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Related Experiment Videos

Retinyl esters are the substrate for isomerohydrolase.

Gennadiy Moiseyev1, Rosalie K Crouch, Patrice Goletz

  • 1Department of Ophthalmology, Medical University of South Carolina, Charleston, South Carolina 29425, USA.

Biochemistry
|February 20, 2003
PubMed
Summary

This study reveals that retinyl esters, not all-trans retinol, are the substrate for the visual cycle

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Vision Science

Background:

  • The visual cycle is crucial for sight, involving the regeneration of 11-cis retinal in the retinal pigment epithelium (RPE).
  • The specific substrate for the isomerization enzyme remains unidentified, with both all-trans retinol and retinyl esters being proposed.
  • Understanding this step is key to comprehending visual pigment regeneration and potential vision disorders.

Purpose of the Study:

  • To definitively identify the substrate of the isomerase enzyme responsible for 11-cis retinal regeneration in the RPE.
  • To elucidate the role of retinyl esters versus all-trans retinol in the visual cycle's isomerization process.

Main Methods:

  • Incubation of bovine RPE microsomes with radiolabeled all-trans retinol and all-trans retinyl palmitate.

Related Experiment Videos

  • Utilizing LRAT inhibitors (AcDCMK) and CRBP to assess substrate involvement.
  • Comparing isomerase activity in RPE65 knockout mice with wild-type mice.

    • Main Results:

    • 11-cis retinol production correlated with retinyl ester levels, not all-trans retinol levels.
    • Inhibition of LRAT or CRBP diminished both retinyl ester and 11-cis retinol generation.
    • RPE65 knockout mice lacked isomerase activity but retained LRAT activity, accumulating excess retinyl esters.
    • Direct incubation with all-trans retinyl palmitate yielded 11-cis retinol.

    Conclusions:

    • Retinyl esters are the direct substrate for the isomerization reaction in the visual cycle.
    • This finding clarifies a critical step in visual pigment regeneration and RPE function.