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PMID: 1705709 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Cloning and tissue-specific expression of five voltage-gated potassium channel cDNAs expressed in rat heart.

Roberds SL, Tamkun MM

Abstract

Five distinct K+ channel cDNA molecules (RK1 to RK5) were cloned from either rat heart or rat aorta cDNA libraries. Four of the channels, RK1 to RK4, are similar or identical to Shaker-like K+ channels previously identified in rat brain cDNA libraries. Major differences among RK1 to RK4 exist in the amino- and carboxyl-terminal regions and in amino acids representing potential extracellular sequence between the S1 and S2 hydrophobic domains. RK5 encodes a unique channel of 490 amino acids having six hydrophobic domains but only five basic residues in the putative voltage-sensing domain. Unlike RK1 to RK4, RK5 is a rat homologue of the Drosophila Shal family of K+ channels, which have not been previously described in mammals. Although RK5 mRNA is present in cardiac atrium and ventricle, it is most abundant in brain. RK1, RK2, and RK3 transcripts are predominantly found in brain but are present also at lower levels in other tissues, such as heart and aorta. RK2 is absent from skeletal muscle whereas RK1 and RK3 are present in this tissue. RK4 mRNA is ubiquitous in electrically excitable tissue, being present at comparable levels in atrium, ventricle, aorta, brain, and skeletal muscle. The cloning of RK5 confirms the presence in mammals of all four Drosophila K+ channel families: Shaker, Shab, Shaw, and Shal.

MeSH Terms
Amino Acid Sequence Aorta/physiology Base Sequence Cloning, Molecular/methods DNA/genetics,isolation & purification Gene Expression Gene Library Heart/physiology Molecular Sequence Data Muscle, Smooth, Vascular/physiology Organ Specificity Polymerase Chain Reaction Potassium Channels/genetics,physiology RNA/genetics,isolation & purification Sequence Homology, Nucleic Acid
Chemicals
Potassium Channels RNA DNA
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Roberds S L
Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232.
Tamkun M M
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1991-03-01
Pages
1798-802
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC51112
Subset
IM
Grants
NIGMS NIH HHS · GM 07628 · United States
NIGMS NIH HHS · GM 41325 · United States
Databases
GENBANK
M58062, M58063, M58064, M58065, M58066, M58067, M59766, M59767, M59768, M59980
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