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Eva Degerman

Eva Degerman

Professor

Eva Degerman

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

Author

  • E Meacci
  • M Taira
  • M Jr Moos
  • C J Smith
  • M A Movsesian
  • Eva Degerman
  • P Belfrage
  • V Manganiello

Summary, in English

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.

Department/s

  • Insulin Signal Transduction

Publishing year

1992

Language

English

Pages

3721-3725

Publication/Series

Proceedings of the National Academy of Sciences

Volume

89

Issue

9

Document type

Journal article

Publisher

National Acad Sciences

Topic

  • Endocrinology and Diabetes

Status

Published

Research group

  • Insulin Signal Transduction

ISBN/ISSN/Other

  • ISSN: 1091-6490