Source:http://linkedlifedata.com/resource/pubmed/id/11406292
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
2001-6-14
|
| pubmed:databankReference | |
| pubmed:abstractText |
Embryonic Xenopus muscle cells grown in culture express voltage-gated K+ currents with inactivating and non-inactivating kinetics. Here we report the cloning of three K+ channel cDNAs, designated XKv1.2', XKv1.4 and XKv1.10, from muscle which may underlie these currents. XKv1.2' cDNA appears to be an allelic variant of the XKv1.2 previously cloned from Xenopus. The second cDNA encodes a homologue of Kv1.4 that has not been previously cloned from Xenopus. The predicted XKv1.4 protein shows 73% overall similarity to mouse and chick Kv1.4, but shows significant divergence in the region corresponding to the chain of the inactivating 'ball and chain' domain. The third K+ channel cDNA isolated from Xenopus muscle is a novel Kv1 isoform designated XKv1.10. The predicted protein shares about 70% similarity with other members of the Kv1 subfamily, and about 40% with members of the Kv2, Kv3 and Kv4 subfamilies. XKv1.4 mRNA appears as early as stage 10.5 in whole embryos and is prominent in muscle throughout development from stage 14 to adult. XKv1.2' mRNA is detected by stage 11.5 in whole embryos, but remains at low levels in embryonic skeletal muscle (stages 14 and 21), and is absent from adult muscle. XKv1.10 mRNA is first detected at stage 21 in whole embryos, and is present in muscle from this stage onwards. All three transcripts are present in spinal cord at stage 21. The results support the notion that channels encoded by XKv1.4 contribute to the inactivating K+ current observed in embryonic muscle cells in culture.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Kv1.2 Potassium Channel,
http://linkedlifedata.com/resource/pubmed/chemical/Kv1.4 Potassium Channel,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Voltage-Gated,
http://linkedlifedata.com/resource/pubmed/chemical/Shaker Superfamily of Potassium...,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0169-328X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
90
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
135-48
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:11406292-Animals,
pubmed-meshheading:11406292-Base Sequence,
pubmed-meshheading:11406292-Cloning, Molecular,
pubmed-meshheading:11406292-DNA, Complementary,
pubmed-meshheading:11406292-Gene Expression,
pubmed-meshheading:11406292-Ion Channel Gating,
pubmed-meshheading:11406292-Kv1.2 Potassium Channel,
pubmed-meshheading:11406292-Kv1.4 Potassium Channel,
pubmed-meshheading:11406292-Molecular Sequence Data,
pubmed-meshheading:11406292-Muscle, Skeletal,
pubmed-meshheading:11406292-Polymerase Chain Reaction,
pubmed-meshheading:11406292-Potassium Channels,
pubmed-meshheading:11406292-Potassium Channels, Voltage-Gated,
pubmed-meshheading:11406292-Protein Structure, Tertiary,
pubmed-meshheading:11406292-Sequence Homology, Amino Acid,
pubmed-meshheading:11406292-Shaker Superfamily of Potassium Channels,
pubmed-meshheading:11406292-Xenopus,
pubmed-meshheading:11406292-Xenopus Proteins
|
| pubmed:year |
2001
|
| pubmed:articleTitle |
Cloning and expression of three K+ channel cDNAs from Xenopus muscle.
|
| pubmed:affiliation |
Division of Basic Medical Sciences, Memorial University of Newfoundland, Newfoundland, A1B 3V6, St John's, Canada.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|