Enhancement of benzodiazepine receptor binding by L-lysine is chloride-dependent and due to increase in binding affinity.
L-Lysine enhanced specific [3H]flunitrazepam binding dose dependently on extensively washed bovine brain membrane in vitro. This enhancement was stimulated by chloride ions dose dependently. Scatchard analysis indicated this enhancement by L-lysine to be due to increase in binding affinity (KD) with no change in receptor density (Bmax). Since enhancement of [3H]flunitrazepam binding by L-lysine was partially inhibited by picrotoxinin, L-lysine may act on a distinct picrotoxinin-sensitive site which was distinct from the gamma-aminobutyric acid receptor site. This binding site, however, appears to have some features resembling that of the central nervous system-depressant barbiturates.
Gao
X M
XM
Department of Biochemistry, University of Maryland Dental School, Baltimore 21201.
Chang
Y F
YF
D000818:Animals; D002417:Cattle; D002712:Chlorides / Q000502:physiology*; D005445:Flunitrazepam / Q000494:pharmacology; D066298:In Vitro Techniques; D007700:Kinetics; D008239:Lysine / Q000494:pharmacology*; D010433:Pentylenetetrazole / Q000494:pharmacology; D010852:Picrotoxin / Q000031:analogs & derivatives / Q000494:pharmacology; D011963:Receptors, GABA-A / Q000187:drug effects*; D054830:Sesterterpenes; D013570:Synaptic Membranes / Q000187:drug effects / Q000378:metabolism
D002712:Chlorides; D005445:Flunitrazepam; D008239:Lysine; D010433:Pentylenetetrazole; D010852:Picrotoxin; D011963:Receptors, GABA-A; D054830:Sesterterpenes; C022961:picrotoxinin