Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase

Gene. 1997 May 20;191(1):89-95. doi: 10.1016/s0378-1119(97)00046-2.

Abstract

Human cyclic GMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase (PDE2A3) cDNAs were cloned from hippocampus and fetal brain cDNA libraries. A 4.2-kb composite DNA sequence constructed from overlapping cDNA clones encodes a 941 amino acid protein with a predicted molecular mass of 105,715 Da. Extracts prepared from yeast expressing the human PDE2A3 hydrolyzed both cyclic AMP (cAMP) and cyclic GMP (cGMP). This activity was inhibited by EHNA, a selective PDE2 inhibitor, and was stimulated three-fold by cGMP. Human PDE2A is expressed in brain and to a lesser extent in heart, placenta, lung, skeletal muscle, kidney and pancreas. The human PDE2A3 differs from the bovine PDE2A1 and rat PDE2A2 proteins at the amino terminus but its amino-terminal sequence is identical to the bovine PDE2A3 sequence. The different amino termini probably arise from alternative exon splicing of the PDE2A mRNA.

MeSH terms

  • 3',5'-Cyclic-GMP Phosphodiesterases / genetics*
  • 3',5'-Cyclic-GMP Phosphodiesterases / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Cyclic GMP / metabolism*
  • DNA, Complementary
  • Enzyme Activation
  • Humans
  • Molecular Sequence Data
  • RNA, Messenger / metabolism
  • Rats
  • Sequence Homology, Amino Acid

Substances

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

Associated data

  • GENBANK/U67733