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1.
Radiats Biol Radioecol ; 53(6): 592-7, 2013.
Article in Russian | MEDLINE | ID: mdl-25486741

ABSTRACT

The influence of the low-rate ionizing radiation (0.055 Gy/min) at the doses of 0.1; 0.5 and 1.0 Gy on the functional state of the mitochondria respiratory chain of the rat small intestine enterocytes was investigated. The dysfunction of the electron transport chain enzymes and changes in the content of cytochromes b, c, a in the mitochondrial inner membrane were revealed 1, 12 and 24 hours after exposure to radiation. The revealed disorders indicate early membrane sensitivity to the radiation effect. The inhibition of the H+ -ATPase activity in the studied dose range indicates the decrease of the mitochondrial energy capacity.


Subject(s)
Electron Transport/radiation effects , Enterocytes/radiation effects , Mitochondrial Membranes/metabolism , Proton-Translocating ATPases/metabolism , Animals , Dose-Response Relationship, Radiation , Intestine, Small/radiation effects , Male , Mitochondrial Membranes/radiation effects , Oxidation-Reduction , Rats , X-Rays
2.
Radiats Biol Radioecol ; 51(6): 684-8, 2011.
Article in Russian | MEDLINE | ID: mdl-22384718

ABSTRACT

The investigations of the functional state of the antioxidant system in epithelial cells from rat small intestine in dynamics after X-ray irradiation (0.1; 0.5 and 1.0 Gy) at a low absorbed dose rate (55 mGy/min) were performed. The obtained results point out the ambiguity of the antioxidant system reaction to the activation of oxidative processes at different doses of irradiation. The multidirectional changes of these antioxidant enzymatic activities whose functioning is characterized by the early post-irradiation recovery depending on the value of the absorbed dose were observed. The sensitivity of superoxide dismutase, glutathione transferase and glutathione peroxidase in mitochondria of epithelial cells to the irradiation exposure in the investigated range of absorbed doses was shown.


Subject(s)
Catalase/metabolism , Glutathione Peroxidase/metabolism , Glutathione Transferase/metabolism , Intestinal Mucosa/radiation effects , Intestine, Small/radiation effects , Superoxide Dismutase/metabolism , Animals , Catalase/analysis , Dose-Response Relationship, Radiation , Glutathione Peroxidase/analysis , Glutathione Transferase/analysis , Intestinal Mucosa/enzymology , Intestine, Small/cytology , Male , Mitochondria/radiation effects , Radiation, Ionizing , Rats , Superoxide Dismutase/analysis , Whole-Body Irradiation
3.
Radiats Biol Radioecol ; 46(1): 27-33, 2006.
Article in Russian | MEDLINE | ID: mdl-16579541

ABSTRACT

The different ways of the radiation-induced effect were revealed in the investigations of chronic ionizing radiation influence in total doses of 0.3, 0.6 and 1.0 Gy (0.0072 Gy/day) on the structural properties of the apical and of the mitochondrial membranes of small intestine enterocytes. The modification of the physical properties of the membrane surface area, the decrease of the structural order of the lipid component and conformational changes of the proteins were shown to be specific for the apical membrane. The disturbance of the dynamic properties and topography of the internal mitochondria membrane was revealed in the investigation of the inductive-resonance energy transfer between the pairs of the fluorophores: tryptophan-pyrene, tryptophan-ANS, pyrene-ANS.


Subject(s)
Enterocytes/radiation effects , Gamma Rays/adverse effects , Intestine, Small/radiation effects , Intracellular Membranes , Mitochondria/radiation effects , Animals , Cell Membrane/metabolism , Cell Membrane/radiation effects , Cell Membrane/ultrastructure , Energy Transfer/radiation effects , Enterocytes/metabolism , Enterocytes/ultrastructure , Intestine, Small/cytology , Intracellular Membranes/metabolism , Intracellular Membranes/radiation effects , Intracellular Membranes/ultrastructure , Male , Membrane Lipids/metabolism , Membrane Proteins/metabolism , Mitochondria/metabolism , Mitochondria/ultrastructure , Radiation Dosage , Rats , Time Factors
4.
Radiats Biol Radioecol ; 34(2): 265-72, 1994.
Article in Russian | MEDLINE | ID: mdl-8193719

ABSTRACT

A comparative investigation of transmembrane ion currents and caffeine-induced responses of single smooth muscle cells isolated from the circular layer of rat small intestine was carried out by the method of "patch-clamp". No reliable difference in potential-dependent and amplitude-kinetic characteristics of transmembrane ion currents in cells of intact and irradiated with dose of 3 Gy rats was revealed. In cells of irradiated animals external application of caffeine (4 mM) was not accompanied by strong quick-inactivated transient Ca(2+)-dependent potassium current as in control. The results obtained suggest that single whole-body X-ray irradiation with dose of 3 Gy does not lead in 5 days to any reliable alteration of potential-controlled channels of rat small intestine smooth muscle cell plasma membranes causing at the same time the disturbance of Ca-binding function of intracellular pools.


Subject(s)
Caffeine/pharmacology , Muscle, Smooth/drug effects , Muscle, Smooth/radiation effects , Animals , Cell Separation , Jejunum/cytology , Jejunum/drug effects , Jejunum/physiology , Jejunum/radiation effects , Membrane Potentials/drug effects , Membrane Potentials/physiology , Membrane Potentials/radiation effects , Muscle, Smooth/cytology , Muscle, Smooth/physiology , Rats , Whole-Body Irradiation
5.
Radiats Biol Radioecol ; 38(2): 186-90, 1998.
Article in Russian | MEDLINE | ID: mdl-9633620

ABSTRACT

The effect of X-ray radiation in doses of 1.0 and 3.0 Gy (1 day after irradiation) on physical properties of the apical membrane of rat small intestine enterocytes is studied. It is shown that the fluidity of the bulk lipids doesn't change but the fluidity of the boundary lipids increases after irradiation. The data on quenching of the tryptophane fluorescence by pyrene and magnesium ions indicates apparently the irradiation--induced protein aggregation in membrane.


Subject(s)
Cell Membrane/radiation effects , Intestine, Small/cytology , Animals , Cell Membrane/metabolism , Data Interpretation, Statistical , Fluorescence , Intestine, Small/radiation effects , Magnesium/metabolism , Male , Membrane Lipids/metabolism , Membrane Proteins/metabolism , Pyrenes/metabolism , Radiation Dosage , Rats , Tryptophan/metabolism
6.
Radiats Biol Radioecol ; 39(6): 644-7, 1999.
Article in Russian | MEDLINE | ID: mdl-10689432

ABSTRACT

The structural state and transport properties of basolateral membrane of rat small intestine enterocytes after exposure to X-ray irradiation (0.5; 1.0 and 2.0 Gy) were studied. The substantional suppression of the active Ca(2+)-transport process concomitant to versatile changes of the membrane structure involving the surface sites and intramembrane protein-lipid complexes was revealed one day after irradiation. Taking into account the early obtained data on apical membrane functional disorders these results confirm that ionizing radiation in sublethal doses induces the structure-function modification of enterocyte plasma membrane affecting the function of the small intestine epithelial cells.


Subject(s)
Basement Membrane/radiation effects , Intestine, Small/radiation effects , Animals , Basement Membrane/metabolism , Basement Membrane/ultrastructure , Calcium/metabolism , Ion Transport/radiation effects , Male , Rats
7.
Ukr Biokhim Zh (1978) ; 58(1): 79-82, 1986.
Article in Russian | MEDLINE | ID: mdl-2935982

ABSTRACT

The method of dynamic capacity in the model organic phase-water system was used to investigate a possibility of studying the electrical function of Ca2+,Mg2+-ATPase from sarcoplasmic reticulum of the rabbit hind limb skeletal muscles. Decane and decane solution of azolectin were used as an organic phase. It is stated that in the model systems the sarcoplasmic reticulum Ca2+,Mg2+-ATPase did not cause ATP-dependent changes in the boundary Volta potential (delta phi) irrespective of the presence of polyvalent cation chelates in the organic phase. The fragmented sarcoplasmic reticulum is able of realizing Mg-ATP, Ca2+-dependent generation of delta phi only with phospholipids present in the organic phase. It is supposed that generation of delta phi of the fragmented sarcoplasmic reticulum is due to the active transport of calcium ions by the reticulum Ca2+,Mg2+-ATPase.


Subject(s)
Ca(2+) Mg(2+)-ATPase/physiology , Calcium-Transporting ATPases/physiology , Lipids , Muscles/enzymology , Sarcoplasmic Reticulum/enzymology , Water , Animals , Membrane Potentials , Models, Biological , Rabbits
8.
Ukr Biokhim Zh (1978) ; 63(3): 113-7, 1991.
Article in Russian | MEDLINE | ID: mdl-1833869

ABSTRACT

A single X-ray irradiation of the rabbit hindlimbs in a dose of 0.24 C/kg evokes a decrease in fluorescence of the ANS probe bound with membranes of the sarcoplasmatic reticulum as a result of the decrease of binding sites, binding constant as well as the quantum output of the probe. A decrease in fluorescence of tryptophan residues of Ca-ATPase localized in membranes and attenuation of interaction of its SH-group with dithionitrobenzoic acid has been also observed at early postradiation terms (1 and 24 h). The obtained results evidence for structural rearrangements occurring in membranes of the sarcoplasmic reticulum under the effect of ionizing radiation. Changes in conformation of CA-ATPase molecules contribute much to this process.


Subject(s)
Sarcoplasmic Reticulum/radiation effects , Animals , Calcium-Transporting ATPases/metabolism , Cell Membrane/enzymology , Cell Membrane/radiation effects , Rabbits , Sarcoplasmic Reticulum/enzymology , Spectrometry, Fluorescence , Tryptophan/chemistry
9.
Ukr Biokhim Zh (1978) ; 60(5): 25-30, 1988.
Article in Russian | MEDLINE | ID: mdl-2974659

ABSTRACT

It is established that local X-ray irradiation of the rabbit hind limb produces a decrease in Ca2+, Mg2+-ATP-dependent formation of electric potentials difference on the membrane of the sarcoplasmic reticulum (SR). These results agree with the observed decrease in the Ca2+-ATPase activity of SR membranes and increase in their electric conduction after irradiation.


Subject(s)
Calcium-Transporting ATPases/antagonists & inhibitors , Radiation Injuries, Experimental/enzymology , Sarcoplasmic Reticulum/enzymology , Animals , Calcium-Transporting ATPases/radiation effects , Membrane Potentials/radiation effects , Rabbits , Sarcoplasmic Reticulum/physiology , Sarcoplasmic Reticulum/radiation effects , Time Factors
10.
Ukr Biokhim Zh (1978) ; 62(2): 58-63, 1990.
Article in Russian | MEDLINE | ID: mdl-2142349

ABSTRACT

It is established that a decrease in the Ca2(+)-ATPase activity in the sarcoplasmic reticulum membranes 1 and 24 hours after the local X-ray irradiation of rabbit hind limb by a dose of 0.21 Cl/kg is caused mainly by a change in the enzymic microenvironment and a damage of native protein-lipid interactions essential for the functional activity of Ca2(+)-ATPase.


Subject(s)
Calcium-Transporting ATPases/radiation effects , Muscles/radiation effects , Sarcoplasmic Reticulum/radiation effects , Adenosine Triphosphate/metabolism , Animals , Calcium-Transporting ATPases/antagonists & inhibitors , Female , Hot Temperature , Hydrolysis , Kinetics , Male , Muscles/enzymology , Protein Denaturation , Rabbits , Radiation Injuries, Experimental/enzymology , Sarcoplasmic Reticulum/enzymology , Time Factors
11.
Ukr Biokhim Zh (1999) ; 84(1): 45-52, 2012.
Article in Russian | MEDLINE | ID: mdl-22679757

ABSTRACT

The influence of ionizing radiation with low absorbed dose rate (55 mGy x min(-1)) in 1, 12 and 24 hours after irradiation in doses of 0.1; 0.5 and 1.0 Gy on functional state of the electron transfer chain of the rat small intestine mitochondria was investigated by assessment of the oxygen consumption rate. The uncoupling of oxidation and phosphorylation, a decrease of phosphorylation rate and inhibition of ATP hydrolysis reactions were established in mitochondria in dependence on the irradiation dose and time interval after irradiation. The functional peculiarities of the oxidation-phosphorylation coupling sites of the mitochondrial electron transfer chain were detected.


Subject(s)
Electron Transport/radiation effects , Mitochondria/radiation effects , Oxidative Phosphorylation/radiation effects , Oxygen Consumption/radiation effects , 2,4-Dinitrophenol/pharmacology , Adenosine Triphosphate/antagonists & inhibitors , Adenosine Triphosphate/biosynthesis , Animals , Dose-Response Relationship, Radiation , Electron Transport/drug effects , Electron Transport/physiology , Enterocytes/drug effects , Enterocytes/metabolism , Enterocytes/radiation effects , Intestine, Small/drug effects , Intestine, Small/metabolism , Intestine, Small/radiation effects , Kinetics , Male , Mitochondria/drug effects , Mitochondria/metabolism , Oxidation-Reduction/drug effects , Oxidation-Reduction/radiation effects , Oxidative Phosphorylation/drug effects , Oxygen Consumption/drug effects , Radiation, Ionizing , Rats , Uncoupling Agents/pharmacology
14.
Radiobiologiia ; 32(6): 807-14, 1992.
Article in Russian | MEDLINE | ID: mdl-1494647

ABSTRACT

It has been shown that single local X-irradiation (0.21 C/kg) of the rabbit hind limb in the early period of acute radiation injury (1 and 14 h) causes a decrease in saturation of sarcoplasmic reticulum membrane lipids. It is mainly connected with a decreased saturation of the total fraction of phosphatidyl serine, phosphatidyl inositol and phosphatidyl choline. The above changes can increase permeability of the sarcoplasmic reticulum membranes for Ca(2+)-ion after X-irradiation.


Subject(s)
Membrane Lipids/radiation effects , Radiation Injuries, Experimental/metabolism , Sarcoplasmic Reticulum/radiation effects , Acute Disease , Animals , Female , Male , Phosphatidylcholines/radiation effects , Phosphatidylinositols/radiation effects , Phosphatidylserines/radiation effects , Rabbits , Radiation Dosage , Time Factors
15.
Biokhimiia ; 53(9): 1427-32, 1988 Sep.
Article in Russian | MEDLINE | ID: mdl-2974308

ABSTRACT

The Ca2+ permeability of proteoliposomes containing Ca2+-ATPase of sarcoplasmic reticulum and its hydrophobic fragment was investigated, using the method of synthetic penetrant ions and the radioisotopic method. The former method was used to determine the diffusional membrane potential formed by Ca2+ concentration gradient. It was demonstrated that Ca2+-ATPase, whose active center is oriented outside, has and asymmetric conductivity, i. e., it facilitates the rapid efflux of Ca2+ from proteoliposomes. This efflux is stimulated by the membrane potential positive inside. The hydrophobic fragment of Ca2+-ATPase forms a Ca2+-channel with a high conductivity for Ca2+. This channel is responsible for the Ca2+ efflux from sarcoplasmic reticulum.


Subject(s)
Calcium-Transporting ATPases/metabolism , Calcium/metabolism , Muscles/metabolism , Sarcoplasmic Reticulum/metabolism , Animals , Binding Sites , Biological Transport , Membrane Potentials , Muscles/enzymology , Permeability , Proteolipids/metabolism , Rabbits , Sarcoplasmic Reticulum/enzymology
16.
Radiobiologiia ; 28(3): 314-7, 1988.
Article in Russian | MEDLINE | ID: mdl-3399630

ABSTRACT

As early as 1 and 24 h following single local X-irradiation (0.21 C/kg) of rabbit hindlimbs an increase was noted in the permeability of skeletal muscle sarcoplasmic reticulum membranes for Ca2+, K+ and Na+. The effect was maximum 1 h after irradiation and more pronounced for K+ and Na+ than Ca2+.


Subject(s)
Cell Membrane Permeability/radiation effects , Sarcoplasmic Reticulum/radiation effects , Animals , Calcium/pharmacokinetics , Calcium/radiation effects , Female , Male , Membrane Potentials/radiation effects , Potassium/pharmacokinetics , Potassium/radiation effects , Rabbits , Sodium/pharmacokinetics , Sodium/radiation effects , Time Factors
17.
Radiobiologiia ; 30(1): 16-9, 1990.
Article in Russian | MEDLINE | ID: mdl-2138339

ABSTRACT

Early (1 and 24 h) after X-irradiation with a dose of 0.21 C/kg changes occurred in the acceptability of the polypeptide chain parts of sarcoplasmic reticulum Ca-ATPase for the effect of trypsin. The analysis of the results of studying the structural and functional properties of a hydrophobic fragment of this enzyme in the control and after irradiation permitted to define the part of the Ca-ATPase polypeptide chain that provided ion selectivity of the fragment.


Subject(s)
Calcium-Transporting ATPases/radiation effects , Muscles/radiation effects , Sarcoplasmic Reticulum/radiation effects , Amino Acids/analysis , Amino Acids/radiation effects , Animals , Calcium-Transporting ATPases/analysis , Female , Male , Muscles/drug effects , Muscles/enzymology , Rabbits , Sarcoplasmic Reticulum/drug effects , Sarcoplasmic Reticulum/enzymology , Time Factors , Trypsin/pharmacology
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