Histamine and GABA. Hydrogen bonds and permeation of vesicles.
Spectroscopic studies on sodium di(2-ethylhexyl)-sulfosuccinate (AOT) inverted micelles, films of AOT and L-alpha-lysolecithin and on dihexadecyl phosphate vesicles show that histamine and gamma-aminobutyric acid (GABA) act differently on these membrane models. Histamine increases the permeability of the membrane to ions through interactions with its polar sites. GABA, on the other hand, prefers self-association to association with the membrane. If these two neurotransmitters are applied jointly, the result is a decrease in the permeating effect of histamine. Possible mechanisms for these processes are discussed.
D004143:Dioctyl Sulfosuccinic Acid; D006632:Histamine; D006860:Hydrogen Bonding; D008244:Lysophosphatidylcholines; D008567:Membranes, Artificial; D008823:Micelles; D008954:Models, Biological; D010755:Organophosphates; D010539:Permeability; D013501:Surface-Active Agents; D005680:gamma-Aminobutyric Acid
D008244:Lysophosphatidylcholines; D008567:Membranes, Artificial; D008823:Micelles; D010755:Organophosphates; D013501:Surface-Active Agents; D004143:Dioctyl Sulfosuccinic Acid; C002290:dicetylphosphate; D005680:gamma-Aminobutyric Acid; D006632:Histamine