Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases

Maley, Frank; Trimble, Robert B.; Tarentino, Anthony L.; Plummer, Thomas H.

doi:10.1016/0003-2697(89)90115-2

Cited by 733 publications

(524 citation statements)

References 74 publications

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“…6 demonstrate that this is unlikely to be the case. Endoglycosidase H requires Man-α(1-3)-Man-α(1-6)-Man-β(1-4)-GlcNAc-β(1-4)-GlcNAc-Asn as minimal structure in order to cleave the N-linked oligosaccharide from a glycoprotein [21]. The observation that the Toxoplasma glycoprotein is always resistant to the action of endoglycosidase H, but not PNGase F, indicates that this particular mannose is indeed absent from Toxoplasma N-linked oligosaccharides, supporting the notion that an ALG3-like enzyme activity is absent from the parasite.…”

Section: Discussionmentioning

confidence: 99%

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N-linked glycosylation of proteins in the protozoan parasite Toxoplasma gondii

Luk

Johnson

Beckers

2008

Molecular and Biochemical Parasitology

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Toxoplasma gondii is an obligate intracellular parasite of animal cells. Infection of humans is common and may result in devastating disease, especially in immunocompromised individuals. Despite previous reports that N-glycosylation of proteins may be a rare post-translational modification in this and related organisms, we demonstrate that it is actually quite prevalent in Toxoplasma. N-glycosylation is completely inhibited by treatment of parasites with tunicamycin, but this does not appear to exert its major effect on the parasites until they have egressed from their host cells. Although the tunicamycin-treated parasites appear structurally normal at this time they are not motile and mostly incapable of invading new host cells. The few tunicamycin-treated parasites that do invade are severely affected in their ability to replicate and accumulate with a distended endoplasmic reticulum, deformed nuclei, and without recognizable late secretory organelles. We provide experimental evidence that indicate that Toxoplasma N-glycans differ structurally from those in other eukaryotes.

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Section: Discussionmentioning

confidence: 99%

“…A) Structure of the typical core N-linked oligosaccharide on newly synthesized animal and yeast glycoproteins. B) Minimal N-linked oligosaccharide structure required for sensitivity to endoglycosidase H [21]. C) Predicted structure of N-linked oligosaccharide on newly synthesized glycoproteins in Toxoplasma gondii.…”

Section: Supplementary Materialsmentioning

confidence: 99%

N-linked glycosylation of proteins in the protozoan parasite Toxoplasma gondii

Luk

Johnson

Beckers

2008

Molecular and Biochemical Parasitology

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“…It has been reported that Endo-H cleaves between two N-acetylglucosamines of N-linked glycoproteins, and that PNGase F cleaves between the N-acetylglucosamine and the asparagine residue of N-linked glycoproteins. 19) Because hen egg OVA has one carbohydrate chain, it gave a band having slightly high mobility on SDS-PAGE after digestion with two glycosidases (lane 1 in Fig. 3A, B, and C).…”

Section: Deglycosylation and Glycosylation Profilingmentioning

confidence: 96%

Structural Characteristics of Hen Egg Ovalbumin Expressed in YeastPichia pastoris

Ito

Matsudomi

2005

Bioscience, Biotechnology, and Biochemistry

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“…Protein lysates were digested with PNGaseF and EndoH. PNGaseF cleaves all N-glycans, while EndoH specifically cleaves those N-glycans that have not been modified in the Golgi (Maley et al, 1989) (Figure 1c). Treatment with EndoH did not change CD26 mobility, indicating that the lower molecular mass of InvEE CD26 did not reflect incomplete maturation.…”

Section: Elevated Cd26 Levels and Activity In Invee Epidermismentioning

confidence: 99%

Upregulation of CD26 expression in epithelial cells and stromal cells during wound-induced skin tumour formation

et al. 2011

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We have previously described InvEE transgenic mice in which non-dividing, differentiating epidermal cells express oncogenically activated MAPK kinase 1 (MEK1). Skin wounding triggers tumour formation in InvEE mice via a mechanism that involves epidermal release of IL-1a and attraction of a pro-tumorigenic inflammatory infiltrate. To look for potential effects on the underlying connective tissue, we screened InvEE and wild-type epidermis for differential expression of cytokines and immune modulators. We identified a single protein, CD26 (dipeptidyl peptidase-4). CD26 serum levels were not increased in InvEE mice. In contrast, CD26 was upregulated in keratinocytes expressing mutant MEK1 and in the epithelial compartment of InvEE tumours, where it accumulated at cell-cell borders. CD26 expression was increased in dermal fibroblasts following skin wounding but was downregulated in tumour stroma. CD26 activity was stimulated by calcium-induced intercellular adhesion in keratinocytes, suggesting that the upregulation of CD26 in InvEE epidermis is due to expansion of the differentiated cell layers. IL-1a treatment of dermal fibroblasts stimulated CD26 activity, and therefore epidermal IL-1a release may contribute to the upregulation of CD26 expression in wounded dermis. Pharmacological blockade of CD26, via Sitagliptin, reduced growth of InvEE tumours, while combined inhibition of IL-1a and CD26 delayed tumour onset and reduced tumour incidence. Our results demonstrate that inappropriate activation of MEK1 in the epidermis leads to changes in dermal fibroblasts that, like the skin inflammatory infiltrate, contribute to tumour formation.

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Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases

Cited by 733 publications

References 74 publications

N-linked glycosylation of proteins in the protozoan parasite Toxoplasma gondii

N-linked glycosylation of proteins in the protozoan parasite Toxoplasma gondii

Structural Characteristics of Hen Egg Ovalbumin Expressed in YeastPichia pastoris

Upregulation of CD26 expression in epithelial cells and stromal cells during wound-induced skin tumour formation

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