Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 62, Issue 2, Pages 119-127Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-004-4339-x
Keywords
protein kinase C; gamma-aminobutyric acid; neurosteroid; ethanol; phosphorylation; receptor for activated C kinase; phorbol ester
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Funding
- NATIONAL INSTITUTE ON ALCOHOL ABUSE AND ALCOHOLISM [R01AA013588, R01AA008117, R37AA013588] Funding Source: NIH RePORTER
- NIAAA NIH HHS [AA013588, AA08117] Funding Source: Medline
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Pharmacological studies with drugs that activate or inhibit several protein kinase C (PKC) isozymes have identified the PKC family of serine-threonine kinases as important in the regulation of gamma-aminobutyric acid type A (GABA(A)) receptor function. PKC modulates GABA(A) receptor surface density, chloride conductance and receptor sensitivity to positive allosteric modulators such as neurosteroids, ethanol, benzodiazepines and barbiturates. Recent studies using PKC isozyme-selective reagents and gene-targeted mice have begun to identify critical roles for three isozymes, PKCbetaII, PKCepsilon and PKCgamma, in various aspects of GABA(A) receptor regulation. Progress in this field touches upon therapeutic areas that are of great clinical importance such as anxiety and addiction. Increased understanding of how PKC regulates GABA(A) receptors and which PKC isozymes are involved holds promise for development of new treatments for diverse neuropsychiatric disorders.
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