[Antioxidant activity of blood plasma of mountain Altai's aborigines Russian and Kazakh nationality of low and medium height altitude areas].

Due to the points about dependence antioxidant activity of organism of human on a nationality, climatic conditions, quality of nutrition are scanty under study a estimate antioxidant activity of blood plasma of Altai's low and medium height altitude aborigines. As a result there has been discovered a dependence of antioxidant activity of blood plasma more upon age and at least geographical and climatic conditions, sex and quality of nutrition.

[Characteristics of the K(+)-ion transport in the rat intestine following the use of natural zeolites as food additives]. / Osobennosti transporta ionov K(+) v kishechnike krys pri ispol'zovanii prirodnykh tseolitov v kachestve pishchevoi dobavki.

Effects of zeolites as a food supplement have been studied on Wistar rats both in vivo perfusion experiments in the jejunum and distal colon and Rb fluxes through intestinal wall in the Ussing chamber. It has been found that zeolites decrease the K+ absorption and stimulate K+ secretion in the gut. This effect was due to inhibition of the apical N(+)-K(+)-ATPase and ouabain-sensitive Na(+)-independent K(+)-ATPase as well as the activation of the basolateral N(+)-K(+)-ATPase.

Regulation of K+ transport in the rat distal colon via angiotensin II subtype receptors and K+ -pathways.

The role of angiotensin subtype-1 (AT1) and -2 (AT2) receptors in mediating the effects of angiotensin II (ANG II) on several K+ transporters was studied in rat distal colon using an Ussing chamber. Angiotensin II induced K+ secretion at two different doses. Secretion occurred at 10-(8) and 10-(4) M, as a result of an increase in serosal-to-mucosal flux (Js-m). The ANG II-induced stimulation of Js-m at a low dose (10-(8) M) was abolished by PD123319 while losartan did not alter the low-dose ANG II-dependent increase in Js-m. In contrast, the increase in Js-m induced by a high-dose of ANG II (10-(4) M) was blocked by losartan, whereas PD123319 partially reduced the stimulatory effect. In the presence of both blockers, high-dose ANG II induced an inhibition of basal Js-m. Low-dose ANG II activated the barium-sensitive K+ channels, whereas the Na+, K+, 2Cl- cotransporter and the Na+, K+ -ATPase pump were unchanged. At the high dose, ANG II activated the barium-sensitive K+ channels and the Na+, K+, 2Cl- cotransporter and inhibited the Na+, K+ -ATPase pump. These data indicate that ANG II stimulates serosal-to-mucosal K+ flux in the rat distal colon at high and low doses via different receptors and K+ transporters.

[Age characteristics of K(+) transport in the rat distal colon]. / Vozrastnye osobennosti transporta K(+) v distal'nom otdele tolstogo kishechnika krys.

In vitro and in vivo experiments with perfusion in 20- and 60-day old rats revealed that K+ absorption in the gut as well as 86Rb uptake in the distal colon was significantly higher in younger rats due probable, to the higher activity of the apex-located K+-dependent ATPase and lower activity of the basolateral K+-carriers. The luminal blockade of K+ absorbing pumps with ouabain or omeprazole resulted in a decrease of the K+ absorption and K2 accumulation in skeletal muscles. The higher K+-absorbing/K_ secreting mechanisms ratio in younger rats contributes to the positive potassium balance.

Beta-adrenergic stimulation of cellular K+ uptake in rat distal colon.

We recently demonstrated that the ratio between colonic K+ absorptive and K+ secretive pathways was higher in infant than in adult rats. To test the hypothesis that hormones selectively affect these pathways during ontogeny we examined the effect of adrenergic agonists on cellular K+ uptake in distal colon from infant (10-day-old) and adult (50-day-old) rats. Here we describe that adrenaline (10(-5) M) increased total and ouabain-insensitive 86Rb uptake in both age groups, but it did not affect ouabain-sensitive 86Rb uptake. This stimulation was more pronounced in adult than in infant rats. The effect of adrenaline was mediated via beta-adrenergic receptors. Incubation in vitro with beta-agonist, isoproterenol, stimulated SCH-28080-sensitive, i.e. H+, K(+)-ATPase-dependent, 86Rb uptake in adult but not in infant rats. The threshold dose of beta-agonist was at 10(-7) M, and the maximal activation was observed at 10(-5) M. In vivo inhibition of beta-adrenergic system with propranolol caused a significant decrease in H+, K(+)-ATPase-dependent 86Rb uptake in infant but not in adult colon. In conclusion, this study suggests that the higher colonic K+ absorption in infant rats may be as a result of a selective beta-adrenergic up-regulation leading to stimulation of the apical H+, K(+)-ATPase.

PKA-mediated phosphorylation and inhibition of Na(+)-K(+)-ATPase in response to beta-adrenergic hormone.

The activity of Na(+)-K(+)-ATPase can be regulated by hormones that activate adenosine 3',5'-cyclic monophosphate-dependent protein kinase (PKA). Here, using a site-directed phosphorylation state-specific antibody, we show that hormonal regulation of Na(+)-K(+)-ATPase can occur via phosphorylation of Ser-943 on its alpha-subunit. cDNAs coding for wild-type rat Na(+)-K(+)-ATPase and Na(+)-K(+)-ATPase in which the PKA phosphorylation site Ser-943 was mutated to Ala were stably and transiently transfected into COS cells. In COS cells expressing wild-type Na(+)-K(+)-ATPase the beta-adrenergic agonist isoproterenol (1 microM) significantly increased the level of phosphorylation of the alpha-subunit. Phosphorylation was accompanied by a significant inhibition of the enzyme activity, as reflected by a decrease in ATP hydrolysis and 86Rb+ transport. The effect of isoproterenol was reproduced by the PKA activator forskolin used in combination with the phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine and was abolished by the specific PKA inhibitor H-89. Okadaic acid, an inhibitor of protein phosphatases 1 and 2A, enhanced phosphorylation and inhibition of Na(+)-K(+)-ATPase induced by isoproterenol. The changes in activity of Na(+)-K(+)-ATPase linearly correlated with the extent of the alpha-subunit of Na(+)-K(+)-ATPase being phosphorylated. When Ser-943 was replaced by alanine, stimulation of the phosphorylation and inhibition of the activity of Na(+)-K(+)-ATPase induced by isoproterenol, alone or in combination with okadaic acid, were not observed. These results indicate that, in intact cells, modulation of the activity of Na(+)-K(+)-ATPase can be achieved by regulation of the state of phosphorylation of Ser-943. Moreover, they provide a biochemical mechanism by which beta-adrenergic agonists can regulate Na(+)-K(+)-ATPase activity.

Glucocorticoids stimulate the maturation of H,K-ATPase in the infant rat stomach.

The development of gastric H,K-ATPase from fetal to adult life was studied in the rat. The alpha and beta H,K-ATPase mRNA abundance, the protein abundance, and the enzyme activity increased postnatally. The sharpest increase in mRNA and enzyme activity was observed in the weaning period. Several intestinal enzymes are known to be stimulated by glucocorticoids at the time of weaning. To study the role of glucocorticoids in the maturation of gastric H,K-ATPase, we treated 10-d-old rats with a single injection of betamethasone. Twenty-four hours after betamethasone injection, the enzyme activity was significantly higher than in the control animals (2.6-fold, p < 0.05). The abundance of catalytic alpha H,K-ATPase protein was also increased (2.5-fold, p < 0.01). The time-dependent effect of betamethasone on alpha H,K-ATPase mRNA was determined from 6 to 24 h after treatment. Glucocorticoids did not significantly alter the mRNA abundance within 18 h. Twenty-four hours after injection, the gastric H,K-ATPase mRNA was significantly increased compared with controls (2.8- and 2.2-fold increase for alpha and beta subunits, respectively, P < 0.01 for both). In conclusion this study indicates that glucocorticoids may regulate the long-term maturation of gastric H,K-ATPase by indirectly stimulating enzyme synthesis.

Ontogeny of K+ transport in rat distal colon.

Infants need to retain more K+ than adults to avoid growth retardation. Since the K+ requirements are different in infants (I) and in adults (A), the mechanisms regulating K+ homeostasis should also be different. The colon plays an important role for the regulation of K+ homeostasis. Colonic K+ transport is bidirectional. In this study we have examined the development of colonic K+ transport with special reference to the contribution of different K(+)-transporting pathways. The net colonic K+ uptake, as determined by in vivo perfusion studies and by 86Rb uptake, was significantly higher in I than in A rats. In both I and A colon, approximately 80% of total 86Rb uptake was dependent on vanadate-sensitive P-type adenosinetriphosphatases (ATPases), but the contribution of these different ATPases changes during development. The activity of colonic Na(+)-K(+)-ATPase, measured as ouabain-sensitive Na(+)-dependent ATP hydrolysis and as 86Rb uptake, was lower in I than in A rats. In contrast, the activity of K(+)-ATPases located in apical membrane and measured as ouabain insensitive and SCH-28080 sensitive, as ouabain-sensitive Na(+)-independent ATP hydrolysis, and as 86Rb uptake was significantly higher in I than in A rats. The ratio between apically located K(+)-ATPases and basolateral Na(+)-K(+)-ATPase activities was almost 3.2-fold higher in I than in A colon. We identified with Northern blot the expression of the colonic H(+)-K(+)-ATPase and the Na(+)-K(+)-ATPase alpha-subunits. The alpha-mRNA expression of both ATPases was significantly higher in I than in A rats. The pH and K+ sensitivity of the ouabain-insensitive, SCH-28080-sensitive K(+)-ATPase was the same in I and A colons. In conclusion, the relative activity of apical K+ absorbing ATPases is higher in the I than in the A colon, which should aid infants in retaining K+.