Literature DB >> 2829866

Isoproterenol induces both cAMP- and calcium-dependent phosphorylation of phospholamban in canine heart in vivo.

P Karczewski1, S Bartel, H Haase, E G Krause.   

Abstract

The phosphorylation state of phospholamban in hearts of dogs depleted from catecholamines or treated with isoproterenol has been characterized using a sensitive back-phosphorylation method that allows to distinguish between cAMP-dependent and Ca2+/calmodulin-dependent phosphorylation occurring at the protein in situ. The data obtained demonstrate that in response to the beta-adrenergic agonist isoproterenol both the cAMP-dependent and the Ca2+/calmodulin-dependent phosphorylatable site are phosphorylated suggesting a physiological significance also for Ca2+-dependent phosphorylation of phospholamban in canine heart in vivo.

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Year:  1987        PMID： 2829866

Source DB:  PubMed          Journal:  Biomed Biochim Acta        ISSN： 0232-766X


  3 in total

1.  Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17.

Authors:  Piero Pollesello; Arto Annila
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

2.  Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer.

Authors:  P Pollesello; A Annila; M Ovaska
Journal:  Biophys J       Date:  1999-04       Impact factor: 4.033

3.  Beta 2-adrenoceptor activation by zinterol causes protein phosphorylation, contractile effects and relaxant effects through a cAMP pathway in human atrium.

Authors:  A J Kaumann; L Sanders; J A Lynham; S Bartel; M Kuschel; P Karczewski; E G Krause
Journal:  Mol Cell Biochem       Date:  1996 Oct-Nov       Impact factor: 3.396
  3 in total

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