Analysis and quantitation of mRNAs encoding the alpha- and beta-subunits of rod photoreceptor cGMP phosphodiesterase in neonatal retinal degeneration (rd) mouse retinas.
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.
Phelan
J K
JK
Department of Neurobiology, University of California, Los Angeles 90095, USA.
Bok
D
D
D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000235:genetics*; D000818:Animals; D000831:Animals, Newborn; D018076:DNA, Complementary / Q000032:analysis; D017403:In Situ Hybridization; D051379:Mice; D008810:Mice, Inbred C57BL; D012333:RNA, Messenger / Q000032:analysis*; D017948:Retinal Rod Photoreceptor Cells / Q000201:enzymology*; D012174:Retinitis Pigmentosa / Q000235:genetics*; D020133:Reverse Transcriptase Polymerase Chain Reaction / Q000379:methods
D018076:DNA, Complementary; D012333:RNA, Messenger; D015106:3',5'-Cyclic-GMP Phosphodiesterases