title: Human cyclic nucleotide phosphodiesterases possess a much broader substrate-specificity than previously appreciated.
abstract: Phosphodiesterases (PDEs) capable of degrading cAMP and cGMP are indispensable for the regulation of cyclic nucleotide-mediated signals. The existence of other cyclic nucleotides such as cCMP and cUMP has been discussed controversially in the literature. Despite publications on PDEs hydrolyzing cCMP or cUMP, the molecular identity of such enzymes remained elusive. Recently, we have provided evidence for a role of cCMP as second messenger in vascular relaxation and inhibition of platelet aggregation. Using an HPLC-MS based assay, here, we show that human PDEs belonging to various families hydrolyze not only cAMP and cGMP but also other cyclic nucleotides.
authors.affiliation: Institute of Pharmacology, Medical School of Hannover, Hannover, Germany.
authors.forename: Daniel
authors.initials: D
authors.lastname: Reinecke
authors.forename: Heike
authors.initials: H
authors.lastname: Burhenne
authors.forename: Peter
authors.initials: P
authors.lastname: Sandner
authors.forename: Volkhard
authors.initials: V
authors.lastname: Kaever
authors.forename: Roland
authors.initials: R
authors.lastname: Seifert
mesh_terms: D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000737:chemistry* / Q000378:metabolism; D003597:Cytosine Nucleotides / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D013379:Substrate Specificity / Q000502:physiology
chemical_list: D003597:Cytosine Nucleotides; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases