Noninvasive two-photon imaging reveals retinyl ester storage structures in the eye

J Cell Biol. 2004 Feb 2;164(3):373-83. doi: 10.1083/jcb.200311079. Epub 2004 Jan 26.

Abstract

Visual sensation in vertebrates is triggered when light strikes retinal photoreceptor cells causing photoisomerization of the rhodopsin chromophore 11-cis-retinal to all-trans-retinal. The regeneration of preillumination conditions of the photoreceptor cells requires formation of 11-cis-retinal in the adjacent retinal pigment epithelium (RPE). Using the intrinsic fluorescence of all-trans-retinyl esters, noninvasive two-photon microscopy revealed previously uncharacterized structures (6.9 +/- 1.1 microm in length and 0.8 +/- 0.2 microm in diameter) distinct from other cellular organelles, termed the retinyl ester storage particles (RESTs), or retinosomes. These structures form autonomous all-trans-retinyl ester-rich intracellular compartments distinct from other organelles and colocalize with adipose differentiation-related protein. As demonstrated by in vivo experiments using wild-type mice, the RESTs participate in 11-cis-retinal formation. RESTs accumulate in Rpe65-/- mice incapable of carrying out the enzymatic isomerization, and correspondingly, are absent in the eyes of Lrat-/- mice deficient in retinyl ester synthesis. These results indicate that RESTs located close to the RPE plasma membrane are essential components in 11-cis-retinal production.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acyltransferases / genetics
  • Acyltransferases / metabolism
  • Animals
  • Carrier Proteins
  • Cytoplasmic Vesicles / chemistry*
  • Cytoplasmic Vesicles / metabolism
  • Diterpenes
  • Esters / analysis*
  • Eye / chemistry
  • Eye / metabolism*
  • Eye / ultrastructure
  • Eye Proteins
  • Membrane Proteins / metabolism
  • Mice
  • Mice, Inbred Strains
  • Mice, Knockout
  • Microscopy, Fluorescence / methods
  • Models, Molecular
  • Molecular Structure
  • Perilipin-2
  • Pigment Epithelium of Eye / cytology
  • Pigment Epithelium of Eye / metabolism*
  • Proteins / genetics
  • Proteins / metabolism
  • Retinaldehyde / administration & dosage
  • Retinaldehyde / chemistry
  • Retinaldehyde / metabolism*
  • Visual Perception / physiology*
  • Vitamin A / chemistry*
  • Vitamin A / metabolism
  • cis-trans-Isomerases

Substances

  • Carrier Proteins
  • Diterpenes
  • Esters
  • Eye Proteins
  • Membrane Proteins
  • Perilipin-2
  • Plin2 protein, mouse
  • Proteins
  • Vitamin A
  • 9-cis-retinal
  • Acyltransferases
  • lecithin-retinol acyltransferase
  • retinoid isomerohydrolase
  • cis-trans-Isomerases
  • Retinaldehyde