The gamma-subunit of the rod photoreceptor cGMP-binding cGMP-specific PDE is expressed in mouse lung

R J Tate, A Lochhead, H Brzeski, V Arshavsky, N J Pyne

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The type 6 phosphodiesterase (PDE-6) from retinal rod photoreceptors is an alpha beta gamma 2 heterotetramer. The alpha- and beta-subunits contain catalytic sites for cGMP hydrolysis, whereas the gamma-subunits (P gamma) serve as a protein inhibitor of the enzyme. P gamma is believed to be expressed only in photoreceptors. Using RT-PCR, we have amplified the complete coding sequence for P gamma from mouse lung RNA. The expression of P gamma in this tissue may be related to its ability to interact the type 5 phosphodiesterase (PDE-5), which is the predominant cGMP binding protein in lung. We therefore suggest that P gamma may have a wider signaling role in mammalian cells than previously appreciated.
Original languageEnglish
Pages (from-to)133-144
Number of pages12
JournalCell Biochemistry and Biophysics
Volume29
Issue number1-2
DOIs
Publication statusPublished - 1998

Keywords

  • 3',5'-cyclic-GMP phosphodiesterases
  • amino acid sequence
  • animals
  • base sequence
  • cyclic AMP-dependent protein kinases
  • cyclic nucleotide phosphodiesterases, type 5
  • cyclic nucleotide phosphodiesterases, Type 6
  • enzyme activation
  • lung
  • mice
  • molecular sequence data
  • RNA, messenger
  • rod cell outer segment

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