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Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5)



Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5)



Biochemical and Biophysical Research Communications 247(2): 249-254



A human PDE5 cDNA has been isolated which contains an open reading frame encoding an 875 amino acid, 100,012 Da polypeptide, the expression of which yields a protein of the predicted size and is capable of hydrolyzing cGMP. The deduced amino acid sequence is very similar (95%) to that of bovine PDE5, and comprises a conserved cGMP-binding domain and catalytic domain. Northern analysis reveals a major and minor transcript of approximately 9 kb and approximately 8 kb respectively, thus indicating the existence of at least two splice variants, the major form being readily detected in bladder, colon, lung, pancreas, placenta, prostate, small intestine, and stomach.

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Accession: 009042191

Download citation: RISBibTeXText

PMID: 9642111

DOI: 10.1006/bbrc.1998.8769



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