Titin-isoform dependence of titin-actin interaction and its regulation by S100A1/Ca2+ in skinned myocardium.
Titin, also known as connectin, is a large filamentous protein that greatly contributes to passive myocardial stiffness. In vitro evidence suggests that one of titin's spring elements, the PEVK, interacts with actin and that this adds a viscous component to passive stiffness. Differential splicing o...
| Publicado en: | Journal of Biomedicine & Biotechnology pp. 727239 - 727240 |
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| Autores principales: | , , |
| Formato: | research Journal Article |
| Publicado: |
Wiley-Blackwell
2010
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=105082040&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 105082040 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 11107243 137K jtl: Journal of Biomedicine & Biotechnology issn: 11107243 maglogo: N pubinfo: dt: 2010 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 105082040 105082040 2010748483 NLM20414336 PMC2855102 105082040 ppf: 727239 ppct: 1 formats: fmt: @attributes: type: P tig: atl: Titin-isoform dependence of titin-actin interaction and its regulation by S100A1/Ca2+ in skinned myocardium. aug: au: Fukushima H Chung CS Granzier H affil: Department of Physiology, Sarver Molecular Cardiovascular Research Program, University of Arizona, PO Box 245217, Tucson, AZ 85724, USA. sug: subj: Calcium Binding Proteins Metabolism Calcium Metabolism Muscle Proteins Metabolism Myocardium Metabolism Protein Kinases Metabolism Analysis of Variance Animal Studies Cattle Elasticity Heart Atrium Heart Atrium Metabolism Heart Ventricle Heart Ventricle Metabolism Male Mice Microfilament Proteins Pharmacodynamics Muscle Tonus Drug Effects Myocardium Proteins Male ab: Titin, also known as connectin, is a large filamentous protein that greatly contributes to passive myocardial stiffness. In vitro evidence suggests that one of titin's spring elements, the PEVK, interacts with actin and that this adds a viscous component to passive stiffness. Differential splicing of titin gives rise to the stiff N2B and more compliant N2BA isoforms. Here we studied the titin-isoform dependence of titin-actin interaction and studied the bovine left atrium (BLA) that expresses mainly N2BA titin, and the bovine left ventricle (BLV) that expresses a mixture of both N2B and N2BA isoforms. For comparison we also studied mouse left ventricular (MLV) myocardium which expresses predominately N2B titin. Using the actin-severing protein gelsolin, we obtained evidence that titin-actin interaction contributes significantly to passive myocardial stiffness in all tissue types, but most in MLV, least in BLA, and an intermediate level in BLV. We also studied whether titin-actin interaction is regulated by S100A1/calcium and found that calcium alone or S100A1 alone did not alter passive stiffness, but that combined they significantly lowered stiffness. We propose that titin-actin interaction is a 'viscous break' that is on during diastole and off during systole. pubtype: Academic Journal doctype: research Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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