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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

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 (αT(1)) is...

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Autores principales: Irías-Mata, Andrea, Sus, Nadine, Hug, Maria-Lena, Müller, Marco, Vetter, Walter, Frank, Jan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7588010/
https://www.ncbi.nlm.nih.gov/pubmed/33086686
http://dx.doi.org/10.3390/molecules25204803
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author Irías-Mata, Andrea
Sus, Nadine
Hug, Maria-Lena
Müller, Marco
Vetter, Walter
Frank, Jan
author_facet Irías-Mata, Andrea
Sus, Nadine
Hug, Maria-Lena
Müller, Marco
Vetter, Walter
Frank, Jan
author_sort Irías-Mata, Andrea
collection PubMed
description 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 (αT(1)) is unknown. We investigated the tissue distribution of αT(1) and αT in wild-type (TTP(+/+)) and TTP knockout (TTP(−/−)) mice fed diets with either αT or αT(1) for two weeks. αT(1) 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. αT(1), contrary to αT, was still present in the blood of TTP(−/−) mice (16% of αT(1) in TTP(+/+)). Autoclaving and storage at room temperature reduced αT and αT(1) in experimental diets. In conclusion, αT(1) 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 αT(1) secretion. Future research should consider compound stability during autoclaving of rodent feed.
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spelling pubmed-75880102020-10-29 α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α-Tocopherol Transfer Protein Irías-Mata, Andrea Sus, Nadine Hug, Maria-Lena Müller, Marco Vetter, Walter Frank, Jan Molecules Article 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 (αT(1)) is unknown. We investigated the tissue distribution of αT(1) and αT in wild-type (TTP(+/+)) and TTP knockout (TTP(−/−)) mice fed diets with either αT or αT(1) for two weeks. αT(1) 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. αT(1), contrary to αT, was still present in the blood of TTP(−/−) mice (16% of αT(1) in TTP(+/+)). Autoclaving and storage at room temperature reduced αT and αT(1) in experimental diets. In conclusion, αT(1) 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 αT(1) secretion. Future research should consider compound stability during autoclaving of rodent feed. MDPI 2020-10-19 /pmc/articles/PMC7588010/ /pubmed/33086686 http://dx.doi.org/10.3390/molecules25204803 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Irías-Mata, Andrea
Sus, Nadine
Hug, Maria-Lena
Müller, Marco
Vetter, Walter
Frank, Jan
α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α-Tocopherol Transfer Protein
title α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α-Tocopherol Transfer Protein
title_full α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α-Tocopherol Transfer Protein
title_fullStr α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α-Tocopherol Transfer Protein
title_full_unstemmed α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α-Tocopherol Transfer Protein
title_short α-Tocomonoenol Is Bioavailable in Mice and May Partly Be Regulated by the Function of the Hepatic α-Tocopherol Transfer Protein
title_sort α-tocomonoenol is bioavailable in mice and may partly be regulated by the function of the hepatic α-tocopherol transfer protein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7588010/
https://www.ncbi.nlm.nih.gov/pubmed/33086686
http://dx.doi.org/10.3390/molecules25204803
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