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ATP-sensitive K+ channels in rat ventricular myocytes are blocked and inactivated by internal divalent cations
| Content Provider | Semantic Scholar |
|---|---|
| Author | Findlay, Ian M. |
| Copyright Year | 2004 |
| Abstract | K+ currents were recorded from ATP-sensitive channels in inside-out patches from isolated rat ventricular myocytes. In the absence of internal divalent cations the current voltage relationship could be described by constant-field assumptions with a permeability of 1.25×10−13 cm2/s; outward currents saturated under a high driving force for K+ movement. Internal 0.1–5.0 mM Mg2+, 0.1 μM Ca2+ and 10 mM Na+ each depressed the flux of K+ ions moving outwards through open channels. Internal 0.1–5.0 mM Mg2+, 0.1–1.0 μM Ca2+ and 1–10 μM Ba2+ and Sr2+ blocked K+ channel activity in a dose-and voltage-dependent manner. Run-down channels could be reactivated by Mg-ATP, but not by AMP-PNP, ATPγS or Mg-free ATP which suggested that phosphorylation of the channels was involved in their activity. Ca2+ (>=1 μM) and Sr2+ (1 mM) markedly inactivated K+ ATP channels, millimolar Ba2+ or Mg2+ were less effective. This suggested that the run down of the channels was a Ca2+-dependent dephosphorylation of the K+ channel protein. |
| Starting Page | 313 |
| Ending Page | 320 |
| Page Count | 8 |
| File Format | PDF HTM / HTML |
| DOI | 10.1007/BF00580282 |
| PubMed reference number | 2446256 |
| Journal | Medline |
| Volume Number | 410 |
| Alternate Webpage(s) | https://page-one.springer.com/pdf/preview/10.1007/BF00580282 |
| Alternate Webpage(s) | https://doi.org/10.1007/BF00580282 |
| Journal | Pflügers Archiv |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
