GABA(sub B) receptors make it to the top - as dimers

Article Abstract:

The functions of the GABA(sub B) receptor as a heterodimer was discussed during the 4th International GABA(sub B) Symposium held in Nov 1998 in Los Angeles, CA. It was reported that these heterodimers are formed from GABA(sub B)R1 and R2 subunits. The interaction between these two receptor proteins represented a novel principle of receptor assembly and signal transduction. It was recommended that further experiments be conducted to determine other functions of the R1 subunit. The regional and cellular relevance of GABA(sub B) receptors in identifying new drugs was recognized.

Conferences, meetings and seminars, Los Angeles, California, Proteins, Neurotransmitters

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Redox state, NMDA receptors and NO-related species

Article Abstract:

Redox modulation of protein receptor sites has been shown to affect ligand-binding. In NMDA receptor activity as well as in other transmitter-gated receptors such as GABA and glycine receptors, author Lipton et al. state that ligand binding is affected by the redox state of the receptor. This form of redox controlled signal regulation is not disputed by Gozlan and Yehezkel, but adds that the flexibility of receptor activity is based on the state of oxidation of the receptor, such that when it is fully oxidized, no regulatory activity can be effected.

Ligand binding (Biochemistry)

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Responses to NMDA receptor antagonists altered by epileptogenesis

Article Abstract:

The presence of epileptogenesis in both human and animal subjects greatly reduced the anticonvulsant effects of N-methyl-D-aspartate (NMDA) antagonists. The brain responded differently to NMDA during epileptic seizures resulting in less susceptibility to NMDA antagonist effect. Various tests using different competitive and noncompetitive NMDA antagonists confirmed the alteration caused by epileptogenesis.

Epilepsy

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