Are Inward Rectifier K+ Channels Responsible for Integrin‐Modulated Oxidative Burst Activity?
نویسندگان
چکیده
منابع مشابه
Silent inward rectifier K+ channels in hypercholesterolemia.
Hypercholesterolemia is an independent risk factor for development of cardiovascular disease1 and has been demonstrated to impair endothelium-dependent and independent vasodilatation.2 However, the mechanisms responsible for changes in vascular reactivity and impaired blood flow regulation induced by hypercholesterolemia remain unclear. Previous studies in cultured endothelial cells have shown ...
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Rectification of macroscopic current through inward-rectifier K+ (Kir) channels reflects strong voltage dependence of channel block by intracellular cations such as polyamines. The voltage dependence results primarily from the movement of K+ ions across the transmembrane electric field, which accompanies the binding-unbinding of a blocker. Residues D172, E224, and E299 in IRK1 are critical for ...
متن کاملCarboxy-terminal Determinants of Conductance in Inward-rectifier K Channels
Previous studies suggested that the cytoplasmic COOH-terminal portions of inward rectifier K channels could contribute significant resistance barriers to ion flow. To explore this question further, we exchanged portions of the COOH termini of ROMK2 (Kir1.1b) and IRK1 (Kir2.1) and measured the resulting single-channel conductances. Replacing the entire COOH terminus of ROMK2 with that of IRK1 de...
متن کاملMechanism of Rectification in Inward-rectifier K+ Channels
Inward rectifiers are a class of K+ channels that can conduct much larger inward currents at membrane voltages negative to the K+ equilibrium potential than outward currents at voltages positive to it, even when K+ concentrations on both sides of the membrane are made equal. This conduction property, called inward rectification, enables inward rectifiers to perform many important physiological ...
متن کاملThe Polyamine Binding Site in Inward Rectifier K+ Channels
Strongly inwardly rectifying potassium channels exhibit potent and steeply voltage-dependent block by intracellular polyamines. To locate the polyamine binding site, we have examined the effects of polyamine blockade on the rate of MTSEA modification of cysteine residues strategically substituted in the pore of a strongly rectifying Kir channel (Kir6.2[N160D]). Spermine only protected cysteines...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2009
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.23.1_supplement.762.21