Abstract
125I-Hydroxyphenylisopropyl adenosine ( 125I-HPIA) was used to characterize adenosine receptors in human adipocyte plasma membranes. Steady state binding was achieved after 6 h at 37°. Scatchard plots were linear, with a K D of approx. 2.5 nM, and B max of 360–1800 fmol/mg protein. (−)N 6-phenylisopropyl adenosine (PIA) was a more potent inhibitor of binding than N-ethyl carboxamido adenosine, and (+)PIA was more than 10-fold less potent than (−)PIA, consistent with A 1 adenosine receptor binding. Theophylline was a potent inhibitor of binding (IC 50 approx. 10 μM). Photoaffinity cross-linking studies demonstrated that the receptor is a single subunit, M r approx. 43 kDa. The findings demonstrate that the human adipocyte adenosine receptor is similar to the A 1 adenosine receptor of rat adipocytes, although its molecular weight is higher, and its affinity for HPIA is lower than that of the rat.
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