h-89 and cesium-chloride

h-89 has been researched along with cesium-chloride* in 2 studies

Other Studies

2 other study(ies) available for h-89 and cesium-chloride

Article	Year
Mediation of hippocampal mossy fiber long-term potentiation by presynaptic Ih channels. Science (New York, N.Y.), 2002, Jan-04, Volume: 295, Issue:5552 Hippocampal mossy fiber long-term potentiation (LTP) is expressed presynaptically, but the exact mechanisms remain unknown. Here, we demonstrate the involvement of the hyperpolarization-activated cation channel (Ih) in the expression of mossy fiber LTP. Established LTP was blocked and reversed by Ih channel antagonists. Whole-cell recording from granule cells revealed that repetitive stimulation causes a calcium- and Ih-dependent long-lasting depolarization mediated by protein kinase A. Depolarization at the terminals would be expected to enhance transmitter release, whereas somatic depolarization would enhance the responsiveness of granule cells to afferent input. Thus, Ih channels play an important role in the long-lasting control of transmitter release and neuronal excitability. Topics: Adenylyl Cyclases; Animals; Benzazepines; Calcium; Cesium; Chlorides; Colforsin; Cyclic AMP; Cyclic AMP-Dependent Protein Kinases; Cyclic Nucleotide-Gated Cation Channels; Dentate Gyrus; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels; In Vitro Techniques; Ion Channels; Isoquinolines; Long-Term Potentiation; Membrane Potentials; Membrane Proteins; Models, Neurological; Mossy Fibers, Hippocampal; Nerve Tissue Proteins; Patch-Clamp Techniques; Potassium; Potassium Channels; Presynaptic Terminals; Pyramidal Cells; Pyrimidines; Rats; Rats, Sprague-Dawley; Sulfonamides; Synaptic Transmission	2002
Common components of patch-clamp internal recording solutions can significantly affect protein kinase A activity. Brain research, 1999, May-15, Volume: 828, Issue:1-2 Common components of whole-cell internal recording solutions were tested both in vitro and in patch-clamp experiments for their effects on the activity of cAMP-dependent protein kinase. Potassium fluoride (KF), 440 mM trimethylamine chloride and exclusion of bovine serum albumin (BSA) decreased the activity of the enzyme, while ethylene glycol-bis (beta-aminoethyl ether) N,N,N',N'-tetraacetic acid (EGTA) and the potassium salts of aspartate, gluconate, methylsulfate and monobasic phosphate increased its activity. Addition of KF to the internal solution produced a hyperpolarizing shift in the V1/2 of Ih channel activation, consistent with the KF-induced reduction of protein kinase A activity. Therefore, consideration of the composition of internal solutions is warranted when studying channel physiology by patch-clamp techniques. Topics: Animals; Aspartic Acid; Calcium; Cells, Cultured; Cesium; Chelating Agents; Chlorides; Cyclic AMP-Dependent Protein Kinases; Egtazic Acid; Enzyme Activation; Enzyme Inhibitors; Fluorides; Gluconates; Ion Channels; Isoquinolines; Methylamines; Olfactory Receptor Neurons; Patch-Clamp Techniques; Phosphates; Phosphorylation; Potassium Compounds; Rats; Second Messenger Systems; Serum Albumin, Bovine; Sulfonamides; Sulfuric Acid Esters; Tetraethylammonium	1999

Article

Year

Mediation of hippocampal mossy fiber long-term potentiation by presynaptic Ih channels.

Science (New York, N.Y.), 2002, Jan-04, Volume: 295, Issue:5552

Hippocampal mossy fiber long-term potentiation (LTP) is expressed presynaptically, but the exact mechanisms remain unknown. Here, we demonstrate the involvement of the hyperpolarization-activated cation channel (Ih) in the expression of mossy fiber LTP. Established LTP was blocked and reversed by Ih channel antagonists. Whole-cell recording from granule cells revealed that repetitive stimulation causes a calcium- and Ih-dependent long-lasting depolarization mediated by protein kinase A. Depolarization at the terminals would be expected to enhance transmitter release, whereas somatic depolarization would enhance the responsiveness of granule cells to afferent input. Thus, Ih channels play an important role in the long-lasting control of transmitter release and neuronal excitability.

Topics: Adenylyl Cyclases; Animals; Benzazepines; Calcium; Cesium; Chlorides; Colforsin; Cyclic AMP; Cyclic AMP-Dependent Protein Kinases; Cyclic Nucleotide-Gated Cation Channels; Dentate Gyrus; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels; In Vitro Techniques; Ion Channels; Isoquinolines; Long-Term Potentiation; Membrane Potentials; Membrane Proteins; Models, Neurological; Mossy Fibers, Hippocampal; Nerve Tissue Proteins; Patch-Clamp Techniques; Potassium; Potassium Channels; Presynaptic Terminals; Pyramidal Cells; Pyrimidines; Rats; Rats, Sprague-Dawley; Sulfonamides; Synaptic Transmission

2002

Common components of patch-clamp internal recording solutions can significantly affect protein kinase A activity.

Brain research, 1999, May-15, Volume: 828, Issue:1-2

Common components of whole-cell internal recording solutions were tested both in vitro and in patch-clamp experiments for their effects on the activity of cAMP-dependent protein kinase. Potassium fluoride (KF), 440 mM trimethylamine chloride and exclusion of bovine serum albumin (BSA) decreased the activity of the enzyme, while ethylene glycol-bis (beta-aminoethyl ether) N,N,N',N'-tetraacetic acid (EGTA) and the potassium salts of aspartate, gluconate, methylsulfate and monobasic phosphate increased its activity. Addition of KF to the internal solution produced a hyperpolarizing shift in the V1/2 of Ih channel activation, consistent with the KF-induced reduction of protein kinase A activity. Therefore, consideration of the composition of internal solutions is warranted when studying channel physiology by patch-clamp techniques.

Topics: Animals; Aspartic Acid; Calcium; Cells, Cultured; Cesium; Chelating Agents; Chlorides; Cyclic AMP-Dependent Protein Kinases; Egtazic Acid; Enzyme Activation; Enzyme Inhibitors; Fluorides; Gluconates; Ion Channels; Isoquinolines; Methylamines; Olfactory Receptor Neurons; Patch-Clamp Techniques; Phosphates; Phosphorylation; Potassium Compounds; Rats; Second Messenger Systems; Serum Albumin, Bovine; Sulfonamides; Sulfuric Acid Esters; Tetraethylammonium

1999