| Autor: |
Suh, Suk H., Watanabe, Hiroyuki, Droogmans, Guy, Nilius, Bernd |
| Předmět: |
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| Zdroj: |
Pflügers Archiv: European Journal of Physiology; Jun2002, Vol. 444 Issue 3, p438-445, 8p |
| Abstrakt: |
We have studied the properties of a non-selective cation current (NSCCa) in macrovascular endothelial cells derived from human umbilical vein (EA cells) that is activated by an increase of intracellular Ca2+ concentration, [Ca2+]i. Current–voltage relationships are linear and the kinetics of the current is time-independent. Current–[Ca2+]i relationships were fitted to a Ca2+ binding site model with a concentration for half-maximal activation of 417±76 nM, a Hill coefficient of 2.3±0.8 and a maximum current of –23.9±2.7 pA/pF at –50 mV. The Ca2+-activated channel is more permeable to Na+ than for Cs+ (PCs/PNa=0.58, n=7), but virtually impermeable to Ca2+. Current activation was transient if ATP was omitted from the pipette solution. The maximal currents at 300 and 500 nM [Ca2+]i were smaller than in the absence of ATP, but were not significantly different at 2 µM. The intracellular Ca2+ concentration for half-maximal activation of the Ca2+-activated current was shifted to 811±12 nM in the absence of ATP. Substitution of ATP by the non-hydrolysable ATP analogue adenylylimidodiphosphate (AMP-PNP) did not affect current activation. Sodium nitroprusside (SNP) decreased NSCCa in a concentration-dependent manner. The nitric oxide (NO) donors S-nitroso-N-acetylpenicillamine (SNAP) and 3-morpholinosydnonimine (SIN-1) also inhibited NSCCa. In contrast, nitro-L-arginine (NLA), which inhibits all NO-synthases, potentiated NSCCa, whereas superoxide dismutase (SOD), which inhibits the breakdown of NO, inhibited NSCCa. It is concluded that the Ca2+-activated non-selective action channel in EA cells is modulated by the metabolic state of the cell and by NO. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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