Kotera J, Fujishige K, Yuasa K, Omori K
Discovery Research Laboratory, Tanabe Seiyaku Co. Ltd., 2-50, Kawagishi-2-chome, Toda, Saitama, 335-8505, Japan.
Biochem Biophys Res Commun. 1999 Aug 11;261(3):551-7. doi: 10.1006/bbrc.1999.1013.
We have isolated a novel alternative splice variant of human cAMP- and cGMP-hydrolyzing phosphodiesterase (PDE10A2) from human fetal lung. The N-terminal sequence of human PDE10A2 differed from that of human PDE10A1 reported previously. PDE10A1 and PDE10A2 expressed in COS-7 cells have cGMP K(m) values of 14 and 13 microM, low cAMP K(m) values of 0.28 and 0.22 microM, and high cAMP K(m) values of 0.96 and 1.1 microM, respectively, at high concentrations of cGMP and cAMP. PCR analysis demonstrated that both PDE10A1 and PDE10A2 transcripts are present in various human tissues and that PDE10A2 transcripts are a major form in some human tissues. The unique N-terminus of PDE10A2 has a putative phosphorylation site by cAMP-dependent protein kinase (cAK), but PDE10A1 does not. The recombinant PDE10A2 protein is preferentially phosphorylated by cAK, although the recombinant PDE10A1 protein is not phosphorylated by cAK.
我们从人胎儿肺中分离出一种新型的人环磷酸腺苷（cAMP）和环磷酸鸟苷（cGMP）水解磷酸二酯酶（PDE10A2）可变剪接变体。人PDE10A2的N端序列与先前报道的人PDE10A1不同。在COS-7细胞中表达的PDE10A1和PDE10A2，在高浓度cGMP和cAMP时，其cGMP的米氏常数（K(m)）值分别为14和13微摩尔，低cAMP的K(m)值分别为0.28和0.22微摩尔，高cAMP的K(m)值分别为0.96和1.1微摩尔。聚合酶链反应（PCR）分析表明，PDE10A1和PDE10A2转录本均存在于各种人体组织中，且PDE10A2转录本在某些人体组织中是主要形式。PDE10A2独特的N端有一个环磷酸腺苷依赖性蛋白激酶（cAK）的假定磷酸化位点，而PDE10A1没有。重组PDE10A2蛋白优先被cAK磷酸化，而重组PDE10A1蛋白不被cAK磷酸化。
