Multiple GABA(sub B) receptors

Article Abstract:

GABA(subB) receptors, distinct from classical GABA receptors were discovered by Bowery and co-workers in 1980. The GABA(subB) receptors were found to be insensitive to bicuculline and to other drugs while being sensitive to L-baclofen in contrast to the classical GABA receptors. However, various studies have shown that there may be multiple GABA(subB) receptors. Electrophysiological studies showed that L-phaclofen interacts with two subtypes of the bicuculline-insensitive receptor. Biochemical studies also suggested GABA(subB) receptor heterogeneity. Neurotransmitter release studies and binding and molecular biology research also supported the theory.

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GABA(sub A) receptor phosphorylation: multiple sites, actions and artifacts

Article Abstract:

Protein phosphorylation initiated by the addition of kinases to neurotransmitter sites resulted in the regulation of GABA(sub A) receptors. The protein kinases which included the types A and C and an undetermined kinase compound controlled desentization processes and neural transfer between GABA(sub A) and adenylate cyclase receptors. The study revealed that kinase-mediated phosphorylation could either enhance or inhibit receptor activity indicating the complexity of GABA(sub A) regulation via phosphorylation reactions.

Protein kinases, Phosphorylation

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Function and pharmacology of multiple GABA(sub A) receptor subunits

Article Abstract:

The alpha, beta, gamma and delta subunits of GABA(sub A) receptors exhibit pharmacological diversity. Each subunit contains multiple variants with different responses to receptor ligands. Variants of the alpha subunit resemble the reactivity of the two benzodiazepine binding sites. Moreover, interactions involving GABA(sub A) receptor variants cannot be restricted to individual subunits because some pharmacological responses are due to the activation of several variants.

Benzodiazepines

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