O-glycosylation pattern of CD24 from mouse brain

Bleckmann, Christina; Geyer, Hildegard; Lieberoth, Annika; Splittstoesser, Frauke; Liu, Yan; Feizi, Ten; Schachner, Melitta; Kleene, Ralf; Reinhold, Vernon N.; Geyer, Rudolf

doi:10.1515/bc.2009.044

Cited by 80 publications

(65 citation statements)

References 63 publications

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“…Using this strategy O-Man glycopeptides from α-DG and a total of 51 unique O-Man glycoproteins were identified, comprising a total of 235 O-Man glycosites (Table 1 and Dataset S1). We did not identify any of the individual proteins more recently suggested to carry O-Man glycans (10)(11)(12)(13)(14), which could be due to a number of reasons including experimental limitations as well as lack of expression of these proteins in MDA-MB-231 cells. Identification of O-Man Glycosites on α-DG.…”

Section: Resultsmentioning

confidence: 87%

Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins

Vester-Christensen¹,

Halim²,

Joshi³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

148

187

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The metazoan O-mannose (O-Man) glycoproteome is largely unknown. It has been shown that up to 30% of brain O-glycans are of the O-Man type, but essentially only alpha-dystroglycan (α-DG) of the dystrophin-glycoprotein complex is well characterized as an O-Man glycoprotein. Defects in O-Man glycosylation underlie congenital muscular dystrophies and considerable efforts have been devoted to explore this O-glycoproteome without much success. Here, we used our SimpleCell strategy using nuclease-mediated gene editing of a human cell line (MDA-MB-231) to reduce the structural heterogeneity of O-Man glycans and to probe the OMan glycoproteome. In this breast cancer cell line we found that O-Man glycosylation is primarily found on cadherins and plexins on β-strands in extracellular cadherin and Ig-like, plexin and transcription factor domains. The positions and evolutionary conservation of O-Man glycans in cadherins suggest that they play important functional roles for this large group of cell adhesion glycoproteins, which can now be addressed. The developed O-Man SimpleCell strategy is applicable to most types of cell lines and enables proteome-wide discovery of O-Man protein glycosylation.POMGnT1 | O-glycosylation | Orbitrap | mass spectrometry | glycoproteomics

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Section: Resultsmentioning

confidence: 87%

Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins

Vester-Christensen¹,

Halim²,

Joshi³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

148

187

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“…Although this type of glycosylation is most frequently discussed in connection with alpha-dystroglycan, other proteins such as CD24, neurofascin, and receptor tyrosine phosphatase beta have also been shown to contain O-mannosyl structures (63)(64)(65). However, the exact site of such modifications has not been identified for these proteins.…”

Section: Fig 4 Etd Spectrum Of 3100 Ngat(galglcnacfuc)c(carbamidomementioning

confidence: 99%

N- and O-Glycosylation in the Murine Synaptosome

Trinidad

Schoepfer²,

Burlingame

et al. 2013

Molecular & Cellular Proteomics

163

230

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We present the first large scale study characterizing both N-and O-linked glycosylation in a site-specific manner on hundreds of proteins. We demonstrate that a lectin-affinity fractionation step using wheat germ agglutinin enriches not only peptides carrying intracellular O-GlcNAc, but also those bearing ER/Golgi-derived N-and O-linked carbohydrate structures. Liquid chromatography-MS (LC/ MS) analysis with high accuracy precursor mass measurements and high sensitivity ion trap electron-transfer dissociation (ETD) were utilized for structural characterization of glycopeptides. Our results reveal both the identity of the precise sites of glycosylation and information on the oligosaccharide structures possible on these proteins. We report a novel iterative approach that allowed us to interpret the ETD data set directly without making prior assumptions about the nature and distribution of oligosaccharides present in our glycopeptide mixture. Over 2500 unique N-and O-linked glycopeptides were identified on 453 proteins. The extent of microheterogeneity varied extensively, and up to 19 different oligosaccharides were attached at a given site. We describe the presence of the well-known mucin-type structures for O-glycosylation, an EGF-domain-specific fucosylation and a rare O-mannosylation on the transmembrane phosphatase Ptprz1. Finally, we identified three examples of O-glycosylation on tyrosine residues. Molecular & Cellular

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“…The saccharide structure of CD24 from mouse brain is now being elucidated. 11,12 Several ligands of CD24 have been identified, and ligand specificity seems to be dependent on cellular context because of the highly variable glycosylation of CD24. For instance, CD24 can promote cancercell rolling and colonization to lung only when fucose transferase VII converts CD24 into a P-selectin ligand.…”

Section: Introductionmentioning

confidence: 99%

CD24: from A to Z

et al. 2010

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As a testament to the importance of CD24, researchers with diverse interests, including adaptive immunity, inflammation, autoimmune diseases and cancer, have encountered CD24. CD24 is overexpressed in many cancers and appears oncogenic. In the adaptive immune response, CD24 is a redundant costimulatory molecule in costimulation-rich lymphoid organs but is essential in selected target organs tested, such as brain and skin. More recent studies suggest it may have a role in discriminating danger and pathogen-associated molecular patterns by dendritic cells. The biology of CD24 is intriguing but poorly understood. Here we summarize the major findings associated with CD24 to stimulate new ideas for further research that may reveal the underlying link among the diverse processes mediated by CD24.

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O-glycosylation pattern of CD24 from mouse brain

Cited by 80 publications

References 63 publications

Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins

Mining the O-mannose glycoproteome reveals cadherins as major O-mannosylated glycoproteins

N- and O-Glycosylation in the Murine Synaptosome

CD24: from A to Z

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