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Vol. 286, Issue 2, 1051-1057, August 1998
Department of Pharmacology, School of Medicine, East Carolina
University, Greenville, North Carolina
Antipeptide antibody was raised in rabbit against the sequence
(361-390) of RDC-8, the presumed adenosine A2A receptor
cDNA from canine. The antibody titer was estimated by solid phase
radioimmunoassay. Western blot analysis under reducing conditions
identified a major 45 ± 1 kDa protein in bovine striatal
membranes. This immunoreactive band was competed in the presence of
excess peptide. Furthermore, the antibody recognized a single 45-kDa
immunoreactive band in membranes from cells transfected with the
recombinant human adenosine A2A receptors, whereas, fail to
cross-react with membranes from cells transfected with recombinant rat
A1 and human A3 receptors. Membranes from human
and porcine coronary artery, ventricle, atria and platelets (human
only) showed a major immunoreactive band at 45 ± 1 kDa size.
Under nonreducing conditions, the migration patterns of the
immunoreactive bands were not altered indicating the absence of
interchain disulfide bond. The 45-kDa immunoreactive band co-migrated
with
2-[4-(2-{2-[(4-aminophenyl)methylcarbonylamino]ethyl-aminocarbonyl}ethyl)phenyl]ethylamino-5'-Nethylcarboxamidoadenosine photoaffinity labeled A2A adenosine receptor using SANPAH
as the photoaffinity cross-linker. We provide immunological evidence for the presence of A2A adenosine receptor in human
cardiovascular tissues that exists as a 45-kDa monomeric protein. This
study also presents evidence for the presence of A2A
adenosine receptor in ventricle and atria in both human and porcine.
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