PDE11A antibody

Background of PDE11A antibody

Cyclic nucleotides are important intracellular second messengers which play important role variety of signal transduction process. The cyclic nucleotides are hydrolyzed and compartmentalized by a family of enzymes called phosphodieterases. Recently a new and distinct member (PDE11) of cyclic nucleotide family has been identified and cloned (1). The PDE11A exhibit 50% amino acid homology with the catalytic domain of the all other PDEs. The PDE11A resembles most to the PDE5 family members but has distinct biochemical properties than PDE5. One of the many phosphodiesterases that compartmentalized and hydrolyze cAMP and cGMP in to AMP and GMP respectively are phosphodiesterase type 11. The human PDE11A contains an open reading frame encoding a 490 amino acid protein (55-56 kDa). The PDE11A has an N-terminus GAF domain homologous to other signaling molecule as found in PDE2, PDE5, PDE6, PDE10 this potentially represent an allosteric cGMP and other small signaling molecules. cyclic nucleotide phosphodiesterase (PDE)11A, which exhibits properties of a dual-substrate PDE, and its splice variants (RNPDE11A2, RNPDE11A3, and RNPDE11A4). The deduced amino-acid sequence of the longest form of rat PDE11A splice variant, A4, was 94% identical with that of the human variant (A4). The Km for for cAMP and cGMP were similar for all PDE11 variants (1.3-1.6 and 2.1-3.9 microM, PDE11A2, A3 and A4, respectively), the Vmax values differed significantly or rat PDE11A (A4>>A2>>A3). Human PDE11A variants also displayed very similar Km values and significantly different Vmax values (A4>>A2>>A3). The Vmax values of HSPDE11A4 for cAMP and cGMP were at least 100 times higher than those of HSPDE11A1. These observations indicate unique characteristics of PDE11A splicing variants (2).
Rat PDE11A splice variants were expressed in a tissue-specific manner. RNPDE11A4 showed unique tissue distribution distinct from HSPDE11A4, which is specifically expressed in the prostate. The PDE11A is sensitive to non-selective PDE inhibitor IBMX as well as zaprinast and dipyrimadole, inhibitors that are generally selective for cGMP-specific enzymes. PDE11A expression is diverse and is found in high levels in skeletal muscle, prostate, kidney, liver, pituitary and testis. At least three variants that may occur in vivo based on the three transcripts identified in various tissues ranging in size from 10.5 kb, 8.5 and 6.0 kb. PDE11A4 is composed of 934 amino acids including two complete GAF domains and shared 630 C-terminal amino acids with PDE11A3 but had a distinct N terminus containing the putative phosphorylation sites for cAMP- and cGMP-dependent protein kinases (3).