Cloning and characterization of two splice variants of human phosphodiesterase 11A

• DOI: 10.1073/pnas.200355397
• Publication Date: 2002-07-26T14:36:44Z
• Authors: Joanna M. Hetman; Nicola Robas; Rhona Baxendale; Mark Fidock; Stephen C. Phillips; Scott H. Soderling; Joseph A. Beavo
• Keywords: splice; Zaprinast; Molecular mass; Cloning (programming)

Phosphodiesterase 11A (PDE11A) is a recently identified family of cAMP and cGMP hydrolyzing enzymes. Thus far, single splice variant designated as PDE11A1 has been reported. In this study, we identify characterize two additional variants PDE11A, PDE11A2 PDE11A3. The full-length cDNAs are 2,141 bp for 2205 ORF predicts protein 576 aa with molecular mass 65.8 kDa. PDE11A3 684 78.1 Comparison the sequence that indicates an 86 at N terminus PDE11A2. Part extends potential binding region (GAF domain) present in PDE11A1. Compared PDE11A2, 108 N-terminal amino acids. Sequence analysis presence another GAF domain region. This diversification regulatory sequences PDE11A suggests interesting possibility differential regulation these Recombinant -A3 proteins expressed Baculovirus expression system have ability to hydrolyze both cGMP. K(m) values hydrolysis 3.3 microM 5.7 PDE11A3, respectively. 3.7 4.2 Both PDEs showed V(max) ratio cAMP/cGMP approximately 1.0. sensitive dipyridamole, IC(50) 1.8 microM, zaprinast, 28 microM. demonstrated similar pattern inhibitor sensitivity 0.82 5 dipyridamole