Analysis and quantitation of mRNAs encoding the alpha- and beta-subunits of rod photoreceptor cGMP phosphodiesterase in neonatal retinal degeneration (rd) mouse retinas

Exp Eye Res. 2000 Aug;71(2):119-28. doi: 10.1006/exer.2000.0861.

Abstract

The retinal degeneration(rd) mouse is a commonly-studied animal model of the family of human-inherited retinal blindness known as retinitis pigmentosa, and is a likely model in which therapies for these conditions will continue to be developed and tested. Mutation of the beta-subunit of the rod photoreceptor cell-specific cyclic GMP phosphodiesterase is known to cause photoreceptor apoptosis in these mice. However, the molecular phenotype of this mutation in terms of quantitative levels of the phosphodiesterase alpha- and beta-subunit messenger RNAs remains unknown. In this study, the expression of the alpha- and beta-phosphodiesterase subunits is compared in C57BL/6J +/+, rd /+, and rd / rd mouse retinas. Using the techniques of quantitative reverse transcription polymerase chain reaction and quantitative in situ hybridization, the expression of the subunit mRNAs was measured in retinas of postnatal mice 0-14 days of age. Additionally, full length coding sequences were amplified for both subunits, and the beta-phosphodiesterase subunit mRNA was further evaluated for evidence of alternative splicing. Lastly, a relative decrease in expression of the mutant beta-phosphodiesterase allele in rd /+ mice was observed.

Publication types

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

MeSH terms

  • 3',5'-Cyclic-GMP Phosphodiesterases / genetics*
  • Animals
  • Animals, Newborn
  • DNA, Complementary / analysis
  • In Situ Hybridization
  • Mice
  • Mice, Inbred C57BL
  • RNA, Messenger / analysis*
  • Retinal Rod Photoreceptor Cells / enzymology*
  • Retinitis Pigmentosa / genetics*
  • Reverse Transcriptase Polymerase Chain Reaction / methods

Substances

  • DNA, Complementary
  • RNA, Messenger
  • 3',5'-Cyclic-GMP Phosphodiesterases