Structures and developmental alterations of<i>N</i><b>-</b>glycans of zebrafish embryos

Hanzawa, Ken; Suzuki, Noriko; Natsuka, Shunji

doi:10.1093/glycob/cww124

Cited by 30 publications

(41 citation statements)

References 73 publications

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“…However, we cannot preclude the possibility that minor Siaα2-6Gal-containing N -Glycans may exist since our MS/MS data could not discriminate α2-3- from α2-6-sialylation on galactose (Gal). Hanzawa and collaborators have previously demonstrated that α2-6-substituted N -glycans were the predominantly expressed sialylated N -glycans in deyolked embryos 31 . In accordance with their study, we have detected α2-6 sialylation on the N -acetylgalactosamine (GalNAc) residue of LacdiNAc motifs in NG15, 24, 58, 59 that were exclusively observed in ovary in our study.…”

Section: Resultsmentioning

confidence: 97%

“…Despite the rush in using zebrafish to study glycosylation-driven Human pathologies, the current lack of a systems wide spatial glycomic view of zebrafish adult tissues and their determinants hinders a more fruitful functional dissection of the underlying molecular mechanisms. So far, only a restricted panel of glycans from the glycomes of zebrafish embryos and oocytes have ever been structurally defined 27 – 31 . These earlier studies established that zebrafish has the potential of synthesizing not only human-like glyco-epitopes, such as Lewis-x, Galβ1-4(Fucα1-3)GlcNAc, mono and di-sialylated T-antigens, ±Neu5Acα2-3Galβ1-3(Neu5Acα2-6)GalNAc, but also species-specific glycan motifs, such as the Galβ1-4(Neu5Ac/Gcα2-3)Galβ1-4(Fucα1-3)GlcNAc glyco-epitope and Fucα1-3GalNAcβ1-4 (Neu5Ac/Gcα2-3)Galβ1-3GalNAc O-glycans.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2018

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The emergence of zebrafish Danio rerio as a versatile model organism provides the unique opportunity to monitor the functions of glycosylation throughout vertebrate embryogenesis, providing insights into human diseases caused by glycosylation defects. Using a combination of chemical modifications, enzymatic digestion and mass spectrometry analyses, we establish here the precise glycomic profiles of eight individual zebrafish organs and demonstrate that the protein glycosylation and glycosphingolipid expression patterns exhibits exquisite specificity. Concomitant expression screening of a wide array of enzymes involved in the synthesis and transfer of sialic acids shows that the presence of organ-specific sialylation motifs correlates with the localized activity of the corresponding glycan biosynthesis pathways. These findings provide a basis for the rational design of zebrafish lines expressing desired glycosylation profiles.

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Section: Resultsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

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

et al. 2018

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“…The addition of sialic acid dramatically changes the physiological role of IgGs, converting them from pro-inflammatory to anti-inflammatory agents [ 6 , 44 ]. In the interactions between different functional elements of IgG glycosylation, it has been shown that the presence of bisecting GlcNAcs reduce galactosylated IgGs [ 6 , 45 , 46 ]. Accumulating evidence indicates that changes in IgG glycosylation mechanism could be part of the molecular mechanism leading to the promotion of inflammation [ 6 , 8 , 44 , 47 ]; therefore, our results indicate inflammation as one of characteristics in dyslipidaemia that can increase the risk of developing other related disorders.…”

Section: Discussionmentioning

confidence: 99%

The changes of immunoglobulin G N-glycosylation in blood lipids and dyslipidaemia

et al. 2018

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BackgroundAlternative N-glycosylation has significant structural and functional consequences on immunoglobulin G (IgG) and can affect immune responses, acting as a switch between pro- and anti-inflammatory IgG functionality. Studies have demonstrated that IgG N-glycosylation is associated with ageing, body mass index, type 2 diabetes and hypertension.MethodsHerein, we have demonstrated patterns of IgG glycosylation that are associated with blood lipids in a cross-sectional study including 598 Han Chinese aged 20–68 years. The IgG glycome composition was analysed by ultra-performance liquid chromatography.ResultsBlood lipids were positively correlated with glycan peak GP6, whereas they were negatively correlated with GP18 (P < 0.05/57). The canonical correlation analysis indicated that initial N-glycan structures, including GP4, GP6, GP9-12, GP14, GP17, GP18 and GP23, were significantly correlated with blood lipids, including total cholesterol, total triglycerides (TG) and low-density lipoprotein (r = 0.390, P < 0.001). IgG glycans patterns were able to distinguish patients with dyslipidaemia from the controls, with an area under the curve of 0.692 (95% confidence interval 0.644–0.740).ConclusionsOur findings indicated that a possible association between blood lipids and the observed loss of galactose and sialic acid, as well as the addition of bisecting GlcNAcs, which might be related to the chronic inflammation accompanying with the development and procession of dyslipidaemia.Electronic supplementary materialThe online version of this article (10.1186/s12967-018-1616-2) contains supplementary material, which is available to authorized users.

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“…More recently, a glycopeptide study reported that PMG‐conjugated peptides, in particular M2F‐glycopeptides (Glycans #10a/b) are prominent features of M. musculus synaptosomes (Trinidad et al ., ). M3 and M3F (Glycans #4 and #12) were also identified in deyolked embryos of Danio rerio (zebrafish), an important vertebrate model for human developmental studies (Hanzawa, Suzuki, & Natsuka, ).…”

Section: Human Pmps: Cues From Higher and Lower Eukaryotesmentioning

confidence: 99%

Human protein paucimannosylation: cues from the eukaryotic kingdoms

et al. 2019

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Paucimannosidic proteins (PMPs) are bioactive glycoproteins carrying truncated α-or β-mannosyl-terminating asparagine (N )-linked glycans widely reported across the eukaryotic domain. Our understanding of human PMPs remains limited, despite findings documenting their existence and association with human disease glycobiology. This review comprehensively surveys the structures, biosynthetic routes and functions of PMPs across the eukaryotic kingdoms with the aim of synthesising an improved understanding on the role of protein paucimannosylation in human health and diseases. Convincing biochemical, glycoanalytical and biological data detail a vast structural heterogeneity and fascinating tissue-and subcellular-specific expression of PMPs within invertebrates and plants, often comprising multi-α1,3/6-fucosylation and β1,2-xylosylation amongst other glycan modifications and non-glycan substitutions e.g. O-methylation. Vertebrates and protists express less-heterogeneous PMPs typically only comprising variable core fucosylation of bi-and trimannosylchitobiose core glycans. In particular, the Manα1,6Manβ1,4GlcNAc(α1,6Fuc)β1,4GlcNAcβAsn glycan (M2F) decorates various human neutrophil proteins reportedly displaying bioactivity and structural integrity demonstrating that they are not degradation products. Less-truncated paucimannosidic glycans (e.g. M3F) are characteristic glycosylation features of proteins expressed by human cancer and stem cells. Concertedly, these observations suggest the involvement of human PMPs in processes related to innate immunity, tumorigenesis and cellular differentiation. The absence of human PMPs in diverse bodily fluids studied under many (patho)physiological conditions suggests extravascular residence and points to localised functions of PMPs in peripheral tissues. Absence of PMPs in Fungi indicates that paucimannosylation is common, but not universally conserved, in eukaryotes. Relative to human PMPs, the expression of PMPs in plants, invertebrates and protists is more tissue-wide and constitutive yet, similar to their human counterparts, PMP expression remains regulated by the physiology of the producing organism and PMPs evidently serve essential functions in development, cell-cell communication and host-pathogen/symbiont interactions. In most PMP-producing organisms, including humans, the N -acetyl-β-hexosaminidase isoenzymes and linkage-specific α-mannosidases are glycoside hydrolases critical for generating PMPs via N -acetylglucosaminyltransferase I (GnT-I)-dependent and GnT-I-independent truncation pathways. However, the identity and structure of many species-specific PMPs in eukaryotes, their biosynthetic routes, strong tissue-and development-specific expression, and diverse functions are still elusive. Deep exploration of these PMP features involving, for example, the characterisation of endogenous PMP-recognising lectins across a variety of healthy and N -acetyl-β-hexosaminidase-deficient human tissue types and identification of microbial adhesins reactive to human PMPs, are amongs...

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Structures and developmental alterations ofN-glycans of zebrafish embryos

Cited by 30 publications

References 73 publications

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

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

The changes of immunoglobulin G N-glycosylation in blood lipids and dyslipidaemia

Human protein paucimannosylation: cues from the eukaryotic kingdoms

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