Chemical activators of OR4C3 can influence its activity through various pathways that lead to the increase of intracellular cyclic adenosine monophosphate (cAMP) levels. Forskolin, a well-known activator of adenylyl cyclase, directly contributes to the elevation of cAMP within the cell. Once adenylyl cyclase is activated by Forskolin, the enzyme converts ATP to cAMP, which then acts as a secondary messenger, potentially leading to the activation of OR4C3. Similarly, Isoproterenol, a synthetic catecholamine, binds to beta-adrenergic receptors, which signal via G proteins to activate adenylyl cyclase, resulting in increased levels of cAMP. This cascade of events can result in the activation of OR4C3, provided that OR4C3 is sensitive to changes in cAMP levels. IBMX, a non-selective phosphodiesterase inhibitor, prevents the breakdown of cAMP, which could help to maintain or enhance the activation state of OR4C3.
Epinephrine and Salbutamol, both adrenergic agonists, trigger similar pathways that lead to raised cAMP levels. Epinephrine engages with adrenergic receptors, while Salbutamol specifically targets beta2-adrenergic receptors, both resulting in cAMP-mediated OR4C3 activation. NECA, acting as an adenosine receptor agonist, and Adenosine itself, through its receptor-mediated actions, also elevate cAMP, thereby activating OR4C3. Rolipram, by selectively inhibiting phosphodiesterase 4, increases cAMP concentration, supporting the sustained activation of OR4C3. Histamine, through H2 receptors, Dopamine, via D1-like receptors, Terbutaline, as a beta2-adrenergic agonist, and PGE2, by engaging with EP receptors, all contribute to the elevation of cAMP levels. Each of these chemicals can facilitate the activation of OR4C3 by enhancing the cAMP signal within the cell, provided that OR4C3 is a cAMP-responsive protein.
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