| pubmed-article:6093100 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6093100 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:6093100 | lifeskim:mentions | umls-concept:C0028778 | lld:lifeskim |
| pubmed-article:6093100 | lifeskim:mentions | umls-concept:C0006685 | lld:lifeskim |
| pubmed-article:6093100 | lifeskim:mentions | umls-concept:C0028127 | lld:lifeskim |
| pubmed-article:6093100 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:6093100 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:6093100 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:6093100 | pubmed:dateCreated | 1984-12-7 | lld:pubmed |
| pubmed-article:6093100 | pubmed:abstractText | Block of Ca2+ currents by the dihydropyridine drug nitrendipine was studied in single canine ventricular cells by using the whole-cell variant of the patch clamp technique. When cells were held at depolarized membrane potentials at which Ca2+ currents were approximately equal to 70% inactivated, nitrendipine blocked Ca2+ currents very potently, with half-block by subnanomolar concentrations. The concentration dependence of block had the form expected for 1:1 binding, with an apparent dissociation constant (Kd) of 0.36 nM. In contrast, when cells were held at hyperpolarized potentials, nitrendipine blocked Ca2+ currents much less potently (Kd approximately equal to 700 nM). The results can be explained if nitrendipine binds very tightly to the inactivated state of the Ca2+ channel and only weakly to the normal resting state. The Kd estimated for binding to the inactivated state is very similar to the dissociation constants previously found for high-affinity [3H]nitrendipine binding to membrane fragments from heart, smooth muscle, brain, and other tissues; moreover, the concentration-dependent kinetics of binding to the inactivated state are similar to those reported for [3H]nitrendipine binding to membranes. These results make it seem very likely that the high-affinity [3H]nitrendipine binding site is an inactivated state of the Ca2+ channel. | lld:pubmed |
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| pubmed-article:6093100 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:6093100 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6093100 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6093100 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:6093100 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:6093100 | pubmed:author | pubmed-author:BeanB PBP | lld:pubmed |
| pubmed-article:6093100 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6093100 | pubmed:volume | 81 | lld:pubmed |
| pubmed-article:6093100 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6093100 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6093100 | pubmed:pagination | 6388-92 | lld:pubmed |
| pubmed-article:6093100 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6093100 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6093100 | pubmed:articleTitle | Nitrendipine block of cardiac calcium channels: high-affinity binding to the inactivated state. | lld:pubmed |
| pubmed-article:6093100 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6093100 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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