Mechanism of hemolysis of canine erythrocytes induced by L-sorbose

Ikuo Goto From the Department of Veterinary Internal Medicine, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060 (Goto, Inaba, Maede) and Food Research Group, Foods Division, Asahi Chemical Industry Co Ltd, Fuji 416 (Shimizu), Japan.

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Mutsumi Inaba From the Department of Veterinary Internal Medicine, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060 (Goto, Inaba, Maede) and Food Research Group, Foods Division, Asahi Chemical Industry Co Ltd, Fuji 416 (Shimizu), Japan.

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Toshio Shimizu From the Department of Veterinary Internal Medicine, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060 (Goto, Inaba, Maede) and Food Research Group, Foods Division, Asahi Chemical Industry Co Ltd, Fuji 416 (Shimizu), Japan.

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Yoshimitsu Maede From the Department of Veterinary Internal Medicine, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060 (Goto, Inaba, Maede) and Food Research Group, Foods Division, Asahi Chemical Industry Co Ltd, Fuji 416 (Shimizu), Japan.

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Summary

The cause of species difference in the susceptibility of erythrocytes to L-sorbose, and the difference in the hemolytic effect of sorbose on high potassium-containing (hk) and low potassium-containing (lk) canine erythrocytes were examined. L-Sorbose was phosphorylated in canine erythrocytes, but not in human erythrocytes. Furthermore, sorbose-1-phosphate, a metabolite of L-sorbose, strongly inhibited the hexokinase of lk canine erythrocytes, but not that of hk canine erythrocytes. These results strongly indicated that inhibition of hexokinase by sorbose-1-phosphate in lk erythrocytes induced severe glycolytic limitation in these cells, resulting in hemolysis, and that hk erythrocytes are resistant to sorbose-induced hemolysis because these cells have a high hexokinase activity.

Summary

The cause of species difference in the susceptibility of erythrocytes to L-sorbose, and the difference in the hemolytic effect of sorbose on high potassium-containing (hk) and low potassium-containing (lk) canine erythrocytes were examined. L-Sorbose was phosphorylated in canine erythrocytes, but not in human erythrocytes. Furthermore, sorbose-1-phosphate, a metabolite of L-sorbose, strongly inhibited the hexokinase of lk canine erythrocytes, but not that of hk canine erythrocytes. These results strongly indicated that inhibition of hexokinase by sorbose-1-phosphate in lk erythrocytes induced severe glycolytic limitation in these cells, resulting in hemolysis, and that hk erythrocytes are resistant to sorbose-induced hemolysis because these cells have a high hexokinase activity.

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