Specific 5-HT2A receptor blockade with sarpogrelate immediately after MCT inhibited PAH and prolongs survival in rats. These effects were accompanied by anti-inflammatory and anti-proliferative effects in the lung tissue and marked improvement of pulmonary vascular endothelial dysfunction and activation.
We have, by using newly developed ratemeters, attempted to examine the effects of exercise intensity, posture, pressure on the skin of the back, and ambient hyperthermic conditions (~30 °C) on the 5-s handgrip exercise-mediated responses of active palmar sweating in humans.Thirty-five right-handed male (n=5) and female (n=30) important that subjects maintain a constant handgrip force and posture and that ambient temperature be kept under normothermic conditions. 4
To analyze both hemoglobin (Hb) and globin chain variants, we modified a commonly used method, capillary isoelectric focusing (CIEF), with detection at 280 nm. The samples were hemolysates prepared from red blood cells, and globin chains obtained from the hemolysates by treatment with cold acidified acetone. When the migration time for the internal reference, carbonic anhydrase I (isoelectric point, pI 6.60), was taken as 1.0, the migration ratio for Hb A0 in normal human blood was 0.877 +/- 0.004 (mean +/- SD, n = 9), and those of the alpha- and beta-globin chains were 0.673 +/- 0.004 and 0.847 +/- 0.005 (mean +/- SD, n = 4), respectively. The ratio of peak heights between the beta- and alpha-globin chains (beta/alpha) in the normal Hbs obtained from four subjects was almost constant at 2.5 +/- 0.1 (mean +/- SD). This ratio indicates which of the globin chains includes a mutation (if one exists). When an Hb variant, Hb Hoshida (in which Gln is substituted for Glu at residue 43 in the beta-globin chain), was analyzed by this method, two main peaks were observed (migration ratios 0.836 and 0.877, corresponding to an abnormal and the normal Hb, respectively). An additional peak with an abnormal migration ratio of 0.788 was also detected in the globin chain profiles. The ratio of peak heights between normal beta- and alpha-globin chains was 1.57, indicating that a mutation exists in the beta-globin chain. We thus established a convenient system using CIEF that provides a rapid and reproducible method for the random analysis of both Hb and globin chain variants.
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