Major retinal autoantigens remain stably expressed during all stages of spontaneous uveitis

Mol Immunol. 2007 Jul;44(13):3291-6. doi: 10.1016/j.molimm.2007.02.027. Epub 2007 Apr 27.

Abstract

Equine recurrent uveitis (ERU) is a valuable model for autoimmune diseases, since it develops frequently and occurs spontaneously. We investigated the overall expression level of three major retinal autoantigens in normal retinas and various ERU stages. Analysis of retinal proteomes of both, healthy and diseased retinas revealed an almost unaffected expression of IRBP, S-antigen and cRALBP in ERU cases. Validation of these findings with western blots and immunohistochemistry confirmed constant to increased expression of these autoantigens, although loss of their physiological expression sites within retina is evident. In contrast to stable expression of autoantigens, rhodopsin, the major component of phototransduction in photoreceptors, disappeared from destructed retinas. These results explain persistent uveitic attacks even in severely damaged eyes and draw the attention to further investigations of biological pathways and regulations in autoimmune target tissues.

Publication types

  • Research Support, Non-U.S. Gov't
  • Validation Study

MeSH terms

  • Animals
  • Arrestin / biosynthesis
  • Arrestin / genetics
  • Autoantigens / biosynthesis*
  • Autoantigens / genetics*
  • Carrier Proteins / biosynthesis
  • Carrier Proteins / genetics
  • Eye Proteins / biosynthesis
  • Eye Proteins / genetics
  • Gene Expression Regulation / immunology
  • Horses
  • Recurrence
  • Retina / immunology*
  • Retina / metabolism
  • Retina / pathology
  • Retinol-Binding Proteins / biosynthesis
  • Retinol-Binding Proteins / genetics
  • Rhodopsin / biosynthesis
  • Rhodopsin / genetics
  • Uveitis / immunology*
  • Uveitis / metabolism*
  • Uveitis / pathology

Substances

  • 11-cis-retinal-binding protein
  • Arrestin
  • Autoantigens
  • Carrier Proteins
  • Eye Proteins
  • Retinol-Binding Proteins
  • interstitial retinol-binding protein
  • Rhodopsin