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pubmed-article:10428827pubmed:abstractTextTroponin I is the putative molecular switch for Ca(2+)-activated contraction within the myofilament of striated muscles. To gain insight into functional troponin I domain(s) in the context of the intact myofilament, adenovirus-mediated gene transfer was used to replace endogenous cardiac troponin I within the myofilaments of adult cardiac myocytes with the slow skeletal isoform or a chimera of the slow skeletal and cardiac isoforms. Efficient expression and myofilament incorporation were observed in myocytes with each exogenous troponin I protein without detected changes in the stoichiometry of other contractile proteins and/or sarcomere architecture. Contractile function studies in single, permeabilized myocytes expressing exogenous troponin I provided support for the presence of a Ca(2+)-sensitive regulatory domain in the carboxyl terminus of troponin I and a second, newly defined Ca(2+)-sensitive domain residing in the amino terminus of troponin I. Additional experiments demonstrated that the isoform-specific, acidic pH-induced contractile dysfunction in myocytes appears to lie in the carboxyl terminus of troponin I. Functional results obtained from adult cardiac myocytes expressing the chimera or isoforms of troponin I now define multiple troponin I regulatory domains operating in the intact myofilament and provide new insight into the Ca(2+)-sensitive properties of troponin I during contraction.lld:pubmed
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pubmed-article:10428827pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:10428827pubmed:articleTitleFunctional analysis of troponin I regulatory domains in the intact myofilament of adult single cardiac myocytes.lld:pubmed
pubmed-article:10428827pubmed:affiliationDepartment of Physiology, School of Medicine, University of Michigan, Ann Arbor, Michigan 48109-0622, USA. wfall@w.imap.itd.umich.edulld:pubmed
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