ArticleThe Journal of physiology1996
Studies on the blocking action of human Kv3.4 inactivation peptide variants in the mouse cloned Kv1.1 K+ channel.
Article in The Journal of physiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Functional analysis of ctenophore Shaker KBiophysical journal · 2024Article
- Ca(2+)/calmodulin regulates Kvβ1.1-mediated inactivation of voltage-gated K(+) channels.Scientific reports · 2015Article
- Bupivacaine blocks N-type inactivating Kv channels in the open state: no allosteric effect on inactivation kinetics.Biophysical journal · 2008Article
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
1. Whole-cell patch clamp recordings were made from Chinese hamster ovary (CHO) cells stably expressing homomeric mouse Kv1.1 (delayed rectifier K+; mKv1.1) channels. The effects of internal application of a number of different peptides, based on part of the amino terminal sequence of the human Kv3.4 channel subunit (hKv3.4), were examined in order to determine their influence on N-type inactivation. 2. For the native hKv3.4 peptide, the association rate constant (kon) increased with membrane depolarization, whilst the dissociation rate constant (koff) had little dependence on voltage. This resulted in the apparent dissociation constant (KD) of the hKv3.4 peptide tending to increase with depolarization. 3. In general, kon increased and apparent KD decreased with positive charge of the hKv3.4 peptide variants; in peptides lacking a hydrophobic amino terminal this correlation was not maintained. In contrast, the rate of dissociation of the variant peptides (koff) was independent of net charge. 4. The blocking activity of the hKv3.4 peptide was not dependent on a disulphide bridge between cysteine residues C6 and C24 and the presence of cysteine residues in the hKv3.4 peptide was not a prerequisite for rapid inactivation. All cysteine-substituted variants, especially at C6, showed a more rapid recovery from inactivation than the hKv3.4 peptide. Substitutions at C24, and not C6, reduced kon. 5. The present results concerning the action of the mammalian hKv3.4 channel inactivation particle on mKv1.1 channels complement earlier models for the invertebrate Shaker K+ channel. It is proposed that the hydrophobic amino terminal region of the hKv3.4 inactivation peptide blocks the channel pore, whilst the adjacent positively charged region interacts with negative charges on the channel protein.
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