Molecular Basis for Vitamin A Uptake and Storage in Vertebrates

Nutrients. 2016 Oct 26;8(11):676. doi: 10.3390/nu8110676.

Abstract

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.

Keywords: lecithin:retinol acyltransferase (LRAT); lipid metabolism; retinol; visual cycle; vitamin A.

Publication types

  • Review

MeSH terms

  • Acyltransferases / chemistry
  • Acyltransferases / genetics
  • Acyltransferases / metabolism
  • Animals
  • Biocatalysis
  • Biological Transport
  • Biological Transport, Active
  • Carboxylic Ester Hydrolases / chemistry
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism
  • Esterification
  • Evolution, Molecular
  • Humans
  • Intestinal Absorption*
  • Intestinal Mucosa / enzymology
  • Intestinal Mucosa / metabolism
  • Liver / enzymology
  • Liver / metabolism
  • Models, Biological*
  • Mutation
  • Protein Conformation
  • Vertebrates / physiology*
  • Visual Pathways / enzymology
  • Visual Pathways / metabolism
  • Vitamin A / metabolism*

Substances

  • Vitamin A
  • Acyltransferases
  • lecithin-retinol acyltransferase
  • Carboxylic Ester Hydrolases
  • retinyl esterase