Inhibition of the electrogenic Na,K pump and Na,K-ATPase activity by tetraethylammonium, tetrabutylammonium, and apamin
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
2838645
DOI
10.1002/jnr.490190414
Knihovny.cz E-zdroje
- MeSH
- apamin farmakologie MeSH
- bránice účinky léků metabolismus MeSH
- draslík metabolismus MeSH
- kvartérní amoniové sloučeniny farmakologie MeSH
- membránové potenciály účinky léků MeSH
- mikrozomy účinky léků metabolismus MeSH
- mozek účinky léků metabolismus MeSH
- myši MeSH
- ouabain metabolismus MeSH
- sodík metabolismus MeSH
- sodíko-draslíková ATPasa metabolismus MeSH
- tetraethylamoniové sloučeniny farmakologie MeSH
- včelí jedy farmakologie MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- apamin MeSH
- draslík MeSH
- kvartérní amoniové sloučeniny MeSH
- ouabain MeSH
- sodík MeSH
- sodíko-draslíková ATPasa MeSH
- tetrabutylammonium MeSH Prohlížeč
- tetraethylamoniové sloučeniny MeSH
- včelí jedy MeSH
The K+-induced hyperpolarization of Na-loaded mouse diaphragm muscle, enzymatic activity of Na,K-ATPase and 3H-ouabain binding to rat brain microsomes was measured in the presence of K+ channel blockers tetraethylammonium (TEA), tetrabutylammonium (TBA) and apamin. TBA, and to a lesser extent TEA in millimolar concentrations, inhibited the electrogenic effect of the Na,K pump, Na,K-ATPase activity, and 3H-ouabain binding. The inhibition of 3H-ouabain binding by TEA or TBA was more evident in the presence of ATP and Na+ ions. Apamin in nanomolar concentrations inhibited the electrogenic effect of Na,K pump and Na,K-ATPase but not the 3H-ouabain binding. The hyperpolarizing effects of insulin and NADH, but not that of noradrenaline, were also prevented by apamin. The inhibition of Na,K pump by TEA and TBA is apparently due to both competition with K+ for a binding site on the Na,K-ATPase and a reduction in the number of transporting sites. The site of action of apamin on Na,K-ATPase is different from that of tetra-alkylammonium compounds; it apparently decreases the turnover rate of the enzyme.
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