| First Author | Irías-Mata A | Year | 2020 |
| Journal | Molecules | Volume | 25 |
| Issue | 20 | PubMed ID | 33086686 |
| Mgi Jnum | J:325264 | Mgi Id | MGI:6705481 |
| Doi | 10.3390/molecules25204803 | Citation | Irias-Mata A, et al. (2020) alpha-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic alphaTocopherol Transfer Protein. Molecules 25(20) |
| abstractText | Tocomonoenols are vitamin E derivatives present in foods with a single double bond at carbon 11' in the sidechain. The alpha-tocopherol transfer protein (TTP) is required for the maintenance of normal alpha-tocopherol (alphaT) concentrations. Its role in the tissue distribution of alpha-11'-tocomonoenol (alphaT1) is unknown. We investigated the tissue distribution of alphaT1 and alphaT in wild-type (TTP(+/+)) and TTP knockout (TTP(-/-)) mice fed diets with either alphaT or alphaT1 for two weeks. alphaT1 was only found in blood, not tissues. alphaT concentrations in TTP(+/+) mice were in the order of adipose tissue > brain > heart > spleen > lungs > kidneys > small intestine > liver. Loss of TTP function depleted alphaT in all tissues. alphaT1, contrary to alphaT, was still present in the blood of TTP(-/-) mice (16% of alphaT1 in TTP(+/+)). Autoclaving and storage at room temperature reduced alphaT and alphaT1 in experimental diets. In conclusion, alphaT1 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 alphaT1 secretion. Future research should consider compound stability during autoclaving of rodent feed. |
