© 1996 American Heart Association, Inc.
Articles |
Adenosine A1 Stimulation Activates 
-Protein Kinase C in Rat Ventricular Myocytes
From the Laboratoire de Physiopathologie et de Pharmacologie Cellulaires et Moléculaires, Hôpital G & R Laënnec, Nantes, France; the Département de Cardiologie, Hôpital Broussais, Paris, France; and INSERM U-390, Hôpital Arnaud de Villeneuve, Montpellier, France.
Correspondence to Dr Denis Escande, Laboratoire de Physiopathologie et de Pharmacologie Cellulaires et Moléculaires, Hôpital G & R Laënnec, BP 1005, 44035 Nantes, France.
Abstract By making use of immunoblotting and
immunocytochemical analysis, we explored whether stimulation of
adenosine A1 receptors would promote the activation
of 
-protein kinase C (-PKC) immunolabeled with a polyclonal
antibody. Immunoblot analysis of Triton
X-100–soluble cell membrane and cytosolic fractions revealed the
presence of a specific 75-kD band reactive to the -PKC polyclonal
antibody. In freshly isolated rat cardiac myocytes, 28% of the total
immunoreactive -PKC was associated with the membrane fraction,
whereas 72% was associated with the soluble fraction. Under
stimulation with the tumor-promoting phorbol 12-myristate
13-acetate (PMA, 500 nmol/L) used as a positive control, -PKC
translocated to the cell membrane, with the membrane fraction
representing 88% and the cytosolic fraction
representing 12% of the total immunoreactive -PKC.
Transverse optical sections performed with confocal laser microscopy
showed that immunostaining with anti–-PKC antibody
was distributed in the cytosol of unstimulated cells but accumulated in
the cell membrane under PMA stimulation. In the membrane fraction of
cells pretreated with adenosine (100 µmol/L) or with the
adenosine A1 agonist
(-)-N6-(2-phenylisopropyl)-adenosine
(R-PIA, 1 µmol/L), the 75-kD band corresponding to -PKC increased
by 57% and 66%, respectively, when compared with nonstimulated cells
processed under the same experimental conditions. In cells exposed to
either of the purine agonists, specific fluorescence staining
decorated the cell membrane, a pattern that was not observed in control
cells. Activation of membrane -PKC produced either by
adenosine itself or by its analogue R-PIA was fully antagonized
by the specific A1 antagonist
8-cyclopentyl-1,3-dipropylxanthine (1 µmol/L). From these data,
we conclude that adenosine A1 stimulation
activates -PKC in freshly isolated rat
ventricular myocytes.
Key Words: adenosine • protein kinase C • phorbol ester • preconditioning • rat ventricular myocytes
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