pubmed-article:7631850 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7631850 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
pubmed-article:7631850 | lifeskim:mentions | umls-concept:C0010853 | lld:lifeskim |
pubmed-article:7631850 | lifeskim:mentions | umls-concept:C0037492 | lld:lifeskim |
pubmed-article:7631850 | pubmed:issue | 1 Pt 2 | lld:pubmed |
pubmed-article:7631850 | pubmed:dateCreated | 1995-9-1 | lld:pubmed |
pubmed-article:7631850 | pubmed:abstractText | To investigate the role of the cytoskeleton in cardiac Na+ channel gating, the action of cytochalasin D (Cyto-D), an agent that interferes with actin polymerization, was studied by whole cell voltage clamp and cell-attached and inside-out patches from rat and rabbit ventricular cardiac myocytes. Cyto-D (20-40 microM) reduced whole cell peak Na+ current by 20% within 12 min and slowed current decay without affecting steady-state voltage-dependent availability or recovery from inactivation. Brief treatments (< 10-15 min) of cell-attached patches by Cyto-D (20 microM) in the bath induced short bursts of Na+ channel openings and prolonged decays of ensemble-averaged currents. Bursting of the Na+ channel was more pronounced when the cell suspension was pretreated with Cyto-D (20 microM) for 1 h before seal formation. Application of Cyto-D on the cytoplasmic side of inside-out patches resulted in more dramatic gating changes. Peak open probability was reduced by > 50% within 20 min, and long bursts of openings occurred. Washout of Cyto-D did not restore ensemble-averaged current amplitude, but burst duration decreased toward control values. Cyto-D also induced an additional slower component to open and closed times. These results suggest that Cyto-D, through effects on cytoskeleton, induced cardiac Na+ channels to enter a mode characterized by a lower peak open probability but a greater persistent activity as if the inactivation rate was slowed. The cytoskeleton, in addition to localizing integral membrane proteins, apparently also plays a role in regulating specific detailed functions of integral membrane proteins such as the gating of Na+ channels. | lld:pubmed |
pubmed-article:7631850 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7631850 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7631850 | pubmed:language | eng | lld:pubmed |
pubmed-article:7631850 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7631850 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7631850 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7631850 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7631850 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7631850 | pubmed:month | Jul | lld:pubmed |
pubmed-article:7631850 | pubmed:issn | 0002-9513 | lld:pubmed |
pubmed-article:7631850 | pubmed:author | pubmed-author:UndrovinasA... | lld:pubmed |
pubmed-article:7631850 | pubmed:author | pubmed-author:MakielskiJ... | lld:pubmed |
pubmed-article:7631850 | pubmed:author | pubmed-author:ShanderG SGS | lld:pubmed |
pubmed-article:7631850 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7631850 | pubmed:volume | 269 | lld:pubmed |
pubmed-article:7631850 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7631850 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7631850 | pubmed:pagination | H203-14 | lld:pubmed |
pubmed-article:7631850 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:7631850 | pubmed:meshHeading | pubmed-meshheading:7631850-... | lld:pubmed |
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pubmed-article:7631850 | pubmed:meshHeading | pubmed-meshheading:7631850-... | lld:pubmed |
pubmed-article:7631850 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7631850 | pubmed:articleTitle | Cytoskeleton modulates gating of voltage-dependent sodium channel in heart. | lld:pubmed |
pubmed-article:7631850 | pubmed:affiliation | Division of Cardiovascular Medicine, Henry Ford Heart and Vascular Institute, Detroit, Michigan 48202, USA. | lld:pubmed |
pubmed-article:7631850 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7631850 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7631850 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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