The special behavior of equine erythrocytes connected with the methemoglobin regulation.
Erythrocytes from thoroughbred horses were submitted to total (80-90%) and partial (25-40%) oxidation of hemoglobin by sodium nitrite. The ability of these cells to reduce methemoglobin to hemoglobin in the presence of either glucose, glucose plus methylene blue or lactate was investigated. The results were compared with those ones obtained for human erythrocytes. Under total oxidation: the horse erythrocytes need longer incubation time with glucose or glucose plus methylene blue than human erythrocytes for reducing the methemoglobin; methylene blue did not enhance methemoglobin reduction in the equine erythrocytes, as occurred in human erythrocytes; for horses, lactate was a more efficient substrate in promoting methemoglobin reduction. The reduction of methemoglobin by equine erythrocytes under partial oxidation was very quick in any of the incubation media. The results can explain the incongruity between the previously reported inability of equine erythrocytes to reduce methemoglobin and the lack of methemoglobinemias in equine veterinary practice.
D000818:Animals; D042966:Cytochrome-B(5) Reductase / Q000097:blood; D004912:Erythrocytes / Q000502:physiology*; D005954:Glucosephosphate Dehydrogenase / Q000097:blood; D005978:Glutathione / Q000097:blood; D005980:Glutathione Reductase / Q000097:blood; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000097:blood; D006736:Horses / Q000097:blood*; D006801:Humans; D007770:L-Lactate Dehydrogenase / Q000097:blood; D008706:Methemoglobin / Q000378:metabolism*; D009249:NADP / Q000378:metabolism; D010734:Phosphogluconate Dehydrogenase / Q000097:blood
D009249:NADP; D008706:Methemoglobin; D007770:L-Lactate Dehydrogenase; D010734:Phosphogluconate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D042966:Cytochrome-B(5) Reductase; D005980:Glutathione Reductase; D005978:Glutathione