Phosphorylation of the red blood cell membrane during the active transport of C++.

Nam, Young Ran; Lee, Kwang Soo

doi:10.1085/jgp.67.2.251

Cited by 11 publications

(4 citation statements)

References 17 publications

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“…This agreed with the finding that a sulfhydryl inhibitor structurally similar to NEM, diamide, locks Na ϩ / Ca ϩϩ exchange in dog erythrocytes in an "on" conformation (Parker, 1986). NEM also blocks dephosphorylation of Ca ϩϩ -ATPase, indicating that the pump is unable to turn off (Cha and Lee, 1976). Therefore, when AsH 3 is present, NEM offers its hemolytic protection to erythrocytes by facilitating Ca ϩϩ efflux.…”

Section: Discussionsupporting

confidence: 87%

“…The effect of NEM on Mg ϩϩ transport seems to be inhibitory although there is very limited data to support this finding. There is some evidence that NEM inhibits Ca ϩϩ ,Mg ϩϩ -ATPase (Cameron and Smariga, 1981;Cha and Lee, 1976) supporting the finding that NEM decreases intracellular Mg ϩϩ concentrations. NEM was ineffective in preventing AsH 3 -induced increase in intracellular Clconcentration.…”

Section: Discussionmentioning

confidence: 81%

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The Effects of Sulfur, Thiol, and Thiol Inhibitor Compounds on Arsine-Induced Toxicity in the Human Erythrocyte Membrane

Rael

2000

Toxicological Sciences

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The mechanism of arsine (AsH(3)) toxicity is not completely understood. The first cytotoxic effect of AsH(3) is disruption of ion homeostasis, with a subsequent hemolytic action. The only accepted treatment for AsH(3) toxicity is exchange transfusion of the blood. In this study the effect of sulfur, sulfur compounds, thiol-containing compounds, and thiol inhibitors on AsH(3)-induced disruption of membrane transport and hemolysis in human erythrocytes was investigated in vitro. Elemental sulfur, sodium thiosulfate, 5, 5'-dithio-bis(2-nitrobenzoic acid), and meso-2,3-dimercaptosuccinic acid were successful in delaying hemolysis, but the most successful agent was the sulfhydryl inhibitor, N-ethylmaleimide (NEM). This indicated that sulfhydryl groups, possibly membrane sulfhydryls, are major factors in the hemolytic mechanism of AsH(3). Measuring intracellular ion concentrations tested the effect of NEM on AsH(3)-induced disruption of membrane transport. AsH(3) alone caused all ions tested to flow with their concentration gradients: Intracellular K+ and Mg++ decreased, whereas Na+, Cl-, and Ca++ increased. NEM was unable to prevent ion loss except for Ca++, whose increase was prevented for 1 h after AsH(3) treatment. The influx of Ca++ in AsH(3)-treated erythrocytes is an irreversible event leading to hemolysis. Reduction of oxygenated hemoglobin to carboxyhemoglobin completely inhibited AsH(3)-induced hemolysis. In addition, AsH(3) and NEM had no direct chemical interactions. We concluded that membrane sulfhydryl groups are likely targets of AsH(3) toxicity, with NEM being able to prevent AsH(3)-induced hemolysis.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionmentioning

confidence: 81%

The Effects of Sulfur, Thiol, and Thiol Inhibitor Compounds on Arsine-Induced Toxicity in the Human Erythrocyte Membrane

Rael

2000

Toxicological Sciences

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“…It has been observed that both calcium and higher levels of magnesium can induce the phosphorylation of erythrocyte membrane proteins by ATP (Knauf, Proverbio & Hoffman, 1974;Rega& Garrahan, 1975;Cha & Lee, 1976) and both types of phosphate bonds are abolished by hydroxylamine. It has also been noted that the phosphoprotein formed in the presence of calcium was dephosphorylated by magnesium (Rega & Garrahan, 1975) while the phosphoprotein formed in the presence of magnesium was dephosphorylated by calcium (Cha & Lee, 1976).…”

Section: Discussionmentioning

confidence: 99%

“…It has also been noted that the phosphoprotein formed in the presence of calcium was dephosphorylated by magnesium (Rega & Garrahan, 1975) while the phosphoprotein formed in the presence of magnesium was dephosphorylated by calcium (Cha & Lee, 1976). One might speculate that the transport of calcium from erythrocyte ghosts may proceed by two mechanisms.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of active strontium transport from erythrocyte ghosts by internal calcium: Evidence for a specificity controlling site

Olson

1979

J. Membrain Biol.

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The inhibition of strontium transport from erythrocyte ghosts by internal calcium was investigated. When active strontium transport was measured in the presence of increasing levels of internal calcium it was found that the inhibition of strontium transport started at an internal calcium level of 0.3 mM and was virtually complete when this concentration reached 1.0 mM. It was also noted that calcium transport was virtually constant between concentrations of 0.3 and 1.0 mM. This experiment indicated that calcium did not inhibit strontium transport by competing for the active site of the transport system. This inhibition was partially reversed by increasing the internal magnesium concentration from 1 to 4 mM. A higher level of magnesium at the time of lysis and during incubation enhanced strontium transport. However, the inhibition remained noncompetitive with respect to calcium. Manganese was also found to support calcium and strontium transport. However, it could not reverse the inhibition of strontium transport by internal calcium at any concentration tested. In fact, manganese restored the inhibition of strontium transport by calcium in ghosts that were prepared and incubated in solutions that had high magnesium levels.

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Phosphorylation of the isolated high-affinity (Ca2+ + Mg2+)-ATPase of the human erythrocyte membrane

Lichtner

Wolf

1980

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Phosphorylation of the red blood cell membrane during the active transport of C++.

Cited by 11 publications

References 17 publications

The Effects of Sulfur, Thiol, and Thiol Inhibitor Compounds on Arsine-Induced Toxicity in the Human Erythrocyte Membrane

The Effects of Sulfur, Thiol, and Thiol Inhibitor Compounds on Arsine-Induced Toxicity in the Human Erythrocyte Membrane

Inhibition of active strontium transport from erythrocyte ghosts by internal calcium: Evidence for a specificity controlling site

Phosphorylation of the isolated high-affinity (Ca2+ + Mg2+)-ATPase of the human erythrocyte membrane

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