Linked Life Data

12479237

Source:http://linkedlifedata.com/resource/pubmed/id/12479237

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:12479237rdf:typepubmed:Citationlld:pubmed
pubmed-article:12479237lifeskim:mentionsumls-concept:C0086418lld:lifeskim
pubmed-article:12479237lifeskim:mentionsumls-concept:C0018801lld:lifeskim
pubmed-article:12479237lifeskim:mentionsumls-concept:C0036226lld:lifeskim
pubmed-article:12479237lifeskim:mentionsumls-concept:C0596235lld:lifeskim
pubmed-article:12479237lifeskim:mentionsumls-concept:C2346689lld:lifeskim
pubmed-article:12479237lifeskim:mentionsumls-concept:C1550025lld:lifeskim
pubmed-article:12479237pubmed:dateCreated2002-12-13lld:pubmed
pubmed-article:12479237pubmed:abstractTextExcitation-contraction coupling and intracellular Ca2+ homeostasis are altered in heart failure. We tested the hypothesis that these changes are related to disturbed Ca2+ handling of the sarcoplasmic reticulum (SR). Isolated, electrically stimulated trabeculae were obtained from end-stage failing (NYHA IV) and nonfailing human hearts. Isometric twitch tension, intracellular Ca2+ transients (aequorin method) and SR Ca2+ content (rapid cooling contractures) were assessed under basal conditions (1 Hz, 37 degrees C) as well as after stepwise increasing rest intervals from 2-240 s (post-rest contractions). Protein expression of SERCA2a and phospholamban (Western blot) was assessed in a subset of failing trabeculae. In addition, the effects of SERCA1 overexpression on contractile function of isolated myocytes was tested. On average, post-rest twitch tension continuously increased with increasing rest intervals in nonfailing, but declined with rest intervals longer than 15 s in failing myocardium. The rest-dependent contractile changes were accompanied by parallel changes in intracellular Ca2+ transients. Failing trabeculae (n = 40) were grouped (group A: post-rest potentiation (force of contraction > pre-rest twitch force) after 120 s rest interval; group B: post-rest decay (force of contraction < pre-rest twitch force) after 120 s rest interval), and post-rest contractile function was related to SERCA2a and PLB expression. While PLB protein expression was not different, SERCA2a protein expression as well as SERCA2a/PLB ratio was significantly higher in group A vs. group B. Transfection of SERCA1 increased shortening amplitude and enhanced relaxation kinetics in failing human myocytes. In conclusion, SR Ca2+ handling is severely altered in human heart failure. Reduced SR Ca2+ release is due to diminished SR Ca2+ content directly related to a depressed expression of SERCA2a protein. Enhancing SERCA function or expression may improve SR Ca2+ handling in failing human myocardium.lld:pubmed
pubmed-article:12479237pubmed:languageenglld:pubmed
pubmed-article:12479237pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12479237pubmed:citationSubsetIMlld:pubmed
pubmed-article:12479237pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12479237pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12479237pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12479237pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12479237pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12479237pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:12479237pubmed:statusMEDLINElld:pubmed
pubmed-article:12479237pubmed:issn0300-8428lld:pubmed
pubmed-article:12479237pubmed:authorpubmed-author:MaierLars SLSlld:pubmed
pubmed-article:12479237pubmed:authorpubmed-author:PieskeBurkert...lld:pubmed
pubmed-article:12479237pubmed:authorpubmed-author:Schmidt-Schwe...lld:pubmed
pubmed-article:12479237pubmed:issnTypePrintlld:pubmed
pubmed-article:12479237pubmed:volume97 Suppl 1lld:pubmed
pubmed-article:12479237pubmed:ownerNLMlld:pubmed
pubmed-article:12479237pubmed:authorsCompleteYlld:pubmed
pubmed-article:12479237pubmed:paginationI63-71lld:pubmed
pubmed-article:12479237pubmed:dateRevised2010-11-18lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:meshHeadingpubmed-meshheading:12479237...lld:pubmed
pubmed-article:12479237pubmed:year2002lld:pubmed
pubmed-article:12479237pubmed:articleTitleSarcoplasmic reticulum Ca2+ load in human heart failure.lld:pubmed
pubmed-article:12479237pubmed:affiliationLabor für Molekulare Kardiologie und Herzmuskelphysiologie, Abteilung Kardiologie und Angiologie, Georg-August-Universität Göttingen, Robert-Koch-Str. 40, 37085 Göttingen, Germany. pieske@med.uni-goettingen.delld:pubmed
pubmed-article:12479237pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:12479237pubmed:publicationTypeIn Vitrolld:pubmed
pubmed-article:12479237pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:487entrezgene:pubmedpubmed-article:12479237lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12479237lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:12479237lld:pubmed