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Adenosine Deaminase Interacts with A 1 Adenosine Receptors in Pig Brain Cortical Membranes
Author(s) -
Saura Carles,
Ciruela Francisco,
Casadó Vicent,
Canela Enric I.,
Mallol Josefa,
Lluis Carmen,
Franco Rafael
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.66041675.x
Subject(s) - adenosine deaminase , adenosine , adenosine a2b receptor , amp deaminase , biochemistry , adenosine a1 receptor , purinergic signalling , adenosine receptor , adenosine a3 receptor , biology , receptor , adenosine deaminase inhibitor , chemistry , agonist
Adenosine deaminase is an enzyme of purine metabolism that has largely been considered to be cytosolic. A few years ago, adenosine deaminase was reported to appear on the surface of cells. Recently, it has been demonstrated that adenosine deaminase interacts with a type II membrane protein known as either CD26 or dipeptidylpeptidase IV. In this study, by immunoprecipitation and affinity chromatography it is shown that adenosine deaminase and A 1 adenosine receptors interact in pig brain cortical membranes. This is the first report in brain demonstrating an interaction between a degradative ectoenzyme and the receptor whose ligand is the enzyme substrate. By means of this interaction adenosine deaminase leads to the appearance of the high‐affinity site of the receptor, which corresponds to the receptor‐G protein complex. Thus, it seems that adenosine deaminase is necessary for coupling A 1 adenosine receptors to heterotrimeric G proteins.