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Cloning and Characterization of Novel PDE4D Isoforms PDE4D6 and PDE4D7

Cloning and Characterization of Novel PDE4D Isoforms PDE4D6 and PDE4D7

Daguang Wang, Chengjun Deng, Bozena Bugaj-Gaweda, May Kwan, Caryn Gunwaldsen, Chris Leonard, Xiaonan Xin, Yinghe Hu, Axel Unterbeck, Michael De Vivo

Cell Signal. 2003 Sep;15(9):883-91.

PMID: 12834813

Abstract:

We report here the cloning and characterization of two novel PDE4D isoforms, PDE4D6 and PDE4D7. PDE4D6 is a supershort form and PDE4D7 a long form of PDE4D. In addition, we have identified another novel long-form variant, PDE4D8, in silico. Like other isoforms, PDE4D6 and PDE4D7 are differentially expressed. Expression of PDE4D6 is restricted to brain whereas PDE4D7 is widely expressed in many tissues. Baculovirus-expressed recombinant PDE4D6 and PDE4D7 enzymes have high affinity for cyclic AMP (cAMP) and are inhibited by rolipram. The activity of PDE4D7, not PDE4D6, is elevated by a protein kinase A (PKA)-dependent mechanism, presumably through phosphorylation of the conserved PKA site in the upstream conserved region 1 (UCR1) domain. In agreement with early reports, human PDE4D6 and PDE4D7 are localized on genomic fragments of chromosome 5. Examination of the promoter regions reveals multiple CREB binding sites upstream of the starting methionine (Met) of each gene, suggesting that the cAMP/PKA signaling pathway may regulate transcriptional expression of PDE4D6 and PDE4D7.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4245719	PDE4D7 active human			Price

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