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Multisite phosphorylation of adipocyte and hepatocyte phosphodiesterase 3B.

Author:
  • Rebecka Lindh
  • Faiyaz Ahmad
  • Svante Resjö
  • Peter James
  • Jeong S Yang
  • Henry M Fales
  • Vincent Manganiello
  • Eva Degerman
Publishing year: 2007
Language: English
Pages: 584-592
Publication/Series: Biochimica et Biophysica Acta: Molecular Cell Research
Volume: 1773
Issue: 4
Document type: Journal article
Publisher: Elsevier

Abstract english

Phosphodiesterase 3B (PDE3B) is an important component of insulin and cAMP-dependent signalling pathways. In order to study phosphorylation of PDE3B, we have used an adenoviral system to express recombinant flag-tagged PDE3B in primary rat adipocytes and H4IIE hepatoma cells. Phosphorylation of PDE3B after treatment of cells with insulin, cAMP-increasing agents, or the phosphatase inhibitor, calyculin A was analyzed by two-dimensional tryptic phosphopeptide mapping and mass spectrometry. We found that PDE3B is multisite phosphorylated in adipocytes and H4IIE hepatoma cells in response to all these stimuli. Several sites were identified; serine (S)273, S296, S421, S424/5, S474 and S536 were phosphorylated in adipocyte as well as H4IIE hepatoma cells whereas S277 and S507 were phosphorylated in hepatoma cells only. Several of the sites were phosphorylated by insulin as well as cAMP-increasing hormones indicating integration of the two signalling pathways upstream of PDE3B, maybe at the level of protein kinase B.

Keywords

  • Endocrinology and Diabetes
  • Phosphorylation
  • PDE3B
  • Adipocyte
  • Insulin
  • Hepatocyte
  • cAMP

Other

Published
  • Insulin Signal Transduction
  • ISSN: 0167-4889
Peter James
E-mail: peter [dot] james [at] immun [dot] lth [dot] se

Professor

Department of Immunotechnology

+46 46 222 14 96

+46 70 247 79 60

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