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Biomedical subjects

Y Maede

Publications and source records attributed to Y Maede.

At least 91 records · Page 5Linked to original sources

Increase of Na+ gradient-dependent L-glutamate and L-aspartate transport in high K+ dog erythrocytes associated with high activity of (Na+, K+)-ATPase.

As reported previously, some dogs possess red cells characterized by low Na+, high K+ concentrations, and high activity of (Na+, K+)-ATPase, although normal dog red cells contain low K+, high Na+, and lack (Na+, K+)-ATPase. Furthermore, these red cells show increased activities of L-glutamate and L-aspartate transport, resulting in high accumulations of such amino acids in their cells. The present study demonstrated: (i) Na+ gradient-dependent L-glutamate and L-aspartate transport in the high K+ and low K+ red cells were dominated by a saturable component obeying Michaelis-Menten kinetics. Although no difference of the Km values was observed between the high K+ and low K+ cells, the Vmax values for both amino acids' transport in the high K+ cells were about three times those of low ones. (ii) L- and D-aspartate, but not D-glutamate, competitively inhibited L-glutamate transport in both types of the cells. (iii) Ouabain decreased the uptake of the amino acids in the high K+ dog red cells, whereas it was not effective on those in the low K+ cells. (iv) The ATP-treated high K+ cells [(K+]i not equal to [K+]o, [Na+]i greater than [Na+]o) showed a marked decrease of both amino acids' uptake rate, which was almost the same as that of the low K+ cells. (v) Valinomycin stimulated the amino acids' transport in both of the high K+ and the ATP-treated low K+ cells [( K+]i greater than [K+]o, [Na+]o), suggesting that the transport system of L-glutamate and L-aspartate in both types of the cells might be electrogenic. These results indicate that the increased transport activity in the high K+ dog red cells was a secondary consequence of the Na+ concentration gradient created by (Na+, K+)-ATPase.

Animals↗

Serum concentration and properties of alpha-fetoprotein and serum level of albumin in sucking piglets.

Porcine alpha-fetoprotein (AFP) was purified from the sera of four-day-old piglets using an immunoadsorbent column. The molecular weight of the AFP was 80,000 when determined by gel filtration on Sephadex G-200 and 75,000 when determined by sodium dodecylsulphate polyacrylamide gel electrophoresis. The isoelectric point of the AFP was pH 4.85 at 0 degree C. The maximum concentration of serum AFP was reached on the fourth day after birth (mean value 1.1 mg ml-1), and it then decreased to 10 micrograms ml-1 when the piglets were 35 days old. The concentration of serum albumin increased rapidly between birth and seven days old, reaching 16 to 17 mg ml-1 at seven days old. Between birth and seven days old, the serum concentrations of AFP and albumin were approximately inversely proportional.

Animals↗

Increase of Na-K-ATPase activity, glutamate, and aspartate uptake in dog erythrocytes associated with hereditary high accumulation of GSH, glutamate, glutamine, and aspartate.

We have found convincing evidence for the presence of Na-K-ATPase and high potassium (K) and low sodium (Na) concentrations in the erythrocytes of some dogs associated with hereditary high concentrations of erythrocyte glutathione and some amino acids, glutamate, glutamine, and aspartate. The Na-K-ATPase activity of the erythrocyte membranes of the dogs was about 3 times that of human erythrocyte membranes, whereas the enzyme activity was not detected in control dogs with a normal level of blood glutathione. The Michaelis constant of the enzyme for ATP (Km ATP) was 6.6 X 10(-3)M in the dogs' erythrocytes and 5.0 X 10(-4)M in the human erythrocytes. The concentration of K in the erythrocytes in the dogs examined was about 11 times that of the controls, whereas the erythrocyte Na concentration in the dogs was about one-third that of the controls. The concentrations of K and Na in the plasma of the dogs were equal to those of the controls. Furthermore, L-3H-glutamate and L-3H-aspartate uptake by those cells with high activity of Na-K-ATPase greatly increased, while L-3H-glutamine uptake was unchanged. It appeared that Na+ and K+ gradients created by Na-K-ATPase across the cell membrane might stimulate glutamate and aspartate uptake by the cells, thus causing the high accumulation of such amino acids in the cells.

Amino Acid Metabolism, Inborn Errors↗

Hereditary high concentration of glutathione in canine erythrocytes associated with high accumulation of glutamate, glutamine, and aspartate.

We have found a dog family in which there were five cases of increased red cell glutathione corresponding to four to five times the normal concentration without any clinical signs. In the present study, we mainly examined the concentrations of free amino acids in the erythrocytes, plasma, and urine of two of the dogs, and we demonstrated that the concentrations of glutamate, aspartate, and glutamine in their erythrocytes increases to 92, 63, and 13 times the mean value in the normal blood, respectively. There were no changes observed in the other amino acids as compared to normal, although the glycine and histidine in the erythrocyte showed slight increases. The concentrations of amino acids in the plasma and urine of the dogs were almost equal to normal ones. The activities of some of the enzymes involved in the glutathione metabolism in the erythrocytes from the two dogs were all within the normal range. The increased level of glutathione could be explained by the fact that the feedback inhibition of gamma-glutamyl cysteine synthetase by glutathione was released by the high levels of glutamate in the erythrocytes.

Amino Acids↗

Sequestration and phagocytosis of Haemobartonella felis in the spleen.

Spleens of two cats infected with Haemobartonella felis were examined by electron microscopy to determine the means by which the organism was sequestered in this organ. The principal means of sequestration occurred when H felis, located on the erythrocytes was removed by phagocytosis by a cordal macrophage, apparently preceded by the adhesion of extended processes of the macrophage to H felis. The second and least frequent means of removal of H felis was by pitting, a process that did not cause destruction of the host erythrocyte. The H felis was pitted from the parasitized erythrocyte when H felis passed through gaps between reticular cells or when the parasitized erythrocyte passed among the cytoplasmic processes of the reticular cells in the splenic cords. Some H felis were closely associated with the plasmalemma of cordal reticular cells and also were located in intracytoplasmic vacuoles of the cells without being influenced by the phagocytic process.

Anaplasmataceae↗