Open AccessIdentification of rat cyclic nucleotide phosphodiesterase 11A (PDE11A)
Author(s) -
Yuasa Keizo,
Ohgaru Takanori,
Asahina Masatoshi,
Omori Kenji
Publication year - 2001
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2001.02366.x
Subject(s) - splice , phosphodiesterase , cyclic nucleotide phosphodiesterase , microbiology and biotechnology , chemistry , biology , enzyme , biochemistry , gene
We have isolated and characterized rat 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, RNPDE11A4, was 94% identical with that of the human variant (HSPDE11A4). 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. Rat PDE11A splice variants were expressed in COS‐7 cells, and their enzymatic characteristics were compared. Although the K m values for cAMP and cGMP were similar for all of them (1.3–1.6 and 2.1–3.9 µ m , respectively), the V max values differed significantly (RNPDE11A4 >> RNPDE11A2 > RNPDE11A3). Human PDE11A variants also displayed very similar K m values and significantly different V max values (HSPDE11A4 >> HSPDE11A2 > HSPDE11A3 >> HSPDE11A1). The V max 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.