ArticlePflugers Archiv : European journal of physiology2009
Functional properties of human neuronal Kv11 channels.
Article in Pflugers Archiv : European journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Mechanistic correlation of potassium channel sensing and nitric oxide activity in neuroinflammation.Molecular biology reports · 2025Review
- Association Study ofFrontiers in psychiatry · 2019Article
- Antiarrhythmics cure brain arrhythmia: The imperativeness of subthalamic ERG KScience advances · 2017Article
- Variants in Ion Channel Genes Link Phenotypic Features of Bipolar Illness to Specific Neurobiological Process Domains.Molecular neuropsychiatry · 2015Review
- A population-based study of KCNH7 p.Arg394His and bipolar spectrum disorder.Human molecular genetics · 2014Article
- Fast detection of extrasynaptic GABA with a whole-cell sniffer.Frontiers in cellular neuroscience · 2014Article
- Article
- Two four-marker haplotypes on 7q36.1 region indicate that the potassium channel gene HERG1 (KCNH2, Kv11.1) is related to schizophrenia: a case control study.Behavioral and brain functions : BBF · 2010Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kv11 potassium channels are important for regulation of the membrane potential. Kv11.2 and Kv11.3 are primarily found in the nervous system, where they most likely are involved in the regulation of neuronal excitability. Two isoforms of human Kv11.2 have been published so far. Here, we present a new splice variant that is present in human brain as demonstrated by reverse transcription PCR. Heterologous expression in Xenopus laevis oocytes revealed a 30-mV shift in the voltage dependence of activation to more depolarized potentials and slower activation together with faster deactivation kinetics compared to hKv11.1. Further, we have cloned and electrophysiologically characterized two splice variants of hKv11.3. When expressed in X. laevis oocytes, both isoform 1 and isoform 2 elicited robust currents with a striking transient current component caused by delayed inactivation. The different current characteristics of the isoforms presented in this work may contribute to the regulation of neuronal excitability.
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