Document Detail

Comparative proteomic analysis of the ATP-sensitive K+ channel complex in different tissue types.
MedLine Citation:
PMID:  23197389     Owner:  NLM     Status:  MEDLINE    
ATP-sensitive K(+) (K(ATP)) channels are expressed ubiquitously, but have diverse roles in various organs and cells. Their diversity can partly be explained by distinct tissue-specific compositions of four copies of the pore-forming inward rectifier potassium channel subunits (Kir6.1 and/or Kir6.2) and four regulatory sulfonylurea receptor subunits (SUR1 and/or SUR2). Channel function and/or subcellular localization also can be modified by the proteins with which they transiently or permanently interact to generate even more diversity. We performed a quantitative proteomic analysis of K(ATP) channel complexes in the heart, endothelium, insulin-secreting min6 cells (pancreatic β-cell like), and the hypothalamus to identify proteins with which they interact in different tissues. Glycolysis is an overrepresented pathway in identified proteins of the heart, min6 cells, and the endothelium. Proteins with other energy metabolic functions were identified in the hypothalamic samples. These data suggest that the metabolo-electrical coupling conferred by K(ATP) channels is conferred partly by proteins with which they interact. A large number of identified cytoskeletal and trafficking proteins suggests endocytic recycling may help control K(ATP) channel surface density and/or subcellular localization. Overall, our data demonstrate that K(ATP) channels in different tissues may assemble with proteins having common functions, but that tissue-specific complex organization also occurs.
Eirini Kefaloyianni; John S Lyssand; Cesar Moreno; Diane Delaroche; Miyoun Hong; David Fenyö; Charles V Mobbs; Thomas A Neubert; William A Coetzee
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2013-01-03
Journal Detail:
Title:  Proteomics     Volume:  13     ISSN:  1615-9861     ISO Abbreviation:  Proteomics     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-23     Completed Date:  2013-06-25     Revised Date:  2014-01-09    
Medline Journal Info:
Nlm Unique ID:  101092707     Medline TA:  Proteomics     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  368-78     Citation Subset:  IM    
Copyright Information:
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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MeSH Terms
ATP-Binding Cassette Transporters
Endothelium / chemistry,  metabolism
Insulin-Secreting Cells / chemistry,  metabolism
KATP Channels / analysis,  chemistry*,  metabolism*
Myocardium / chemistry,  metabolism
Organ Specificity
Potassium Channels, Inwardly Rectifying
Proteomics / methods*
Receptors, Drug
Sulfonylurea Receptors
Grant Support
Reg. No./Substance:
0/Abcc8 protein, mouse; 0/KATP Channels; 0/Potassium Channels, Inwardly Rectifying; 0/Receptors, Drug; 0/Sulfonylurea Receptors

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