AbstractMg2+-loaded rat erythrocytes performed Mn+/Mg2+ antiport, which was nonspecifically stimulated by anions and cations. Mn2+/Mg2+ antiport was shown to operate via the Na+Mg2+ antiporter because extracellular Na+ and Mn2+ inhibited the intracellular uptake of each other's ions competitively. Furthermore, Mn2+/Mg2+ antiport and Na+/Mg2+ antiport were identically inhibited by various amiloride derivatives. Na+/Mg2+ antiport of chicken and human erythrocytes cannot perform Mn2+/Mg2+ antiport although chicken erythrocytes took up more Mn2+ than raterythrocytes
TRPM7 channels are nonselective cation channels that possess a functional α-kinase domain. It has be...
AbstractTRPM7 channels are nonselective cation channels that possess a functional α-kinase domain. I...
AbstractManganese uptake by human erythrocytes was investigated in the concentration range 0.5–20 mM...
AbstractMg2+-loaded rat erythrocytes performed Mn+/Mg2+ antiport, which was nonspecifically stimulat...
AbstractRat erythrocytes loaded with Mg2+ plus Na+ performed Mg2+ uptake under an intracellular/extr...
AbstractChicken erythrocytes preloaded with Mg2+ exchange one extracellular Mn2+ fo two intracellula...
AbstractIn rat erythrocytes, the regulation of Na+/Mg2+ antiport by protein kinases (PKs), protein p...
AbstractMg2+ efflux from rat erythrocytes was measured in NaCl, NaNO3, NaSCN and Na gluconate medium...
AbstractNa+-independent Mg2+ efflux from Mg2+-loaded human, rat and chicken erythrocytes was reduced...
AbstractNon-Mg2+-loaded rat erythrocytes with a physiological level of Mg2+i exhibited Mg2+ efflux w...
AbstractRabbit erythroid cells can take up non-transferrin-bound iron by a high-affinity and a low-a...
AbstractNet Mg2+ efflux from Mg2+-loaded human, rat and chicken erythrocytes was measured in sucrose...
AbstractEvidence was presented previously that rabbit erythroid cells possess a low-affinity Fe2+ tr...
AbstractTwo types of Na+-independent Mg2+ efflux exist in erythrocytes: (1) Mg2+ efflux in sucrose m...
AbstractMg2+ efflux from Mg2+-loaded rat thymocytes was stimulated by 0.1 mM dibutyryl cAMP (db cAMP...
TRPM7 channels are nonselective cation channels that possess a functional α-kinase domain. It has be...
AbstractTRPM7 channels are nonselective cation channels that possess a functional α-kinase domain. I...
AbstractManganese uptake by human erythrocytes was investigated in the concentration range 0.5–20 mM...
AbstractMg2+-loaded rat erythrocytes performed Mn+/Mg2+ antiport, which was nonspecifically stimulat...
AbstractRat erythrocytes loaded with Mg2+ plus Na+ performed Mg2+ uptake under an intracellular/extr...
AbstractChicken erythrocytes preloaded with Mg2+ exchange one extracellular Mn2+ fo two intracellula...
AbstractIn rat erythrocytes, the regulation of Na+/Mg2+ antiport by protein kinases (PKs), protein p...
AbstractMg2+ efflux from rat erythrocytes was measured in NaCl, NaNO3, NaSCN and Na gluconate medium...
AbstractNa+-independent Mg2+ efflux from Mg2+-loaded human, rat and chicken erythrocytes was reduced...
AbstractNon-Mg2+-loaded rat erythrocytes with a physiological level of Mg2+i exhibited Mg2+ efflux w...
AbstractRabbit erythroid cells can take up non-transferrin-bound iron by a high-affinity and a low-a...
AbstractNet Mg2+ efflux from Mg2+-loaded human, rat and chicken erythrocytes was measured in sucrose...
AbstractEvidence was presented previously that rabbit erythroid cells possess a low-affinity Fe2+ tr...
AbstractTwo types of Na+-independent Mg2+ efflux exist in erythrocytes: (1) Mg2+ efflux in sucrose m...
AbstractMg2+ efflux from Mg2+-loaded rat thymocytes was stimulated by 0.1 mM dibutyryl cAMP (db cAMP...
TRPM7 channels are nonselective cation channels that possess a functional α-kinase domain. It has be...
AbstractTRPM7 channels are nonselective cation channels that possess a functional α-kinase domain. I...
AbstractManganese uptake by human erythrocytes was investigated in the concentration range 0.5–20 mM...