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Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase

Meacci, E; Taira, M; Moos, M Jr; Smith, C J; Movsesian, M A; Degerman, Eva LU ; Belfrage, P and Manganiello, V (1992) In Proceedings of the National Academy of Sciences 89(9). p.3721-3725
Abstract
We have cloned a cDNA for a myocardial cGMP-inhibited cAMP phosphodiesterase (cGI PDE) from a human heart cDNA library in lambda Zap II. The open reading frame [3.5 kilobases (kb)] of cDNA clone n.13.2 (7.7 kb) encodes a protein of 125 kDa. In Northern blots of total human ventricle RNA, a single mRNA species (8.3 kb) hybridized with a 4-kb EcoRI restriction fragment of clone n.13.2 cDNA (containing the entire open reading frame). The carboxyl-terminal region of the deduced amino acid sequence of the cGI PDE contains the putative catalytic domain conserved among mammalian PDE families. A partial cDNA clone, n.2, encoding a truncated, 54-kDa cGI PDE containing the conserved domain was expressed as a catalytically active fusion protein in... (More)
We have cloned a cDNA for a myocardial cGMP-inhibited cAMP phosphodiesterase (cGI PDE) from a human heart cDNA library in lambda Zap II. The open reading frame [3.5 kilobases (kb)] of cDNA clone n.13.2 (7.7 kb) encodes a protein of 125 kDa. In Northern blots of total human ventricle RNA, a single mRNA species (8.3 kb) hybridized with a 4-kb EcoRI restriction fragment of clone n.13.2 cDNA (containing the entire open reading frame). The carboxyl-terminal region of the deduced amino acid sequence of the cGI PDE contains the putative catalytic domain conserved among mammalian PDE families. A partial cDNA clone, n.2, encoding a truncated, 54-kDa cGI PDE containing the conserved domain was expressed as a catalytically active fusion protein in Escherichia coli. cAMP hydrolytic activity was inhibited by cGMP and OPC 3911 but not by rolipram. Thus, this report provides direct proof that the conserved domain contains the catalytic core of cGI PDEs. (Less)
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author
organization
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Contribution to journal
publication status
published
subject
in
Proceedings of the National Academy of Sciences
volume
89
issue
9
pages
3721 - 3725
publisher
National Acad Sciences
external identifiers
  • pmid:1315035
  • scopus:0026552359
ISSN
1091-6490
language
English
LU publication?
yes
id
4f84779e-ed45-485d-bd51-6db3df5761bd (old id 1106737)
date added to LUP
2008-08-08 13:39:03
date last changed
2017-07-02 03:35:37
@article{4f84779e-ed45-485d-bd51-6db3df5761bd,
  abstract     = {We have cloned a cDNA for a myocardial cGMP-inhibited cAMP phosphodiesterase (cGI PDE) from a human heart cDNA library in lambda Zap II. The open reading frame [3.5 kilobases (kb)] of cDNA clone n.13.2 (7.7 kb) encodes a protein of 125 kDa. In Northern blots of total human ventricle RNA, a single mRNA species (8.3 kb) hybridized with a 4-kb EcoRI restriction fragment of clone n.13.2 cDNA (containing the entire open reading frame). The carboxyl-terminal region of the deduced amino acid sequence of the cGI PDE contains the putative catalytic domain conserved among mammalian PDE families. A partial cDNA clone, n.2, encoding a truncated, 54-kDa cGI PDE containing the conserved domain was expressed as a catalytically active fusion protein in Escherichia coli. cAMP hydrolytic activity was inhibited by cGMP and OPC 3911 but not by rolipram. Thus, this report provides direct proof that the conserved domain contains the catalytic core of cGI PDEs.},
  author       = {Meacci, E and Taira, M and Moos, M Jr and Smith, C J and Movsesian, M A and Degerman, Eva and Belfrage, P and Manganiello, V},
  issn         = {1091-6490},
  language     = {eng},
  number       = {9},
  pages        = {3721--3725},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase},
  volume       = {89},
  year         = {1992},
}