Visual cycle impairment in cellular retinaldehyde binding protein (CRALBP) knockout mice results in delayed dark adaptation

Neuron. 2001 Mar;29(3):739-48. doi: 10.1016/s0896-6273(01)00248-3.

Abstract

Mutations in the human CRALBP gene cause retinal pathology and delayed dark adaptation. Biochemical studies have not identified the primary physiological function of CRALBP. To resolve this, we generated and characterized mice with a non-functional CRALBP gene (Rlbp1(-/-) mice). The photosensitivity of Rlbp1(-/-) mice is normal but rhodopsin regeneration, 11-cis-retinal production, and dark adaptation after illumination are delayed by >10-fold. All-trans-retinyl esters accumulate during the delay indicating that isomerization of all-trans- to 11-cis-retinol is impaired. No evidence of photoreceptor degeneration was observed in animals raised in cyclic light/dark conditions for up to 1 year. Albino Rlbp(-/-) mice are protected from light damage relative to the wild type. These findings support a role for CRALBP as an acceptor of 11-cis-retinol in the isomerization reaction of the visual cycle.

Publication types

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

MeSH terms

  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology*
  • Dark Adaptation*
  • Electroretinography
  • Light
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Photoreceptor Cells / metabolism
  • Retina / physiopathology
  • Retinaldehyde / metabolism
  • Rhodopsin / metabolism
  • Vision, Ocular / physiology*

Substances

  • 11-cis-retinal-binding protein
  • Carrier Proteins
  • Rhodopsin
  • Retinaldehyde