Alpha 1-adrenoceptor activation increases ecto-5'-nucleotidase activity and adenosine release in rat cardiomyocytes by activating protein kinase C

Circulation. 1995 Apr 15;91(8):2226-34. doi: 10.1161/01.cir.91.8.2226.

Abstract

Background: Adenosine is an important regulator of many cardiac functions and is synthesized primarily by ecto- and cytosolic 5'-nucleotidase. We have previously reported that alpha 1-adrenoceptor blockade attenuates adenosine release from ischemic myocardium, raising the possibility that alpha 1-adrenoceptor activation activates 5'-nucleotidase. This study tested whether activation of protein kinase C by alpha 1-adrenoceptor activation increases 5'-nucleotidase activity and augments adenosine release.

Methods and results: Cardiomyocytes were isolated from adult male Wistar rats and suspended in modified HEPES-Tyrode's buffer solution. After stabilization, the cardiomyocytes were incubated with and without an exposure to norepinephrine (10(-9) to 10(-5) mol/L) while being treated with propranolol and yohimbine or with and without an exposure to methoxamine (10(-9) to 10(-5) mol/L). Ecto-5'-nucleotidase activity was increased by norepinephrine and methoxamine during 30 minutes in a dose-dependent manner, whereas cytosolic 5'-nucleotidase was not activated. These increases in ecto-5'-nucleotidase activity were inhibited by GF109203X, an inhibitor of protein kinase C, and mimicked by phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C. The increase in ecto-5'-nucleotidase was not prevented by cycloheximide. When ecto-5'-nucleotidase activity increased, adenosine release was augmented in methoxamine- and PMA-treated cardiomyocytes (1299 +/- 252% and 1372 +/- 149%, respectively) compared with the untreated group (578 +/- 26%). The increase in adenosine release was blunted by GF109203X and alpha, beta-methyleneadenosine 5'-diphosphate, an inhibitor of ecto-5'-nucleotidase.

Conclusions: Thus, we conclude that alpha 1-adrenoceptor-mediated increases in ecto-5'-nucleotidase activity are attributed to activation of protein kinase C in rat cardiomyocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5'-Nucleotidase / antagonists & inhibitors
  • 5'-Nucleotidase / metabolism*
  • Adenosine / metabolism*
  • Adenosine Diphosphate / analogs & derivatives
  • Adenosine Diphosphate / pharmacology
  • Adenosine Monophosphate / metabolism
  • Animals
  • Cells, Cultured
  • Dose-Response Relationship, Drug
  • Enzyme Activation
  • In Vitro Techniques
  • Indoles / pharmacology
  • Male
  • Maleimides / pharmacology
  • Methoxamine / pharmacology
  • Myocardium / cytology
  • Myocardium / metabolism*
  • Norepinephrine / pharmacology
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism*
  • Rats
  • Rats, Wistar
  • Receptors, Adrenergic, alpha-1 / drug effects
  • Receptors, Adrenergic, alpha-1 / physiology*
  • Tetradecanoylphorbol Acetate / pharmacology

Substances

  • Indoles
  • Maleimides
  • Receptors, Adrenergic, alpha-1
  • alpha,beta-methyleneadenosine 5'-diphosphate
  • Adenosine Monophosphate
  • Adenosine Diphosphate
  • Protein Kinase C
  • 5'-Nucleotidase
  • Methoxamine
  • Adenosine
  • bisindolylmaleimide I
  • Tetradecanoylphorbol Acetate
  • Norepinephrine