Biomaterial Database

Receptors linked to inhibition of adenylate cyclase: additional signaling mechanisms. 1988

L E Limbird

Department of Pharmacology, Vanderbilt University, Nashville, Tennessee 37232.

Many hormones and neurotransmitters attenuate cyclic AMP (cAMP) accumulation in intact cells by virtue of their ability to inhibit adenylate cyclase activity via the GTP-binding protein denoted as Gi. Nonetheless, a number of physiological findings suggest that attenuation of cAMP production is not sufficient to serve as the only signal for eliciting the diverse physiological effects provoked by these various receptor populations. Additional biochemical and electrophysiological changes are known to occur after occupancy of receptors linked to inhibition of adenylate cyclase, including acceleration of Na+/H+ exchange, activation of K+ conductances, and inhibition of voltage-sensitive Ca2+ channels. This review summarizes the current understanding of how these receptors are coupled to their multiple potential effector mechanisms and offers some speculation about the possible interplay between the biochemical and electrophysiological sequels of receptor occupancy. It is hoped that future studies will establish which constellation of possible signaling mechanisms actually brings about changes in metabolic, secretory, or contractile events in different target cells.

UI	MeSH Term	Description	Entries
D011956	Receptors, Cell Surface	Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.	Cell Surface Receptor,Cell Surface Receptors,Hormone Receptors, Cell Surface,Receptors, Endogenous Substances,Cell Surface Hormone Receptors,Endogenous Substances Receptors,Receptor, Cell Surface,Surface Receptor, Cell
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D000067956	Adenylyl Cyclase Inhibitors	Compounds that bind to and inhibit the action of ADENYLYL CYCLASES.	Adenylate Cyclase Inhibitors,Cyclase Inhibitors, Adenylate,Cyclase Inhibitors, Adenylyl,Inhibitors, Adenylate Cyclase,Inhibitors, Adenylyl Cyclase
D000242	Cyclic AMP	An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.	Adenosine Cyclic 3',5'-Monophosphate,Adenosine Cyclic 3,5 Monophosphate,Adenosine Cyclic Monophosphate,Adenosine Cyclic-3',5'-Monophosphate,Cyclic AMP, (R)-Isomer,Cyclic AMP, Disodium Salt,Cyclic AMP, Monoammonium Salt,Cyclic AMP, Monopotassium Salt,Cyclic AMP, Monosodium Salt,Cyclic AMP, Sodium Salt,3',5'-Monophosphate, Adenosine Cyclic,AMP, Cyclic,Adenosine Cyclic 3',5' Monophosphate,Cyclic 3',5'-Monophosphate, Adenosine,Cyclic Monophosphate, Adenosine,Cyclic-3',5'-Monophosphate, Adenosine,Monophosphate, Adenosine Cyclic
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D017923	Sodium-Hydrogen Exchangers	A family of plasma membrane exchange glycoprotein antiporters that transport sodium ions and protons across lipid bilayers. They have critical functions in intracellular pH regulation, cell volume regulation, and cellular response to many different hormones and mitogens.	Na(+)-H(+)-Antiporter,Na(+)-H(+)-Exchanger,Sodium-Hydrogen Antiporter,Na(+)-H(+)-Antiporters,Na(+)-H(+)-Exchangers,SLC9 Na(+)-H(+) Exchangers,SLC9 Protein Family,SLC9 Proteins,SLC9-NHE Protein Family,Sodium-Hydrogen Antiporters,Sodium-Hydrogen Exchanger,Sodium-Proton Antiporter,Sodium-Proton Antiporters,Solute Carrier 9 Protein Family,Solute Carrier 9 Proteins,Antiporter, Sodium-Hydrogen,Antiporter, Sodium-Proton,Antiporters, Sodium-Hydrogen,Antiporters, Sodium-Proton,Exchanger, Sodium-Hydrogen,Exchangers, Sodium-Hydrogen,Protein Family, SLC9,Protein Family, SLC9-NHE,SLC9 NHE Protein Family,Sodium Hydrogen Antiporter,Sodium Hydrogen Antiporters,Sodium Hydrogen Exchanger,Sodium Hydrogen Exchangers,Sodium Proton Antiporter,Sodium Proton Antiporters