Dephosphorylation of myo-inositol phosphates in the in vitro intestinal Caco-2 cell model |
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| Authors: | Karlis Briviba Margit Schollenberger Markus Rodehutscord Ralf Greiner |
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| Affiliation: | 1. Department of Physiology and Biochemistry of Nutrition, Max Rubner-Institut, Federal Research Institute of Nutrition and Food, Karlsruhe, Germany;2. Karlis.briviba@mri.bund.de;4. Institut für Nutztierwissenschaften, Universit?t Hohenheim, Stuttgart, Germany;5. Department of Food Technology and Bioprocess Engineering, Max Rubner-Institut, Federal Research Institute of Nutrition and Food, Karlsruhe, Germany |
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| Abstract: | ![]()
Plant and microbial phytases present in raw materials can cause a dephosphorylation of phytate (myo-inositol hexakisphosphate) (InsP6)) during food processing resulting in a broad range of different myo-inositol phosphates such as pentakisphosphate (InsP5) and tetrakisphosphate (InsP4) in foods. Here, we investigated whether the human intestinal epithelium is able to dephosphorylate myo-inositol phosphates (InsP6, InsP5-, InsP4-, InsP3-isomers) using an in vitro model with differentiated human Caco-2 cells cultured on semipermeable inserts. Incubation of InsP6 and an InsP5-isomer with cells for 3?h showed no dephosphorylation of both InsPs. Treatment of cells with a mixture of different InsP4-isomers, however, caused a formation of about 3.5% of an InsP3-isomer (Ins(1,5,6)P3) and treatment with a mixture of different InsP3-isomers caused about 20% formation of InsP2-isomers, respectively. Thus, human intestinal cells can contribute to the dephosphorylation of myo-inositol phosphates of partly dephosphorylated forms such as InsP3 and InsP4. |
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| Keywords: | Inositol phosphates phytate dephosphorylation intestinal epithelia Caco-2 cells |
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