Molecular mechanism of general anesthesia: I. Fluorescence studies in mitochondrial membranes.
We have tested the working hypothesis that anesthetics, by labilizing lipid-protein interactions, induce conformational changes in membrane proteins involved in the transmission of neural impulses. In the first communication of this series we report that general anesthetics induce changes in the fluorescence of the probes ANS and NPN in model membranes, lipid vesicles and mitochondria. The changes observed concern the quantumyield but not the position of the emission maximum. Such changes may be interpreted as due to fluidization of the membrane core (NPN), accompanied by variable effects in the membrane surface(ANS).
D000768:Anesthesia, General; D000777:Anesthetics / Q000494:pharmacology*; D000818:Animals; D001921:Brain / Q000187:drug effects; D000440:Butanols / Q000494:pharmacology; D005456:Fluorescent Dyes; D006221:Halothane / Q000494:pharmacology; D066298:In Vitro Techniques; D007649:Ketamine / Q000494:pharmacology; D008560:Membrane Fluidity / Q000187:drug effects; D008563:Membrane Lipids; D008565:Membrane Proteins / Q000032:analysis; D008733:Methoxyflurane / Q000494:pharmacology; D008928:Mitochondria / Q000187:drug effects*; D011487:Protein Conformation / Q000187:drug effects; D013552:Swine
D000777:Anesthetics; D000440:Butanols; D005456:Fluorescent Dyes; D008563:Membrane Lipids; D008565:Membrane Proteins; D008733:Methoxyflurane; D007649:Ketamine; D006221:Halothane