Effect of carbohydrate load on the structuro-functional organization of cell membranes in patients with hypertension

Carbohydrate load induces in patients with essential hypertension reduction of the phospholipid fraction in the system blood plasma--surface-deep phospholipid pool of erythrocytic membranes, and the lowering of the levels of polyenic and dienic fatty acids.     

Non-isothermal Kinetics of Benzo[a]Pyrene Photooxidation in Glyceryl Trioctanoate

Benzo[a]pyrene (BaP) was dissolved in glyceryl trioctanoate, heated in a glass reaction vessel within temperature range 297.95–361.85 K with heating rate of 1 K/min and simultaneously exposed to UV light at wavelength λ = 365 nm at radiation power 20 mW cm^?2 in order to study the decrease of BaP concentration due to its photooxidation. The concentration of BaP was determined by HPLC-FD periodically in 5 min intervals. As observed, the BaP concentration decreased from 62.2 μg L^-1 to 19.8 μg L^-1. From the experimental results, the parameters characterizing the non-isothermal kinetics of BaP photooxidation have been obtained. The parameters were tested at two various isothermal conditions (290.16 and 323.26 K) to verify a suitability of derived parameters. Comparing calculated and measured data of half-lives of BaP decrease at mentioned temperatures it was found that calculated half-lives are in a good accordance with those experimentally obtained values, when relative standard deviations at 290.16 K were 17.0% and 5.4% at 323.26 K, respectively. The kinetic parameters enable the calculation of the rate constant for any temperature in isothermal regime and make possible to model, in general, the kinetics of such processes without a deeper insight into their mechanisms.     

Endaural reflex diagnosis of cochleovestibular dysfunctions in patients with vascular brain diseases

Results obtained prove that respiration stimulation of mitochondria Ca2+, Sr2+, Mn2+ is determined by transport of these cations to the indicated subcellular structures with participation of Ca2(+)-uniporter. Effect of Cd2+ on respiration of mitochondria is of two-phase character. Concentration of Cd2+ being above 100 microM the stimulation phase is accompanied by the further inhibition of mitochondria respiration. La3+ inhibits respiration of mitochondria. However La3+ and Cd2+ stimulate H+ production by mitochondria, that is not blocked by ruthenium red (10 microM). Probably, the effect of La3+ and Cd2+ on respiration of mitochondria is determined by the change of proton conductivity of mitochondrion membrane. Direct inhibiting effect of Cd2+ on the respiration chain of mitochondria has been established.     

The Effects of Endogenous Non-Peptide Molecule Isatin and Hydrogen Peroxide on Proteomic Profiling of Rat Brain Amyloid-β Binding Proteins: Relevance to Alzheimer’s Disease?

The amyloid-β peptide is considered as a key player in the development and progression of Alzheimer’s disease (AD). Although good evidence exists that amyloid-β accumulates inside cells, intracellular brain amyloid-binding proteins remain poorly characterized. Proteomic profiling of rat brain homogenates, performed in this study, resulted in identification of 89 individual intracellular amyloid-binding proteins, and approximately 25% of them were proteins that we had previously identified as specifically binding to isatin, an endogenous neuroprotector molecule. A significant proportion of the amyloid-binding proteins (more than 30%) are differentially expressed or altered/oxidatively modified in AD patients. Incubation of brain homogenates with 70 µM hydrogen peroxide significantly influenced the profile of amyloid-β binding proteins and 0.1 mM isatin decreased the number of identified amyloid-β binding proteins both in control and hydrogen peroxide treated brain homogenates. The effects of hydrogen peroxide and isatin have been confirmed in optical biosensor experiments with purified glyceraldehyde-3-phosphate dehydrogenase, one of the known crucial amyloid-β binding proteins (also identified in this study). Data obtained suggest that isatin protects crucial intracellular protein targets against amyloid binding, and possibly favors intracellular degradation of this protein via preventing formation of amyloid-β oligomers described in the literature for some isatin derivatives.