Webbläsaren som du använder stöds inte av denna webbplats. Alla versioner av Internet Explorer stöds inte längre, av oss eller Microsoft (läs mer här: * https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Var god och använd en modern webbläsare för att ta del av denna webbplats, som t.ex. nyaste versioner av Edge, Chrome, Firefox eller Safari osv.

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

In English

Författare

  • 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.

Publiceringsår

1992

Språk

Engelska

Sidor

3721-3725

Publikation/Tidskrift/Serie

Proceedings of the National Academy of Sciences

Volym

89

Issue

9

Dokumenttyp

Artikel i tidskrift

Förlag

National Academy of Sciences

Ämne

  • Endocrinology and Diabetes

Status

Published

Forskningsgrupp

  • Insulin Signal Transduction

ISBN/ISSN/Övrigt

  • ISSN: 1091-6490