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Molecular Basis for Vitamin A Uptake and Storage in Vertebrates

The ability to store and distribute vitamin A inside the body is the main evolutionary adaptation that allows vertebrates to maintain retinoid functions during nutritional deficiencies and to acquire new metabolic pathways enabling light-independent production of 11-cis retinoids. These processes gr...

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Autores principales: Chelstowska, Sylwia, Widjaja-Adhi, Made Airanthi K., Silvaroli, Josie A., Golczak, Marcin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5133064/
https://www.ncbi.nlm.nih.gov/pubmed/27792183
http://dx.doi.org/10.3390/nu8110676
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author Chelstowska, Sylwia
Widjaja-Adhi, Made Airanthi K.
Silvaroli, Josie A.
Golczak, Marcin
author_facet Chelstowska, Sylwia
Widjaja-Adhi, Made Airanthi K.
Silvaroli, Josie A.
Golczak, Marcin
author_sort Chelstowska, Sylwia
collection PubMed
description The ability to store and distribute vitamin A inside the body is the main evolutionary adaptation that allows vertebrates to maintain retinoid functions during nutritional deficiencies and to acquire new metabolic pathways enabling light-independent production of 11-cis retinoids. These processes greatly depend on enzymes that esterify vitamin A as well as associated retinoid binding proteins. Although the significance of retinyl esters for vitamin A homeostasis is well established, until recently, the molecular basis for the retinol esterification enzymatic activity was unknown. In this review, we will look at retinoid absorption through the prism of current biochemical and structural studies on vitamin A esterifying enzymes. We describe molecular adaptations that enable retinoid storage and delineate mechanisms in which mutations found in selective proteins might influence vitamin A homeostasis in affected patients.
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spelling pubmed-51330642016-12-11 Molecular Basis for Vitamin A Uptake and Storage in Vertebrates Chelstowska, Sylwia Widjaja-Adhi, Made Airanthi K. Silvaroli, Josie A. Golczak, Marcin Nutrients Review The ability to store and distribute vitamin A inside the body is the main evolutionary adaptation that allows vertebrates to maintain retinoid functions during nutritional deficiencies and to acquire new metabolic pathways enabling light-independent production of 11-cis retinoids. These processes greatly depend on enzymes that esterify vitamin A as well as associated retinoid binding proteins. Although the significance of retinyl esters for vitamin A homeostasis is well established, until recently, the molecular basis for the retinol esterification enzymatic activity was unknown. In this review, we will look at retinoid absorption through the prism of current biochemical and structural studies on vitamin A esterifying enzymes. We describe molecular adaptations that enable retinoid storage and delineate mechanisms in which mutations found in selective proteins might influence vitamin A homeostasis in affected patients. MDPI 2016-10-26 /pmc/articles/PMC5133064/ /pubmed/27792183 http://dx.doi.org/10.3390/nu8110676 Text en © 2016 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 Review
Chelstowska, Sylwia
Widjaja-Adhi, Made Airanthi K.
Silvaroli, Josie A.
Golczak, Marcin
Molecular Basis for Vitamin A Uptake and Storage in Vertebrates
title Molecular Basis for Vitamin A Uptake and Storage in Vertebrates
title_full Molecular Basis for Vitamin A Uptake and Storage in Vertebrates
title_fullStr Molecular Basis for Vitamin A Uptake and Storage in Vertebrates
title_full_unstemmed Molecular Basis for Vitamin A Uptake and Storage in Vertebrates
title_short Molecular Basis for Vitamin A Uptake and Storage in Vertebrates
title_sort molecular basis for vitamin a uptake and storage in vertebrates
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5133064/
https://www.ncbi.nlm.nih.gov/pubmed/27792183
http://dx.doi.org/10.3390/nu8110676
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