ABSTRACT
The human Phosphodiesterase 11 (PDE11) family is composed of four splice variants, namely PDE11A1, PDE11A2, PDE11A3, and PDE11A4. PDE11A is a 3',5'-cyclic adenosine monophosphate- and guanosine 3',5' -monophosphate (cGMP)-hydrolyzing enzyme although it is the most homologous among PDEs to PDE5A, a cGMP-PDE. Immunoblot analysis or immunohistochemistry of PDE11A protein has been reported in several papers. The human PDE11A gene is located in the 480 kb genomic DNA region of chromosome 2. Transcription of mRNAs of the four PDE11A splice variants is regulated by distinct promoters. Northern blot analysis has demonstrated that long forms of PDE11A mRNA are densely present in the prostate and that a short form of PDE11A mRNA can be found in the testis. PDE11A-specific inhibitors would help understand endogenous activities of PDE11A and its involvement in cyclic nucleotide hydrolysis in tissue extracts. PDE11A immunoreactive protein has been reported in human and mouse reproductive systems by immunohistochemistry with the polyclonal antibody against EPH-3.
