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Identification of the site in the cGMP-inhibited phosphodiesterase phosphorylated in adipocytes in response to insulin and isoproterenol

  • Tova Rahn
  • Lars Rönnstrand
  • Marie-Josephe Leroy
  • Christer Wernstedt
  • Hans Tornqvist
  • Vincent C. Manganiello
  • Per Belfrage
  • Eva Degerman
Publishing year: 1996
Language: English
Pages: 11575-11580
Publication/Series: Journal of Biological Chemistry
Volume: 271
Issue: 19
Document type: Journal article
Publisher: ASBMB

Abstract english

Stimulation of rat adipocytes with insulin and isoproterenol results in serine phosphorylation and activation of the adipocyte cGMP-inhibited phosphodiesterase (cGI PDE), events believed to be important in the antilipolytic action of insulin (Degerman, E., Smith, C.J., Tornqvist, H., Vasta, V., Manganiello, V.C., and Belfrage, P. (1990) Proc. Natl. Acad. Sci. U.S.A. 87,533-537). Here we demonstrate, by two-dimensional phosphopeptide mapping, that the major phosphopeptide generated by trypsin, or trypsin followed by Asp-N protease digestion of [32P]cGI PDE phosphorylated in adipocytes in response to isoproterenol and/or insulin, in each case co-migrates with the phosphopeptide released by the same treatment of M297FRRPS(P)LPCISREQ310. This peptide was synthesized based on the deduced sequence of the cloned rat adipocyte cGI PDE and phosphorylated by cAMP-dependent protein kinase (protein kinase A). Radiosequencing of authentic and synthetic tryptic 32P-peptides showed that a single site in cGI PDE (Ser302) was phosphorylated in adipocytes incubated with isoproterenol and/or insulin. The more than additive phosphorylation and activation of cGI PDE in response to the two hormones found in this report and previously (Smith, C.J., Vasta, V., Degerman, E., Belfrage, P., and Manganiello, V.C. (1991) J. Biol. Chem. 266, 13385-13390) is proposed to reflect cross-talk between their respective signal transduction pathways at the level of the cGI PDE serine protein kinase or upstream regulatory component(s).


  • Endocrinology and Diabetes
  • Medicinal Chemistry


  • Insulin Signal Transduction
  • ISSN: 1083-351X
Eva Degerman
E-mail: eva [dot] degerman [at] med [dot] lu [dot] se


Insulin Signal Transduction

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