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Excitatory amino acids in synaptic transmission in the Schaffer collateral‐commissural pathway of the rat hippocampus.
Results indicate that the synaptic receptor in the Schaffer collateral‐commissural pathway may be of the kainate or quisqualate type and although NMA receptors do not appear to be involved in normal synaptic transmission in this pathway they may play a role in synaptic plasticity.
The antagonism of amino acid‐induced excitations of rat hippocampal CA1 neurones in vitro.
DGG and APV did not affect ACh excitations and these selective antagonists should be of value in studying the involvement of the excitatory amino acids in synaptic transmission in the hippocampus, while PDA, GDEE, D‐ and L‐APB may be less useful in this regard.
Molecular determinants of the inhibition of human Kv1.5 potassium currents by external protons and Zn2+
In light of the requirement for R487, the homologue of Shaker T449, as well as the block‐relieving action of K+o, it is proposed that H+ or Zn2+ binding to histidine residues in the pore turret stabilizes a channel conformation that is most likely an inactivated state.
An activation gating switch in Kv1.2 is localized to a threonine residue in the S2-S3 linker.
Two modes of activation gating in Kv1.2 channels are demonstrated and specific residues in the S2-S3 linker that act as a switch between these modes are identified.
A Direct Demonstration of Closed-State Inactivation of K+ Channels at Low pH
Fluorescence experiments suggest the major mechanism of pH-induced peak current reduction is inactivation of channels from closed states from which they can activate, but not open; this occurs in addition to acceleration of P/C-type inactivation from the open state.
Large-conductance Calcium-activated Potassium Channels of Cultured Rat Melanotrophs
The Ca2+ dependence of the gating was approximated by a fourth power relationship suggesting the presence of fourCa2+ binding sites on the BK channel, and the channel had a conductance of ≈260 pS.
Modulation of human ether‐à‐go‐go‐related K+ (HERG) channel inactivation by Cs+ and K+
It is found that raising the concentration of external Cs+ (Cs+0) dramatically slows HERG channel inactivation without affecting activation, and a quantitative analysis suggests thatCs+0 binds to a site in the pore that is influenced by the transmembrane electrical field, so that Cs-induced slowing of HERG inactivation is less prominent at strong depolarizations.
Control of voltage-gated K+ channel permeability to NMDG+ by a residue at the outer pore
Reversal potential shifts in mixtures of K+ and NMDG+ are in accordance with PK+/PNMDG+, indicating that the ions compete for permeation and suggesting that N-methyl-d-glucamine passes through the open state.
Eicosatetraynoic acid (ETYA), a non-metabolizable analogue of arachidonic acid, blocks the fast-inactivating potassium current of rat pituitary melanotrophs.
  • S. J. Kehl
  • Chemistry, Medicine
    Canadian journal of physiology and pharmacology
  • 1 April 2001
ETYA caused a small left shift of the I(K)(f) steady-state inactivation curve and significantly slowed recovery from inactivation and the possibility that ETYA acts as an open-channel blocker is discussed.
Single channel analysis reveals different modes of Kv1.5 gating behavior regulated by changes of external pH.
The effects of external acidification, thought to reflect the protonation of a histidine residue in the turret, point to an important role for the turret in the regulation of channel availability and inactivation in the voltage-gated potassium channel.