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PubMedDate not supplied

[Histophysiological characteristics of the structures of the subcommissural organ of the brain and the glomerular zone of the adrenal gland in changes of the water-electrolyte balance].

Experiments were conducted on 45 male rats; histophysiological characteristics of ependymocytes of the subcommissural organ (SCO) and of adrencorticocytes of the glomerular zone of the adrenal cortex (GZA) was investigated under conditions of dehydration and water loading. A marked activation of H-6-PDH, HDH, NAD-dependent alphaHPDH, and an enhancement of the H-6-PDH, NAD-diaphorase and 3betaol activity in the GZA adrencorticocytes resulted from dehydration. Water loading depressed the synthetic processes, particularly in the SCO ependymocytes. The data obtained suggest a functional interrelation between the SCO and GZA.

Adrenal Cortex↗
PubMed1978

[Enzymes of the outer segments of the retinal rods: The problem of localization and coupling with rhodopsin].

The problem of the presence of enzymes in retina rod outer segments is summarized using both literature and the author's own data. Difficulties in the solving of this problem are analyzed. It has been shown that some enzymes involved in the primary mechanisms of the photoreceptor process are localized in the inner segment of the photoreceptor cell at a distance from the photoreceptor membranes. A conclusion is drawn that the enzymes necessary for rhodopsin (or its retinal-part) conversions as well as those ensuring synthesis and decay of cyclic nucleotides are concentrated in the outer segments. These data served as a ground for a conclusion about a strictly "biochemial" specialization of particular parts of the photoreceptor cell in which tightly linked chemical transformations proceed in different compartments. Besides, some unusual properties of the plasma membrane of the photoreceptor cell are noticed, in particular, the absence in part of this membrane of some typical marking enzymes. The interrelations between rhodopsin and enzymes as well as a possible participation of Ca-ions in this process are examined. It is supposed that one part of the rhodopsin molecule may act as a Ca2+ binding protein.

Adenosine Triphosphatases↗
PubMed1995

Impaired activation of glucose oxidation and NADPH supply in human endothelial cells exposed to H2O2 in high-glucose medium.

The effects of glucose concentration on D-glucose oxidation and reduced nicotinamide adenine dinucleotide phosphate (NADPH) supply were studied during exposure of cultured human umbilical vein endothelial cells to hydrogen peroxide (H2O2). The activation of glucose oxidation via the pentose phosphate pathway (PPP), induced by exposure of cells to 200 mumol/l H2O2 for 1 h, was reduced by 50% (P < 0.01) in cells cultured for 5-7 days in 33 mmol/l D-glucose (HG) versus those cultured in 5.5 mmol/l D-glucose without (NG) or with (HR) 27.5 mmol/l D-raffinose. The intracellular NADPH content in HG cells, but not in NG or HR cells, was decreased by 42% (P < 0.01) by exposing cells to 200 mumol/l H2O2. The decrease in NADPH was dependent on D-glucose concentration in the medium and was prevented in glutathione (GSH)-depleted cells. The latter observation suggests that the decrease in NADPH is associated with activation of the GSH redox cycle. In the presence of 200 mumol/l H2O2, lactate release into the medium, NADH/NAD ratio, and phosphofructokinase activity in HG cells were 56, 53, and 68% greater, respectively, than in the NG group, which indicates that inhibition of glycolysis by H2O2 is less marked in the HG group compared with NG group. These results indicate that activation of the PPP was impaired in endothelial cells cultured under conditions of high-glucose and oxidative stress, resulting in a decreased supply of NADPH to various NADPH-dependent pathways, including the GSH redox cycle.

Adenosine Triphosphate↗
PubMed1980

Short-term action of streptozotocin on biochemical activity and morphology of the rat liver golgi apparatus.

After six hours, the diabetogenic dose of streptozotocin has neither induced the release of hepatocyte cytoplasmic enzyme nor visibly injured the hepatocyte. As a rule, however, these doses of streptozotocin induced various responses in individual rat livers. Morphological studies have shown hypertrophy of the rat liver Golgi apparatus, higher numbers of secretory vacuoles and dilated cisternae. After this time liver Golgi-rich fractions revealed increased total liver galactosyl transferase activity and higher level but unaltered electrophoretical patterns of protein.

Alanine↗