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|In vitro digestion of heat treated cashew nut
Reitsma, M. ; Bastiaan-Net, S. ; Wichers, H.J. - \ 2014
Protein transport across the small intestine in food hypersensitivity
Reitsma, M. ; Westerhout, J. ; Wichers, H.J. ; Wortelboer, H. ; Verhoeckx, K.C.M. - \ 2014
Molecular Nutrition & Food Research 58 (2014)1. - ISSN 1613-4125 - p. 194 - 205.
transepithelial antigen transport - undegraded dietary antigen - simulated gastric fluid - human peyers-patches - dendritic cells - macromolecular transport - in-vitro - beta-lactoglobulin - immune-system - epithelial exosomes
In view of the imminent deficiency of protein sources for human consumption in the near future, new protein sources need to be identified. However, safety issues such as the risk of allergenicity are often a bottleneck, due to the absence of predictive, validated and accepted methods for risk assessment. The current strategy to assess the allergenic potential of proteins focuses mainly on homology, stability and cross-reactivity, although other factors such as intestinal transport might be of added value too. In this review, we present an overview of the knowledge of protein transport across the intestinal wall and the methods currently being used to measure this. A literature study reveals that protein transport in sensitised persons occurs para-cellularly with the involvement of mast cells, and trans-cellularly via enterocytes, while in non-sensitised persons micro-fold cells and enterocytes are considered most important. However, there is a lack of comparable systematic studies on transport of allergenic proteins. Knowledge of the multiple protein transport pathways and which model system can be useful to study these processes may be of added value in the risk assessment of food allergenicity.
Endocrine disrupting effects of thioxanthone photoinitiators
Reitsma, M. ; Bovee, T.F.H. ; Peijnenburg, A.A.C.M. ; Hendriksen, P.J.M. ; Hoogenboom, L.A.P. ; Rijk, J.C.W. - \ 2013
Toxicological sciences 132 (2013)1. - ISSN 1096-6080 - p. 64 - 74.
tandem mass-spectrometry - cell-line - liquid-chromatography - gas-chromatography - in-vitro - expression - bioassay - itx - steroidogenesis - protein
Photoinitiators used in food packaging ink, such as 2-isopropylthioxanthone (2-ITX), have been shown to migrate into food and beverages. Recently, several studies indicated that 2-ITX might be an endocrine disrupting chemical. In the present work, the effects of 2-ITX, 4-isopropylthioxanthone (4-ITX), 2,4-diethylthioxanthone (2,4-diethyl-TX), 2-chlorothioxanthone (2-chloro-TX) and 1-chloro-4-propoxythioxanthone (1-chloro-4-propoxy-TX) on steroidogenesis and androgen and estrogen receptor-mediated transcription activation have been studied using human H295R adrenocarcinoma cells and yeast hormone bioassays, respectively. None of the compounds showed androgenic or estrogenic activities, but clear anti-androgenic as well as anti-estrogenic activities were observed for 2-ITX, 4-ITX and 2,4-diethyl-TX, while 2-chloro-TX showed only anti-androgenic activity. In an adapted version of the H295R steroidogenesis assay, using gas chromatography-tandem mass spectrometry analysis of H295R media, all five compounds increased levels of 17ß-estradiol and estrone. H295R cells incubated with 2-ITX also showed significantly reduced androgen and increased pregnenolone and progesterone levels. Expression of particular steroidogenic genes, including the one encoding for aromatase (CYP19A1), were significantly up-regulated after incubation of H295R cells with 2-ITX, 4-ITX and 2,4-diethyl-TX. In line with the increased CYP19A1 mRNA expression, 2-ITX increased catalytic activity of aromatase in H295R cells as measured by cognate aromatase assays. The results indicate that thioxanthone derivatives can act as potential endocrine disruptors both at the level of nuclear receptor signalling and steroid hormone production.
B-glucans are involved in immune-modulation of THP-1
Chanput, W. ; Reitsma, M. ; Kleinjans, L. ; Mes, J.J. ; Savelkoul, H.F.J. ; Wichers, H.J. - \ 2012
Molecular Nutrition & Food Research 56 (2012)5. - ISSN 1613-4125 - p. 822 - 833.
lactic-acid bacteria - factor-kappa-b - cell-line - cytokine production - interferon-gamma - dendritic cells - receptor - lentinan - mice - lipopolysaccharide
Scope We aimed to examine different immunological aspects of ß-glucans derived from different food sources (oat, barley and shiitake) on phorbol myristate acetate (PMA)-differentiated THP-1 macrophages. Commercially purified barley ß-glucan (commercial BG) and lentinan were included to compare ß-glucans from the same origin but different degree of purity and processing. Methods and results Chemical composition and molecular weight distribution of ß-glucan samples were determined. Inflammation-related gene expression kinetics (IL-1ß, IL-8, nuclear factor kappa B [NF-¿B] and IL-10) after 3, 6 and 24 h of stimulation with 100 µg/mL ß-glucan were investigated. All tested ß-glucans mildly upregulated the observed inflammation-related genes with differential gene expression patterns. Similar gene expression kinetics, but different fold induction values, was found for the crude ß-glucan extracts and their corresponding commercial forms. Pre-incubation of THP-1 macrophages with ß-glucans prior to lipopolysaccharide (LPS) exposure decreased the induction of inflammation-related genes compared to LPS treatment. No production of nitric oxide (NO) and hydrogen peroxide (H2O2) was detected in ß-glucan stimulated THP-1 macrophages. Phagocytic activity was not different after stimulation by ß-glucan samples. Conclusion Based on these in vitro analyses, it can be concluded that the analysed ß-glucans have varying levels of immunomodulating properties, which are likely related to structure, molecular weight and compositional characteristic of ß-glucan