title: Molecular Basis for Vitamin A Uptake and Storage in Vertebrates.
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-cisretinoids. 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.
authors: Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. sxc968@case.edu.|Laboratory of Hematology and Flow Cytometry, Department of Hematology, Military Institute of Medicine, PL 04-141 Warsaw, Poland. sxc968@case.edu.
authors: Sylwia
authors: S
authors: Chelstowska
authors: Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. nkw5@case.edu.
authors: Made Airanthi K
authors: MA
authors: Widjaja-Adhi
authors: Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. jxs1329@case.edu.
authors: Josie A
authors: JA
authors: Silvaroli
authors: Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. mxg149@case.edu.|Cleveland Center for Membrane and Structural Biology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA. mxg149@case.edu.
authors: Marcin
authors: M
authors: Golczak
mesh_terms: D000217:Acyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000818:Animals; D055162:Biocatalysis; D001692:Biological Transport; D001693:Biological Transport, Active; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D004951:Esterification; D019143:Evolution, Molecular; D006801:Humans; D007408:Intestinal Absorption; D007413:Intestinal Mucosa / Q000201:enzymology / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000378:metabolism; D008954:Models, Biological; D009154:Mutation; D011487:Protein Conformation; D014714:Vertebrates / Q000502:physiology*; D014795:Visual Pathways / Q000201:enzymology / Q000378:metabolism; D014801:Vitamin A / Q000378:metabolism*
chemical_list: D014801:Vitamin A; D000217:Acyltransferases; C056942:lecithin-retinol acyltransferase; D002265:Carboxylic Ester Hydrolases; C022523:retinyl esterase
keywords: lecithin:retinol acyltransferase (LRAT); lipid metabolism; retinol; visual cycle; vitamin A