Halothane interaction with guanine nucleotide binding proteins in mouse heart

• Published in: Anesthesiology (Philadelphia) Vol. 69; no. 6; pp. 876 - 880
• Main Authors: VULLIEMOZ, Y, VEROSKY, M
• Format: Journal Article
• Language: English
• Published: Hagerstown, MD Lippincott 01.12.1988
• Subjects: Adenylate Cyclase Toxin; Anesthetics. Neuromuscular blocking agents; Animals; Biological and medical sciences; Cyclic AMP - metabolism; Cyclic GMP - metabolism; Halothane - metabolism; Halothane - pharmacology; Male; Medical sciences; Mice; Myocardium - metabolism; Neuropharmacology; Pertussis Toxin; Pharmacology. Drug treatments; Virulence Factors, Bordetella - pharmacology; Cyclic AMP; Interaction
• ISSN: 0003-3022; 1528-1175
• DOI: 10.1097/00000542-198812000-00012

Volatile anesthetics have been shown to decrease hormone-induced adenosine cyclic monophosphate (cAMP) formation and to increase guanosine cyclic monophosphate (cGMP) content in mouse ventricular myocardium. Hormone-induced inhibition of adenylate cyclase, the enzyme that synthesizes cAMP, and the cGMP response to alpha adrenergic agonists are mediated by a guanine nucleotide binding protein (N) sensitive to pertussis toxin. To evaluate the involvement of N proteins in the action of halothane on cyclic nucleotides in the heart, mice were pretreated with pertussis toxin, 50 micrograms/kg, ip, 72 h prior to exposure to halothane, 1.2 vol%. Pretreatment with the toxin decreased the cGMP response to halothane by 65% but was without effect on the decrease in myocardial cAMP induced by the anesthetic. The results indicate that a functionally active pertussis toxin-sensitive N protein is involved in the cGMP response to halothane, but not in the cAMP response.