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J. Biol. Chem., Vol. 266, Issue 33, 22285-22289, Nov, 1991
R Munshi, IH Pang, PC Sternweis and J Linden
A1 adenosine receptors and associated guanine nucleotide-binding proteins
(G proteins) were purified from bovine cerebral cortex by affinity
chromatography (Munshi, R., and Linden, J. (1989) J. Biol. Chem. 264,
14853-14859). In this study we have identified the pertussis
toxin-sensitive G protein subunits that co-purify with A1 adenosine
receptors by immunoblotting with specific antipeptide antisera. Gi alpha 1,
Gi alpha 2, Go alpha, G beta 35, and G beta 36 were detected. Of the total
[35S]guanosine 5'-O-(3-thio)triphosphate [( 35S]GTP gamma S) binding sites,
Gi alpha 1 and Go alpha each accounted for greater than 37% whereas Gi
alpha 2 comprised less than 13%. G beta 35 was found in excess over G beta
36. Low molecular mass (21-25 kDa) GTP- binding proteins were not detected.
We also examined the characteristics of purified receptors and various
purified bovine brain G proteins reconstituted into phospholipid vesicles.
All three alpha- subunits restored GTP gamma S-sensitive high affinity
binding of the agonist 125I-aminobenzyladenosine to a fraction (25%) of
reconstituted receptors with a selectivity order of Gi2 greater than Go
greater than or equal to Gi1 (ED50 values of G proteins measured as fold
excess over the receptor concentration were 4.7 +/- 1.2, 24 +/- 5, and 34
+/- 7, respectively). Furthermore, receptors occupied with the agonist R-
phenylisopropyladenosine catalytically increased the rate of binding of
[35S]GTP gamma S to reconstituted G proteins by 6.5-8.5-fold. These results
suggest that A1 adenosine receptors couple indiscriminately to pertussis
toxin-sensitive G proteins.
A1 adenosine receptors of bovine brain couple to guanine nucleotide- binding proteins Gi1, Gi2, and Go
Department of Internal Medicine (Cardiology), University of Virginia, Charlottesville 22908.
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