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Phosphodiesterase 4 and 5 are Dominant cAMP‐ and cGMP‐hydrolyzing Isoforms in Rat Skeletal Muscle Arteries and Venules
Author(s) -
Wang Jianjie,
Kazmi Murtaza,
Huxley Virginia H.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.765.3
Subject(s) - phosphodiesterase 3 , phosphodiesterase , medicine , endocrinology , skeletal muscle , gene isoform , pde10a , rolipram , vascular smooth muscle , biology , chemistry , enzyme , biochemistry , smooth muscle , gene
Phosphodiesterases (PDEs) hydrolyze cAMP and cGMP, important second messengers controlling blood flow, vascular exchange, and remodeling. PDE inhibitors have been used clinically in many disease states including inflammation, asthma, septic shock, and ischemia. Our previous study showed the PDE expression profile in primary cultured microvascular endothelial cells (FASEB J. 2008 22:1145.4). To understand the basis of PDE in the regulation of vascular function in vivo, we first identified the distribution of PDE isoforms in intact arteries and venules of abdominal skeletal muscle from strain‐ and age‐ matched male and female rats. PDE mRNA was quantified via real‐time RT‐PCR assay. Five PDE isoforms (PDE1, PDE2, PDE3, PDE4, and PDE5) were expressed in all arteries and venules. The expression levels were: 1) cAMP‐hydrolyzing PDE, PDE33 months) males and females. The findings indicate PDE1‐5 are present in all vessels while PDE4 and PDE5 are dominant cAMP‐ and cGMP‐hydrolyzing PDE isoforms, respectively. (Supported by NIH RO1HL078816 and NASA NNJ05HF37G. *The first 2 authors contributed equally to this work).