Abstract
The antagonist radioligand 1,3-[3H]dipropyl-8-cyclopentylxanthine ([3H]DPCPX) was used to characterize adenosine A1 receptors in membrane preparations from atrial and ventricular myocardium of rat, rabbit, guinea pig and pig. Kd values in crude membranes from guinea pig atria and ventricles (3.3 and 3.0 nM) were higher than those in the other species (ranges, 1.5-1.8 and 1.5-1.9 nM). Bmax values were greater in atria than in ventricles in all four species, and in atria and ventricles of guinea pig (76 and 34 fmol/mg), than in the other species (ranges, 15-17 and undetectable to 12 fmol/mg). In contrast, guinea pig Kd and Bmax values for β-adrenoceptors, which were labelled with (-)3-[125I]iodocyanopindolol, fell within the range of values for the other three mammalian species. In semipurified membrane preparations from pig, [3H]DPCPX and the agonist radioligand [125I]-N6-4-aminobenzyladenosine appeared to label a similar population of receptors and gave comparable Kd values in atria (0.73 and 0.66 nM) and in ventricles (0.57 and 0.70 nM). In semipurified preparations from pig, the agonist R-(-)-N6-2(-phenylisopropyl)adenosine (R-PIA) displaced [3H]DPCPX in a manner consistent with the presence of both high- and low-affinity adenosine A1 receptors. The data from this study indicate that the density of adenosine A1 receptors in atria is greater than in ventricles, but similar Kd values suggest that the A1 receptor population is the same in the two cardiac tissues. Also, the data demonstrate that the [3H]DPCPX antagonist binding characteristics of guinea pig myocardium differ from those in rat, rabbit and pig.
| Original language | English |
|---|---|
| Pages (from-to) | 105-111 |
| Number of pages | 7 |
| Journal | European Journal of Pharmacology: Molecular Pharmacology |
| Volume | 246 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jul 15 1993 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Pharmacology
Cite this
Species comparison of adenosine and β-adrenoceptors in mammalian atrial and ventricular myocardium. / Musser, Beth; Morgan, Michael E.; Leid, Mark; Murray, Thomas F.; Linden, Joel; Vestal, Robert E.
In: European Journal of Pharmacology: Molecular Pharmacology, Vol. 246, No. 2, 15.07.1993, p. 105-111.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Species comparison of adenosine and β-adrenoceptors in mammalian atrial and ventricular myocardium
AU - Musser, Beth
AU - Morgan, Michael E.
AU - Leid, Mark
AU - Murray, Thomas F.
AU - Linden, Joel
AU - Vestal, Robert E.
PY - 1993/7/15
Y1 - 1993/7/15
N2 - The antagonist radioligand 1,3-[3H]dipropyl-8-cyclopentylxanthine ([3H]DPCPX) was used to characterize adenosine A1 receptors in membrane preparations from atrial and ventricular myocardium of rat, rabbit, guinea pig and pig. Kd values in crude membranes from guinea pig atria and ventricles (3.3 and 3.0 nM) were higher than those in the other species (ranges, 1.5-1.8 and 1.5-1.9 nM). Bmax values were greater in atria than in ventricles in all four species, and in atria and ventricles of guinea pig (76 and 34 fmol/mg), than in the other species (ranges, 15-17 and undetectable to 12 fmol/mg). In contrast, guinea pig Kd and Bmax values for β-adrenoceptors, which were labelled with (-)3-[125I]iodocyanopindolol, fell within the range of values for the other three mammalian species. In semipurified membrane preparations from pig, [3H]DPCPX and the agonist radioligand [125I]-N6-4-aminobenzyladenosine appeared to label a similar population of receptors and gave comparable Kd values in atria (0.73 and 0.66 nM) and in ventricles (0.57 and 0.70 nM). In semipurified preparations from pig, the agonist R-(-)-N6-2(-phenylisopropyl)adenosine (R-PIA) displaced [3H]DPCPX in a manner consistent with the presence of both high- and low-affinity adenosine A1 receptors. The data from this study indicate that the density of adenosine A1 receptors in atria is greater than in ventricles, but similar Kd values suggest that the A1 receptor population is the same in the two cardiac tissues. Also, the data demonstrate that the [3H]DPCPX antagonist binding characteristics of guinea pig myocardium differ from those in rat, rabbit and pig.
AB - The antagonist radioligand 1,3-[3H]dipropyl-8-cyclopentylxanthine ([3H]DPCPX) was used to characterize adenosine A1 receptors in membrane preparations from atrial and ventricular myocardium of rat, rabbit, guinea pig and pig. Kd values in crude membranes from guinea pig atria and ventricles (3.3 and 3.0 nM) were higher than those in the other species (ranges, 1.5-1.8 and 1.5-1.9 nM). Bmax values were greater in atria than in ventricles in all four species, and in atria and ventricles of guinea pig (76 and 34 fmol/mg), than in the other species (ranges, 15-17 and undetectable to 12 fmol/mg). In contrast, guinea pig Kd and Bmax values for β-adrenoceptors, which were labelled with (-)3-[125I]iodocyanopindolol, fell within the range of values for the other three mammalian species. In semipurified membrane preparations from pig, [3H]DPCPX and the agonist radioligand [125I]-N6-4-aminobenzyladenosine appeared to label a similar population of receptors and gave comparable Kd values in atria (0.73 and 0.66 nM) and in ventricles (0.57 and 0.70 nM). In semipurified preparations from pig, the agonist R-(-)-N6-2(-phenylisopropyl)adenosine (R-PIA) displaced [3H]DPCPX in a manner consistent with the presence of both high- and low-affinity adenosine A1 receptors. The data from this study indicate that the density of adenosine A1 receptors in atria is greater than in ventricles, but similar Kd values suggest that the A1 receptor population is the same in the two cardiac tissues. Also, the data demonstrate that the [3H]DPCPX antagonist binding characteristics of guinea pig myocardium differ from those in rat, rabbit and pig.
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UR - http://www.scopus.com/inward/citedby.url?scp=0027213989&partnerID=8YFLogxK
U2 - 10.1016/0922-4106(93)90086-O
DO - 10.1016/0922-4106(93)90086-O
M3 - Article
VL - 246
SP - 105
EP - 111
JO - European Journal of Pharmacology - Molecular Pharmacology Section
JF - European Journal of Pharmacology - Molecular Pharmacology Section
SN - 0922-4106
IS - 2
ER -