Retinal S antigen identified as the 48K protein regulating light-dependent phosphodiesterase in rods

Science. 1985 May 17;228(4701):891-3. doi: 10.1126/science.2988124.

Abstract

Retinal S antigen chromatographically purified from whole retina, induces experimental autoimmune uveoretinitis in laboratory animals. The 48K protein, a soluble protein found in rod outer segments, is purified through its specific binding to photoexcited rhodopsin and is involved in the quenching of light-induced guanosine 3',5'-monophosphate-phosphodiesterase activity. Biochemical, immunological, functional, and pathological tests showed that retinal S antigen and the 48K protein are identical.

Publication types

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

MeSH terms

  • 3',5'-Cyclic-GMP Phosphodiesterases / metabolism*
  • Animals
  • Antigens* / isolation & purification
  • Arrestin
  • Autoimmune Diseases / etiology
  • Cattle
  • Eye Proteins / immunology
  • Eye Proteins / isolation & purification
  • Eye Proteins / pharmacology
  • Light
  • Molecular Weight
  • Photoreceptor Cells / enzymology*
  • Rats
  • Retina / analysis
  • Retina / immunology*
  • Rod Cell Outer Segment / analysis
  • Rod Cell Outer Segment / immunology
  • Uveitis / etiology

Substances

  • Antigens
  • Arrestin
  • Eye Proteins
  • 3',5'-Cyclic-GMP Phosphodiesterases