N-linked glycan structures of glycoproteins in suspension-cultured Arabidopsis thaliana MM2d cells

Fujiyama, Kazuhito; Tanaka, R.; Terashima, Masaaki; Seki, Tatsuji

doi:10.5511/plantbiotechnology.24.255

Cited by 5 publications

(5 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Multiple glycomics and glycoproteomics studies have been performed to investigate the natural glycosylation features of A. thaliana (Fujiyama et al ., ; Henquet et al ., ; Liebminger et al ., ; Ma et al ., ; Strasser et al ., , ; Xu et al ., ; Yoo et al ., ; Zeng et al ., ; Zhang et al ., ). These diverse studies spanned explorations of the biosynthetic machinery of A. thaliana through knockouts of genes encoding specific glycosylation enzymes to evaluation of the response to physiological stress under various conditions involving comparative glycoprofiling in different tissues, developmental stages and growth conditions.…”

Section: Surveying Pmps Across the Eukaryotic Kingdoms And Phylamentioning

confidence: 98%

Human protein paucimannosylation: cues from the eukaryotic kingdoms

et al. 2019

View full text Add to dashboard Cite

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...

show abstract

Section: Surveying Pmps Across the Eukaryotic Kingdoms And Phylamentioning

confidence: 98%

Human protein paucimannosylation: cues from the eukaryotic kingdoms

et al. 2019

View full text Add to dashboard Cite

show abstract

“…Hydrazine, TOF, glycans (2-AP), Exoglycosidase Structural determination of paucimannosidic glycans from suspension-culture in MM2d cells (Fujiyama, et al, 2007a) Arabidopsis thaliana Leaves PNGase A, TOF (DHB), highmannose and paucimannosidic glycans…”

Section: Total Glycoproteinsmentioning

confidence: 99%

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

Harvey

2011

Mass Spectrometry Reviews

View full text Add to dashboard Cite

This review is the fifth update of the original review, published in 1999, on the application of MALDI mass spectrometry to the analysis of carbohydrates and glycoconjugates and brings coverage of the literature to the end of 2008. The first section of the review covers fundamental studies, fragmentation of carbohydrate ions, use of derivatives and new software developments for analysis of carbohydrate spectra. Among newer areas of method development are glycan arrays, MALDI imaging and the use of ion mobility spectrometry. The second section of the review discusses applications of MALDI MS to the analysis of different types of carbohydrate. Specific compound classes that are covered include carbohydrate polymers from plants, N- and O-linked glycans from glycoproteins, biopharmaceuticals, glycated proteins, glycolipids, glycosides and various other natural products. There is a short section on the use of MALDI mass spectrometry for the study of enzymes involved in glycan processing and a section on the use of MALDI MS to monitor products of the chemical synthesis of carbohydrates with emphasis on carbohydrate-protein complexes and glycodendrimers. Corresponding analyses by electrospray ionization now appear to outnumber those performed by MALDI and the amount of literature makes a comprehensive review on this technique impractical. However, most of the work relating to sample preparation and glycan synthesis is equally relevant to electrospray and, consequently, those proposing analyses by electrospray should also find material in this review of interest.

show abstract

“…However, the second most predominant structures were M3FX in the early phase, GN 1 M3FX in the middle phase, and M3FX in the late phase. This N-glycosylation profile is quite different from that of A. thaliana MM2d (Fujiyama et al 2007), where M3FX was 70% of the total glycan.…”

mentioning

confidence: 78%

“…Plant-specific sugar residues have been suggested to be potentially immunogenic or allergenic (Altmann 2007;Bencúrová et al 2004;Jin et al 2008). Previously, we examined N-glycan structures derived from endogenous and soluble proteins of suspensioncultured cells of tobacco (Nicotiana tabacum) BY2 (Misaki et al 2001;Palacpac et al 1999) and A. thaliana MM2d (Fujiyama et al 2007), and showed that M3FX is the predominant structure. However, little is known about the effect of culture conditions on the Nglycosylation profile.…”

mentioning

confidence: 99%

<i>N</i>-Glycan structures of glycoproteins in suspension-cultured <i>Arabidopsis thaliana</i> T87 cells

Kajiura

Tanaka

Kato

et al. 2012

Plant Biotechnology

Self Cite

View full text Add to dashboard Cite

Suspension-cultured plant cells are feasible bioreactors for the production of pharmaceutical proteins. Posttranslational modification, such as glycosylation, is important for in vivo biological and physiological roles of proteins. However, little is known about the effect of suspension-culture conditions on protein N-glycosylation. In this study, we studied the N-glycan structures of soluble and endogenous glycoproteins at different growth stages of suspension-cultured Arabidopsis thaliana T87 cells. At the late growth stage, the amount of N-glycans with terminal N-acetylglucosamine (GlcNAc) decreased, whereas that of N-glycans with fucose and xylose increased. This indicates that N-glycans have more plant-specific sugar residues as the cultivation reaches the late or end stage of plant growth.

show abstract

N-linked glycan structures of glycoproteins in suspension-cultured Arabidopsis thaliana MM2d cells

Cited by 5 publications

References 29 publications

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Human protein paucimannosylation: cues from the eukaryotic kingdoms

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2007–2008

<i>N</i>-Glycan structures of glycoproteins in suspension-cultured <i>Arabidopsis thaliana</i> T87 cells

Contact Info

Product

Resources

About