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  • α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α‑Tocopherol Transfer Protein.

α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α‑Tocopherol Transfer Protein.

Molecules (Basel, Switzerland) (2020-10-23)
Andrea Irías-Mata, Nadine Sus, Maria-Lena Hug, Marco Müller, Walter Vetter, Jan Frank
摘要

Tocomonoenols are vitamin E derivatives present in foods with a single double bond at carbon 11' in the sidechain. The α-tocopherol transfer protein (TTP) is required for the maintenance of normal α-tocopherol (αT) concentrations. Its role in the tissue distribution of α-11'-tocomonoenol (αT1) is unknown. We investigated the tissue distribution of αT1 and αT in wild-type (TTP+/+) and TTP knockout (TTP-/-) mice fed diets with either αT or αT1 for two weeks. αT1 was only found in blood, not tissues. αT concentrations in TTP+/+ mice were in the order of adipose tissue > brain > heart > spleen > lungs > kidneys > small intestine > liver. Loss of TTP function depleted αT in all tissues. αT1, contrary to αT, was still present in the blood of TTP-/- mice (16% of αT1 in TTP+/+). Autoclaving and storage at room temperature reduced αT and αT1 in experimental diets. In conclusion, αT1 is bioavailable, reaches the blood in mice, and may not entirely depend on TTP function for secretion into the systemic circulation. However, due to instability of the test compounds in the experimental diets, further in vivo experiments are required to clarify the role of TTP in αT1 secretion. Future research should consider compound stability during autoclaving of rodent feed.

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Sigma-Aldrich
Triton X-100, laboratory grade
Sigma-Aldrich
胸腺嘧啶核苷5′-三磷酸 钠盐, ≥96%
Sigma-Aldrich
Goat Anti-Rabbit IgG, H & L Chain Specific Peroxidase Conjugate, liquid, Calbiochem®