Abstract
Genistein, a potent inhibitor for protein tyrosine kinase, remarkably inhibited the stimulatory action of N6-(L-2-phenylisopropyl)adenosine (PIA), an A1-adenosine receptor agonist, on thyrotropin (TSH)-induced phospholipase C activation in FRTL-5 thyroid cells. This drug also suppressed both the A1-receptor-mediated inhibition of cAMP accumulation in the cells and binding of [3H]8-cyclopentyl-1,3-dipropylxanthine, a specific antagonist for A1-receptor, to the cell membranes in a competitive manner. Adenosine-induced cAMP accumulation through A2-receptor in pertussis toxin-treated cells was also competitively antagonized by genistein. We conclude that genistein is also a competitive antagonist for P1-purinergic receptors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Deaminase / pharmacology
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Animals
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Cell Line
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Cell Membrane / metabolism
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Cyclic AMP / metabolism
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Dose-Response Relationship, Drug
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Enzyme Activation
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Genistein
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Inositol Phosphates / metabolism
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Isoflavones / pharmacology*
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Kinetics
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Phenylisopropyladenosine / pharmacology
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Protein-Tyrosine Kinases / antagonists & inhibitors*
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Purinergic P1 Receptor Agonists
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Purinergic P1 Receptor Antagonists*
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Rats
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Theophylline / analogs & derivatives
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Theophylline / metabolism
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Theophylline / pharmacology
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Thyroid Gland
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Thyrotropin / pharmacology*
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Type C Phospholipases / metabolism*
Substances
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Inositol Phosphates
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Isoflavones
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Purinergic P1 Receptor Agonists
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Purinergic P1 Receptor Antagonists
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Phenylisopropyladenosine
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8-cyclopentyl-1,3-dimethylxanthine
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Thyrotropin
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Theophylline
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Genistein
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Cyclic AMP
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Protein-Tyrosine Kinases
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Type C Phospholipases
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Adenosine Deaminase