Systems glycomics of adult zebrafish identifies organ-specific sialylation and glycosylation patterns

Yamakawa, Nao; Vanbeselaere, Jorick; Chang, Lan-Yi; Yu, Shin‐Yi; Ducrocq, Lucie; Harduin-Lepers, Anne; Kurata, Junichi; Aoki‐Kinoshita, Kiyoko F.; Sato, Chihiro; Khoo, Kay‐Hooi; Kitajima, Ken; Guérardel, Yann

doi:10.1038/s41467-018-06950-3

Cited by 83 publications

(85 citation statements)

References 75 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…10B). Although ␤1,3-galactose is also present in mammals, the typical vertebrate modification with ␤1,4-galactose is absent in the brittle star, as are digalactose motifs, whether these be Gal␣1,3/4Gal or Gal␤1,4Gal, as found in many mammals, birds, and fish (35)(36)(37), and histo- In case of isomers with internal NeuGc, ␤1,3-galactosidase was able to cleave two residues (B and G) compared with one galactose for those with one terminal sialic acid residue (R and W); only after ␤1,3-galactosidase digest could the key fragment for the NeuGc-HexNAc modification, m/z 511 (insets in B, C, G, and H) be detected. The four isomers also differed in their susceptibility to ␣2,3-sialidase S, which only cleaves off terminal NeuGc (S and Y), whereas internal NeuGc was removed with acid hydrolysis (D and I).…”

Section: Discussionmentioning

confidence: 99%

Glycosylation at an evolutionary nexus: the brittle star Ophiactis savignyi expresses both vertebrate and invertebrate N-glycomic features

Eckmair

Jin²,

Karlsson³

et al. 2020

Journal of Biological Chemistry

View full text Add to dashboard Cite

Echinoderms are among the most primitive deuterostomes and have been used as model organisms to understand chordate biology because of their close evolutionary relationship to this phylogenetic group. However, there are almost no data available regarding the N-glycomic capacity of echinoderms, which are otherwise known to produce a diverse set of species-specific glycoconjugates, including ones heavily modified by fucose, sulfate, and sialic acid residues. To increase the knowledge of diversity of carbohydrate structures within this phylum, here we conducted an in-depth analysis of N-glycans from a brittle star (Ophiactis savignyi) as an example member of the class Ophiuroidea. To this end, we performed a multi-step N-glycan analysis by HPLC and various exoglyosidase and chemical treatments in combination with MALDI-TOF MS and MS/MS. Using this approach, we found a wealth of hybrid and complex oligosaccharide structures reminiscent of those in higher vertebrates as well as some classical invertebrate glycan structures. 70% of these N-glycans were anionic, carrying either sialic acid, sulfate, or phosphate residues. In terms of glycophylogeny, our data position the brittle star between invertebrates and vertebrates and confirm the high diversity of N-glycosylation in lower organisms. Figure 4. RP HPLC fractionation of anionic N-glycans. A-K, for the first dimension, anionic enriched N-glycans were separated on a Kinetex C18 RP HPLC (pH 6; calibrated in terms of glucose units). The color code and letters indicate pooled peaks whose second-dimension HIAX-HPLC profiles are shown in Fig. S5, A-K. Fractions are annotated with example glycans according to the symbol nomenclature for glycans (where Me and S represent methyl and sulfate, respectively). The illustrated structures are based on a combination of MS/MS analysis, RP and HIAX-HPLC elution times, as well as enzymatic and/or chemical treatments. Because of the separation properties of the RP column used as the first dimension, multiple sulfated structures are shown in A, modified hybrid structures in B, multiple sialylated biantennary structures in C-E, and those with methylated N-glycolylneuraminic acid and multiantennary structures in G-K. The 4 g.u. RP HPLC peak not subject to 2D-HPLC contains a nondigestible glycan not related to other analyzed structures. Brittle star N-glycome

show abstract

Section: Discussionmentioning

confidence: 99%

Glycosylation at an evolutionary nexus: the brittle star Ophiactis savignyi expresses both vertebrate and invertebrate N-glycomic features

Eckmair

Jin²,

Karlsson³

et al. 2020

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…[22][23][24][25][26][27] Unfortunately, the low ionization efficiency and complicated MS pattern of glycans limit the application of MS in glycan proling at a single-cell level. [28][29][30] Therefore, there is great demand to develop a singlecell MS approach which could analyse multiple glycans sensitively at the single-cell level and provide spatial information of glycans on tissues.…”

Section: Introductionmentioning

confidence: 99%

Laser cleavable probes for in situ multiplexed glycan detection by single cell mass spectrometry

et al. 2019

View full text Add to dashboard Cite

show abstract

“…The mid mode (mass range m / z 1000–3000) was used with laser power set at 85 for two shots in 100 locations per spot. Assignment was made tentatively from calculated mass composition and a literature search …”

Section: Methodsmentioning

confidence: 99%

OGT Controls the Expression and the Glycosylation of E‐cadherin, and Affects Glycosphingolipid Structures in Human Colon Cell Lines

et al. 2019

Self Cite

View full text Add to dashboard Cite

Colorectal cancer (CRC) affects both women and men living in societies with a high sedentary lifestyle. Amongst the phenotypic changes exhibited by tumor cells, a wide range of glycosylation has been reported for colon cancer‐derived cell lines and CRC tissues. These aberrant modifications affect different aspects of glycosylation, including an increase in core fucosylation and GlcNAc branching on N‐glycans, alteration of O‐glycans, upregulated sialylation, and O‐GlcNAcylation. Although O‐GlcNAcylation and complex glycosylations differ in many aspects, sparse evidences report on the interference of O‐GlcNAcylation with complex glycosylation. Nevertheless, this relationship is still a matter of debate. Combining different approaches on three human colon cell lines (HT29, HCT116 and CCD841CoN), it is herein reported that silencing O‐GlcNAc transferase (OGT, the sole enzyme driving O‐GlcNAcylation), only slightly affects overall N‐ and O‐glycosylation patterns. Interestingly, silencing of OGT in HT29 cells upregulates E‐cadherin (a major actor of epithelial‐to‐mesenchymal transition) and changes its glycosylation. On the other hand, OGT silencing perturbs biosynthesis of glycosphingolipids resulting in a decrease in gangliosides and an increase in globosides. Together, these results provide novel insights regarding the selective regulation of complex glycosylations by O‐GlcNAcylation in colon cancer cells.

show abstract

Systems glycomics of adult zebrafish identifies organ-specific sialylation and glycosylation patterns

Cited by 83 publications

References 75 publications

Glycosylation at an evolutionary nexus: the brittle star Ophiactis savignyi expresses both vertebrate and invertebrate N-glycomic features

Glycosylation at an evolutionary nexus: the brittle star Ophiactis savignyi expresses both vertebrate and invertebrate N-glycomic features

Laser cleavable probes for in situ multiplexed glycan detection by single cell mass spectrometry

OGT Controls the Expression and the Glycosylation of E‐cadherin, and Affects Glycosphingolipid Structures in Human Colon Cell Lines

Contact Info

Product

Resources

About