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Properties of recombinant adenosine receptors
Author(s) -
Linden Joel,
Tucker Amy L.,
Robeva Anna S.,
Graber Stephen G.,
Munshi Ravi
Publication year - 1993
Publication title -
drug development research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.582
H-Index - 60
eISSN - 1098-2299
pISSN - 0272-4391
DOI - 10.1002/ddr.430280308
Subject(s) - receptor , recombinant dna , adenosine receptor , biology , biochemistry , adenosine , g protein coupled receptor , ligand (biochemistry) , g protein , amino acid , pertussis toxin , class c gpcr , microbiology and biotechnology , chemistry , metabotropic receptor , agonist , gene
Abstract Four subtypes of adenosine receptors have been cloned in several laboratories. The receptors all interact with G proteins and span the plasma membrane 7 times. They range in size from 319 to 412 amino acids. Conservation of structure among 10 different receptor clones for various species suggests that ligand recognition sites involve amino acids in the 2, 3, and 7 transmembrane segments of receptors. Species differences in ligand binding to A 1 receptors in tissues are very similar; for bovine receptors the affinity is R ‐PIA ≫ NECA, for canine receptors NECA ≥ R ‐PIA. Purified bovine A 1 receptors functionally couple to the pertussis toxin sensitive recombinant G proteins, G i1 , G i2 , G i3 , and G o . © 1993 Wiley‐Liss, Inc.