Source:http://linkedlifedata.com/resource/pubmed/id/10428827
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
32
|
pubmed:dateCreated |
1999-9-2
|
pubmed:abstractText |
Troponin 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.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
6
|
pubmed:volume |
274
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
22508-16
|
pubmed:dateRevised |
2011-11-17
|
pubmed:meshHeading |
pubmed-meshheading:10428827-Actin Cytoskeleton,
pubmed-meshheading:10428827-Allosteric Regulation,
pubmed-meshheading:10428827-Animals,
pubmed-meshheading:10428827-Calcium,
pubmed-meshheading:10428827-Female,
pubmed-meshheading:10428827-Gene Transfer Techniques,
pubmed-meshheading:10428827-Heart,
pubmed-meshheading:10428827-Hydrogen-Ion Concentration,
pubmed-meshheading:10428827-Isometric Contraction,
pubmed-meshheading:10428827-Muscle, Skeletal,
pubmed-meshheading:10428827-Muscle Fibers, Slow-Twitch,
pubmed-meshheading:10428827-Myocardial Contraction,
pubmed-meshheading:10428827-Myocardium,
pubmed-meshheading:10428827-Protein Isoforms,
pubmed-meshheading:10428827-Rats,
pubmed-meshheading:10428827-Recombinant Fusion Proteins,
pubmed-meshheading:10428827-Troponin I
|
pubmed:year |
1999
|
pubmed:articleTitle |
Functional analysis of troponin I regulatory domains in the intact myofilament of adult single cardiac myocytes.
|
pubmed:affiliation |
Department of Physiology, School of Medicine, University of Michigan, Ann Arbor, Michigan 48109-0622, USA. wfall@w.imap.itd.umich.edu
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|