Role of Glycosylation in Development

Haltiwanger, Robert S.; Lowe, John B.

doi:10.1146/annurev.biochem.73.011303.074043

Cited by 695 publications

(503 citation statements)

References 262 publications

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“…Protein glycosylation is involved in many, if not most, biological processes and there is extensive literature that documents its involvement in diverse areas such as cell-cell recognition, cell-extracellular matrix interactions, tissue development, immune response, host-pathogen recognition, protein folding editing control, and protein stability [3][4][5][6]. Glycans are not directly encoded in the genome.…”

mentioning

confidence: 99%

A glycomics platform for the analysis of permethylated oligosaccharide alditols

Costello

Contado-Miller

Cipollo

2007

J. Am. Soc. Mass Spectrom.

156

166

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This communication reports the development of an LC/MS platform for the analysis of permethylated oligosaccharide alditols that, for the first time, demonstrates routine online oligosaccharide isomer separation of these compounds before introduction into the mass spectrometer. The method leverages a high-resolution liquid chromatography system with the superior fragmentation pattern characteristics of permethylated oligosaccharide alditols that are dissociated under low-energy collision conditions using quadrupole orthogonal time-offlight (QoTOF) instrumentation and up to pseudo MS 3 mass spectrometry. Glycoforms, including isomers, are readily identified and their structures assigned. The isomer-specific spectra include highly informative cross-ring and elimination fragments, branch position specific signatures, and glycosidic bond fragments, thus facilitating linkage, branch, and sequence assignment. The method is sensitive and can be applied using as little as 40 fmol of derivatized oligosaccharide. Because permethylation renders oligosaccharides nearly chemically equivalent in the mass spectrometer, the method is semiquantitative and, in this regard, is comparable to methods reported using high field NMR and capillary electrophoresis. In this postgenomic age, the importance of glycosylation in biological processes has become clear. The nature of many of the important questions in glycomics is such that sample material is often extremely limited, thus necessitating the development of highly sensitive methods for rigorous structural assignment of the oligosaccharides in complex mixtures. The glycomics platform presented here fulfills these criteria and should lead to more facile glycomics analyses. (J Am

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mentioning

confidence: 99%

A glycomics platform for the analysis of permethylated oligosaccharide alditols

Costello

Contado-Miller

Cipollo

2007

J. Am. Soc. Mass Spectrom.

156

166

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“…This mutation is predicted to cause a frameshift leading to premature truncation, deleting the carboxy-terminus of the MESP2 protein. The Lunatic fringe (Lfng) gene encodes a glycosyltransferase that modifies O-fucose residues in Notch family proteins, thereby modulating Notch signal transmission (Haltiwanger and Lowe, 2004). Previous comparative analysis of mouse models had demonstrated that mice mutant for the Dll3 and Lfng genes exhibited very similar somite and skeletal defects (Evrard et al, 1998;Kusumi et al, 1998Kusumi et al, , 2004Zhang and Gridley, 1998;Dunwoodie et al, 2002;Zhang et al, 2002), suggesting the LFNG gene as another possible spondylocostal dysostosis gene in humans.…”

Section: Spondylocostal Dysostosis Is Caused By Mutations In Notch Pamentioning

confidence: 99%

The long and short of it: Somite formation in mice

Gridley

2006

Developmental Dynamics

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A fundamental characteristic of the vertebrate body plan is its segmentation along the anterior-posterior axis. This segmental pattern is established during embryogenesis by the formation of somites, the transient epithelial blocks of cells that derive from the unsegmented presomitic mesoderm. Somite formation involves a molecular oscillator, termed the segmentation clock, in combination with gradients of signaling molecules such as fibroblast growth factor 8, WNT3A, and retinoic acid. Disruption of somitogenesis in humans can result in disorders such as spondylocostal dysostosis, which is characterized by vertebral malformations. This review summarizes recent findings concerning the role of Notch signaling in the segmentation clock, the complex regulatory network that governs somitogenesis, the genes that cause inherited spondylocostal dysostosis, and the mechanisms that regulate bilaterally symmetric somite formation. Developmental Dynamics 235:2330 -2336, 2006.

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“…or chemokines (CXCL4, stromal cell-derived factor 1, RANTES, etc. ), thus modulating their activities [6][7][8][9][10][11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Glycotranscriptome study reveals an enzymatic switch modulating glycosaminoglycan synthesis during B‐cell development and activation

et al. 2011

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B-cell fate and responses are modulated by soluble mediators and direct cellular interactions. Migration properties also vary during differentiation, commitment and activation. In many cells, modulation of responses to stimuli involves cell surface glycans, whose architecture depends on the simultaneous expression of multiple enzymes. By looking at the glycosylation-related gene expression patterns among B-cell populations, we determined in this study that the strongest variations were observed for CSGalNAcT-1 and EXTL1. These are enzymes involved in the biosynthesis of alternative forms of glycosaminoglycans (GAGs), namely chondroitin sulfate and heparan sulfate, respectively. These two enzymes showed inverse fluctuations in progenitors, resting B cells and activated B cells, suggesting a developmentally regulated switch between chondroitin and heparan sulfate synthesis. To explore whether these variations contributed to optimal B-cell differentiation, we overexpressed EXTL1 in the B-cell lineage of transgenic mice, yielding a partial differentiation blockade at the pro-B to pre-B transition. In the periphery, this defect was almost fully compensated for in vivo, with normal-size B-cell compartments and normal serum immunoglobulin levels in the transgenic EXTL1 mice. The peripheral B cells from EXTL1 transgenics were only affected with regard to their in vitro responses to polyclonal activation, showing reduced proliferation. Together the data suggest that despite their low amounts in lymphocytes, the heparan sulfate chains decorating the endogenous GAGs appear to be regulators of B-cell physiology.

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Role of Glycosylation in Development

Cited by 695 publications

References 262 publications

A glycomics platform for the analysis of permethylated oligosaccharide alditols

A glycomics platform for the analysis of permethylated oligosaccharide alditols

The long and short of it: Somite formation in mice

Glycotranscriptome study reveals an enzymatic switch modulating glycosaminoglycan synthesis during B‐cell development and activation

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