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

被引：78

作者：

Stacey, P ^{[1
]}

Rulten, S ^{[1
]}

Dapling, A ^{[1
]}

Phillips, SC ^{[1
]}

机构：

[1] Pfizer Ltd, Cent Res, Dept Mol Pharmacol, Sandwich CT13 9NJ, Kent, England

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 247卷 / 02期

关键词：

D O I：

10.1006/bbrc.1998.8769

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 similar to 9 kb and similar to 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. (C) 1998 Academic Press.

引用

页码：249 / 254

页数：6

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