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In Vitro and Animal Studies

Dephosphorylation of myo-inositol phosphates in the in vitro intestinal Caco-2 cell model

, , ORCID Icon & ORCID Icon
Pages 46-51 | Received 24 Jan 2017, Accepted 10 May 2017, Published online: 30 May 2017
 

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.

Graphical Abstract

Acknowledgements

We gratefully acknowledge the excellent technical assistance of R. Lambertz, B. Mathony-Holschuh and M. Liebscher.

Disclosure statement

The authors report no conflicts of interest.

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