Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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    We will mail you new results for this query: keywords==deglycosylation
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Combining an in vitro reporter gene assay with metabolomics to identify tomato phytochemicals responsible for inducing electrophile-responsive element (EpRE)-mediated gene transcription
Eekelen, H.D.L.M. van; Gijsbers, L. ; Maliepaard, C.A. ; Vreeburg, R.A.M. ; Finkers, H.J. ; Tikunov, Y.M. ; Gomez Roldan, M.V. ; Haan, L.H.J. de; Vos, R.C.H. de; Aarts, J.M.M.J.G. ; Rietjens, I. ; Bovy, A.G. - \ 2015
Metabolomics 11 (2015)2. - ISSN 1573-3882 - p. 302 - 311.
solanum-lycopersicon - mass-spectrometry - fruit - expression - health - metabolism - flavonoids - lycopene - deglycosylation - polyphenols
The electrophile-responsive element (EpRE) is a transcriptional enhancer involved in cancer-chemoprotective gene expression effects of certain dietary compounds. In this study we measured the ability of extracts of glycosidase treated tomato fruits from 97 different accessions to induce EpRE-mediated luciferase expression using EpRE-LUX reporter cells and analyzed the same extracts using LC–MSbased untargeted metabolomics profiling. We were able to pinpoint those tomato compounds that were most correlated with EpRE-mediated luciferase induction, by combining reporter gene assay data with the metabolic profiles of the same extracts. Flavonoids were the compounds showing the strongest positive correlation with EpRE-LUX activity. These results were validated using a transgenic tomato line accumulating high levels of flavonoids. Results obtained corroborated that flavonoids are an important determinant of the ability of tomato fruit extracts to induce EpRE-mediated beneficial health effects. Overall, these results indicate that combining untargeted metabolomics with reporter gene assays provides a powerful tool for nutritionists, plant breeders and food chemists towards identification of potential health-beneficial constituents of tomato fruits, as well as of other crops and products derived thereof.
N-glycan occupancy of Arabidopsis N-glycoproteins
Song, W. ; Mentink, R. ; Henquet, M.G.L. ; Cordewener, J.H.G. ; Dijk, A.D.J. van; Bosch, H.J. ; America, A.H.P. ; Krol, A.R. van der - \ 2013
Journal of Proteomics 93 (2013). - ISSN 1874-3919 - p. 343 - 355.
lectin affinity-chromatography - mass-spectrometry - glycosylated proteins - linked glycoproteins - identification - plants - glycopeptides - deglycosylation - glycomics - precursor
Most secreted proteins in eukaryotes are modified on the amino acid consensus sequence NxS/T by an N-glycan through the process of N-glycosylation. The N-glycans on glycoproteins are processed in the endoplasmic reticulum (ER) to different mannose-type N-glycans or, when the protein passes through the Golgi apparatus, to different complex glycan forms. Here we describe the capturing of N-glycopeptides from a trypsin digest of total protein extracts of Arabidopsis plants and release of these captured peptides following Peptide N-glycosidase (PNGase) treatment for analysis of N-glycan site-occupancy. The mixture of peptides released as a consequence of the PNGase treatment was analyzed by two dimensional nano-LC–MS. As the PNGase treatment of glycopeptides results in the deamidation of the asparagine (N) in the NxS/T site of the released peptide, this asparagine (N) to aspartic acid (D) conversion is used as a glycosylation ‘signature’. The efficiency of PNGase F and PNGase A in peptide release is discussed. The identification of proteins with a single glycopeptide was limited by the used search algorithm but could be improved using a reference database including deamidated peptide sequences. Additional stringency settings were used for filtering results to minimize false discovery. This resulted in identification of 330 glycopeptides on 173 glycoproteins from Arabidopsis, of which 28 putative glycoproteins, that were previously not annotated as secreted protein in The Arabidopsis Information Resource database (TAIR). Furthermore, the identified glycosylation site occupancy helped to determine the correct topology for membrane proteins. A quantitative comparison of peptide signal was made between wild type and complex-glycan-less (cgl) mutant Arabidopsis from three replicate leaf samples using a label-free MS peak comparison. As an example, the identified membrane protein SKU5 (AT4G12420) showed differential glycopeptide intensity ratios between WT and cgl indicating heterogeneous glycan modification on single protein.
The cytosolic B-glucosidase GBA3 does not influence type 1 Gaucher disease manifestation
Dekker, N. ; Voorn-Brouwer, T. ; Verhoek, M. ; Wennekes, T. ; Narayan, R.S. ; Speijer, D. ; Hollak, C.E.M. ; Overkleeft, H.S. ; Boot, R.G. ; Aerts, J.M.F.G. - \ 2011
Blood Cells Molecules and Diseases 46 (2011)1. - ISSN 1079-9796 - p. 19 - 26.
klotho-related protein - human-liver - nonlysosomal glucosylceramidase - marked elevation - specificity - glucocerebrosidase - phenotype - beta-glucosidase-2 - deglycosylation - identification
GBA3, also known as cytosolic ß-glucosidase, is thought to hydrolyze xenobiotic glycosides in man. Deficiency of glucocerebrosidase (GBA), a ß-glucosidase degrading glucosylceramide, underlies Gaucher disease. We examined GBA3, which recently was proposed to degrade glucosylceramide and influence the clinical manifestation of Gaucher disease. Recombinant GBA3 was found to hydrolyze artificial substrates such as 4-methylumbelliferyl-ß-D-glucoside and C6-NBD-glucosylceramide, but hydrolysis of naturally occurring lipids like glucosylceramide and glucosylsphingosine was hardly detected. Consistent with this, inhibition of GBA3 in cultured cells using a novel inhibitor (alpha-1-C-nonyl-DIX) did not result in an additional increase in glucosylceramide as compared to GBA inhibition alone. Examination of the GBA3 gene led to the identification of a common substitution in its open reading frame (1368T¿A), resulting in a truncated GBA3 protein missing the last a-helix of its (ß/a)8 barrel. Both recombinant 1368A GBA3 and 1368A enzyme from spleen of a homozygous individual were found to be inactive. Amongst non-neuronopathic (type 1) Gaucher disease patients, we subsequently identified individuals being wild-type, heterozygous, or homozygous for the GBA3 1368T¿A mutation. No correlation was observed between GBA3 1368A/T haplotypes and severity of type 1 Gaucher disease manifestation. In conclusion, GBA3 does not seem to modify type 1 Gaucher disease manifestation
The type of sugar moiety is a major determinant of the small intestinal uptake and subsequent biliary excretion of dietary quercetin glycosides
Arts, I.C.W. ; Sesink, A.L.A. ; Faassen, M. ; Hollman, P.C.H. - \ 2004
British Journal of Nutrition 91 (2004)6. - ISSN 0007-1145 - p. 841 - 847.
lactase-phlorhizin hydrolase - conjugated derivatives - flavonoid glycosides - rat plasma - bioavailability - absorption - quercetin-3-glucoside - humans - quercetin-4'-glucoside - deglycosylation
Quercetin is an important dietary flavonoid with putative beneficial effects in the prevention of cancer and CVD. The in vivo bioactivity of quercetin depends on its bioavailability, which varies widely between foods. We used an in situ rat intestinal perfusion model to study whether differential small intestinal hydrolysis of the sugar moiety of five naturally occurring quercetin glycosides determines the small intestinal uptake and subsequent biliary excretion of quercetin. After 30 min perfusion, a decrease of intact quercetin glycoside in perfusate was observed for quercetin-3-O-beta-glucoside (20.9 (SEM 1-4) mumol/l) and quercetin-4'-O-beta-glucoside (23.5 (SEM 1-6) mumol/l), but not of quercetin-3-O-beta-galactoside, quercetin-3-O-beta-rhamnoside and quercetin-3-O-alpha-arabinopyranoside. Appearance of free quercetin in perfusate and conjugated quercetin metabolites (quercetin, isorhammetin, and tamarixetin) in portal and peripheral plasma and bile were also significantly greater after treatment with quercetin-3-O-beta-glucoside or quercetin-4'-O-beta-glucoside compared with any of the other glycosides. Thus, the type of sugar moiety is a major determinant of the small intestinal absorption of quercetin glycosides, but the position (3 or 4') of the glucose moiety does not further influence absorption. The poor bioavailability of important dietary quercetin glycosides has implications for their in vivo bioactivities.
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