Cilostazol, a cyclic AMP phosphodiesterase inhibitor, stimulates nitric oxide production and sodium potassium adenosine triphosphatase activity in SH-SY5Y human neuroblastoma cells

Life Sciences ◽  
1999 ◽  
Vol 65 (13) ◽  
pp. 1413-1422 ◽  
Author(s):  
Hidetoshi Inada ◽  
Hideo Shindo ◽  
Masato Tawata ◽  
Toshimasa Onaya
Keyword(s):  
Nitric Oxide ◽  
Cyclic Amp ◽  
Adenosine Triphosphatase ◽  
Neuroblastoma Cells ◽  
Phosphodiesterase Inhibitor ◽  
Nitric Oxide Production ◽  
Human Neuroblastoma Cells ◽  
Human Neuroblastoma ◽  
Sodium Potassium ◽  
Adenosine Triphosphatase Activity

scholarly journals DREAM-αCREM Interaction via Leucine-Charged Domains Derepresses Downstream Regulatory Element-Dependent Transcription

2000 ◽  
Vol 20 (24) ◽  
pp. 9120-9126 ◽  
Author(s):  
Fran Ledo ◽  
Angel M. Carrión ◽  
Wolfgang A. Link ◽  
Britt Mellström ◽  
José R. Naranjo
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinase A ◽  
Regulatory Element ◽  
Neuroblastoma Cells ◽  
Human Neuroblastoma Cells ◽  
Binding Properties ◽  
Human Neuroblastoma ◽  
Protein Protein Interaction ◽  
Kinase A

ABSTRACT Protein kinase A-dependent derepression of the human prodynorphin gene is regulated by the differential occupancy of the Dyn downstream regulatory element (DRE) site. Here, we show that a direct protein-protein interaction between DREAM and the CREM repressor isoform, αCREM, prevents binding of DREAM to the DRE and suggests a mechanism for cyclic AMP-dependent derepression of the prodynorphin gene in human neuroblastoma cells. Phosphorylation in the kinase-inducible domain of αCREM is not required for the interaction, but phospho-αCREM shows higher affinity for DREAM. The interaction with αCREM is independent of the Ca2+-binding properties of DREAM and is governed by leucine-charged residue-rich domains located in both αCREM and DREAM. Thus, our results propose a new mechanism for DREAM-mediated derepression that can operate independently of changes in nuclear Ca2+.

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