The calcium transport mechanism of cardiac sarcoplasmic reticulum (SR) is (SR) is regulated by a phosphoregulatory mechanism involving the phosphorylation-dephosphorylation of an integral membrane component, termed phospholamban. Phospholamban, a 27,000 Da proteolipid, contains phosphorylation sites
Activation by intracellular calcium of a potassium channel in cardiac sarcoplasmic reticulum
โ Scribed by Akira Uehara; Midori Yasukohchi; Shigenori Ogata; Issei Imanaga
- Publisher
- Springer
- Year
- 1991
- Tongue
- English
- Weight
- 325 KB
- Volume
- 417
- Category
- Article
- ISSN
- 0031-6768
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โฆ Synopsis
The effects of low (pCa 7.5 to 3) concentrations of intracellular calcium ion on a single potassium channel in the sarcoplasmic reticulum of canine heart ventricular muscle were investigated using a planar lipid bilayer technique. The low concentrations were obtained by mixing EGTA and calcium chloride. By varying the pCa of the cytoplasmic face between 3 to 7.5, two novel effects were observed.
First, an increase in the intracellular Ca 2+ concentration produced an increase in the unit current amplitude of open states; the voltage-current relationship was ohmic at these concentrations_ Second, an increase in the Ca 2+ concentration increased the open probability. Both these effects of Ca 2+ were dose-dependent, arid were consistently observed in all channels tested.
Thus, the SR potassium channel observed appears to belong to the class of Ca "+ -activated potassium channels.
๐ SIMILAR VOLUMES
Concentration-dependent effects of intracellular GTP on activation of the muscarinic K + channel were examined in inside-out patches of cardiac atrial myocytes. The pipette solution contained 0.i ~I ACh. GTP (0.01-30 ~M) and 0.5 mM MgCI 2 were applied to the inside side of the patch membrane. K + ch
Calcium-activated potassium channels in the luminal membrane of Amphiuma diluting segment were studied using the patch-clamp technique in both the cell-attached and inside-out configurations. The open probability (Po) of the channel is sensitive to both membrane potential and cytoplasmic calcium act