Biomedical subjects

J Teisinger

Publications and source records attributed to J Teisinger.

At least 37 records · Page 2Linked to original sources

PubMed1987

Arachidonate has a positive effect on the electrogenic sodium-potassium pump in the mouse diaphragm.

Sodium arachidonate 5 X 10(-5) mol X l-1 shortened the time course of hyperpolarization caused by the electrogenic Na+-K+ pump in intact muscle fibres in the mouse diaphragm preincubated in a K+-free physiological solution. Contrary to experiments on membrane fragments, no inhibition of the ouabain-sensitive Na+-K+ ATPase was observed. It is unlikely that the arachidonate may be identical with the endogenous "ouabain-like" substance (Bidard et al. 1984).

Animals↗

PubMed1987

The toxic effect of dermotrophic substances in tests in vitro.

In the model system of tissue culture, the effect of dermatotrophic substances, such as the tenzides and conservatory substances, was tested. The cytotoxic effect of the substances was evaluated according to the vitality of the cells and the lactate dehydrogenase (LDH) activity in the suspension culture of human lymphocytes and further according to the migration inhibition of cells from the animal spleen fragments (SF). The cells obtained from rabbits, guinea pigs, mice and man were used. The highest correlation between the concentration of the substance in the cultivation medium and its toxic effect in the culture has been proved in the tests of LDH activity from the supernatant of the human peripheral lymphocytes culture and further in the migration inhibition test from rabbit SF. Both the tests are in mutual correlation. The determination of LDH activity represents a sensitive marker of the cell damage, the least sensitive is the estimation of the cell vitality. It has been proved that the system of suspension culture of human peripheral lymphocytes and the migration inhibition test from rabbit SF is suitable for the screening determination of the effect of dermatotrophic substances. The system of tissue culture compared to classical tests of skin irritation performed in vivo secures overall objectivity in evaluating the results and the possibility of making a number of parallels without any ethical limits.

Animals↗

PubMed1986

Vanadyl ions increase the order parameter of plasma membranes without changing the rotational relaxation time.

Differential polarized phase fluorometry of 1,6-diphenyl-1,3,5-hexatriene showed that vanadyl ions (VO2+) increased its limiting anisotropy (order parameter) in crude plasma membranes from brown adipose tissue of the golden hamster (Mesocricetus auratus). This was about 10(3) times larger than the effect of Ca2+ and was several times greater than the action of Co2+. Vanadate anions were without any effect. During the membrane treatment with VO2+, the rotational relaxational time of diphenylhexatriene did not change. This results suggest a possible positive influence of tetravalent vanadium on the stability of cell membranes.

Adipose Tissue, Brown↗

PubMed1986

Effect of catecholamines and metal chelating agents on the brain and brown adipose tissue Na,K-ATPase.

Catecholamines stimulate Na,K-ATPase activity in the microsomal membranes of the brain and brown adipose tissue. This stimulation is apparent in the absence of soluble, cytosolic inhibitors and exhibits the same characteristics in both tissues: it occurs at high concentrations (10(-6)-10(-4) M) only; there is no difference in potency between isoprenaline, norepinephrine and epinephrine (EC50 = 1-2 X 10(-5) M); the D-stereoisomer of isoprenaline is equally as effective as the L-form; stimulation of Na,K-ATPase may also be achieved by the metal chelators EDTA, EGTA and desferal; the hydrophobic beta-blockers, propranolol and alprenolol, inhibit both the norepinephrine-stimulated and basal levels of enzyme activity at concentrations of 10(-5)-10(-3) M; phenoxybenzamine, an irreversible alpha-adrenergic blocker, inhibits basal Na,K-ATPase as well as norepinephrine-stimulated enzyme activity (EC50 = 2.5 X 10(-5) M). Because none of these observations can be related to the properties of the stereospecific adrenergic receptor (alpha or beta), it may be concluded that the catecholamine-Na,K-ATPase interaction is not mediated by the receptor. More probably, catecholamines may antagonize the Na,K-ATPase inhibition caused by some tightly membrane-bound metals (but not vanadium) via the ortho-catechol moiety of the catecholamine molecule. The stimulation of brown fat Na,K-ATPase by catecholamines does not have much relevance to the norepinephrine-stimulated thermogenesis in this tissue.

Adipose Tissue, Brown↗

PubMed1985

The effect of opioids and of naloxone on Na+,K+-adenosine triphosphatase activity in frog spinal cord membrane fractions.

The effects of opioids and of naloxone on ouabain-sensitive Na+,K+-adenosine triphosphatase (ATPase) activity were studied in vitro on membrane fractions from frog spinal cords. The addition of morphine and of the stable enkephalin analogue, D-Ala2,D-Leu5-enkephalin, in concentrations from 10(-7) to 10(-4) M significantly increased Na+,K+-ATPase activity. No effect was found with methionine enkephalin (Met-Enk). However, the addition of two peptidase inhibitors, captopril and phosphoramidon (10(-5) M each), significantly increased Na+,K+-ATPase activity. A further increase in enzyme activity was found when Met-Enk (10(-4) or 10(-7) M) was added simultaneously with peptidase inhibitors. On the other hand, the addition of the opiate antagonist, naloxone, at low concentration (10(-7) M) decreased the activity of Na+,K+-ATPase. These results are discussed with respect to the effect of synthetic and endogenous opioids on the activity of Na+,K+-ATPase.

Animals↗

PubMed1985

On the mechanism of catecholamine-induced hyperpolarization of skeletal muscle cells.

Catecholamines (noradrenaline, adrenaline and isoprenaline) were tested for their effect on the resting membrane potential of mouse skeletal muscle cells. In freshly isolated muscles incubated in the normal solution containing 5 mol . l-1, catecholamines increased the resting membrane potential (RMP) by 3-5 mV. In Na+-loaded muscles incubated in a K+-free solution, however, catecholamines increased the RMP by 13-16 mV; consequent application of K+ to these muscles did not hyperpolarize the membrane further. A significant decrease of input membrane resistance was observed during the noradrenaline-induced hyperpolarization. This indicates that the passive membrane permeability for K+ ions was apparently increased. Noradrenaline-induced hyperpolarization requires the presence of calcium ions in the incubation solution. We therefore assume that catecholamines hyperpolarize the membrane by Ca2+-dependent K+-channels activation. The action of catecholamines on the resting membrane potential of skeletal muscle exhibits a 50% nonspecific effect as far as the adrenergic receptor is concerned, and the rest may be blocked by adrenergic blocking agents.

Animals↗

PubMed1985

Reduction of vanadate by some psychotropic drugs (chlorpromazine, imipramine and dosulepin) and the effect of bleomycine on Na, K-ATPase.

The reduction of vanadate (+5V) to vanadyl (+4V) was demonstrated by ESR spectra in the presence of methylene-blue, chlorpromazine, imipramine and dosulepin, but not in the presence of benzodiazepines and Li+. Bleomycine forms an (inactive) complex with +4V which may explain the disinhibition of the brain microsomal Na+-K+ ATPase in the presence of vanadyl. The reduction of +5V to +4V by antidepressants would diminish the binding of +5V to the ATPase and could account for some of the therapeutic action of the drugs in manic-depressive illness.

Animals↗

PubMed1984

The effect of anion channel blockers on enzymatic activity of Na+/K+-ATPase and the electrogenic Na+/K+ pump.

Disulfonic stilbenes which block the anion-transport in red blood cells were found to inhibit the brain microsomal Na+/K+-ATPase but not the electrogenic Na+/K+ pump in intact muscle cells. In contrast to the anion-transport system, the Na+/K+-ATPase is inhibited by disulfonic stilbenes, apparently from the cytoplasmic side of the membrane. The pathways for anion and active cation transport are thus different but similar groups of sulfhydryl and/or amino acid residues must play an important role in both systems.

Animals↗

PubMed1984

Hyperpolarization of mouse skeletal muscle plasma membrane induced by extracellular NADH.

Extracellularly applied NADH, but not NAD or NADPH, increases the resting membrane potential from -74.1 to -76.6 mV in freshly isolated muscles in the presence of K+ in the incubation medium and from -64.6 to -72.9 mV in muscles equilibrated for 4-6 h in a K+-free solution. The NADH-induced hyperpolarization is blocked by pretreatment of muscles with ouabain, and the inhibitors of plasma membrane NADH dehydrogenase (adriamycin, azide, PCMB, atebrine, DIDS and bleomycin). The effect of NADH is accompanied by the disappearance of NADH from the incubation medium and by decreased membrane resistance. We conclude that NADH hyperpolarization is due to the enhancement of passive membrane permeability, apparently for K+, which might result from the conformational changes in the plasma membrane during the NADH dehydrogenase reaction. The possibility is discussed that NADH dehydrogenase mediates transport of K+ out from the cell using a pathway connected with the transmembrane Na+/K+ pump.

Animals↗

PubMed1984

Vanadyl (VO2+) and vanadate (VO-3) ions inhibit the brain microsomal Na,K-ATPase with similar affinities. Protection by transferrin and noradrenaline.

The activity of Na,K-ATPase was measured in brain microsomes as the function of increasing concentrations of vanadyl (VOSO4, V4+) and the vanadate (NaVO3, V5+) ions. Both forms of vanadium inhibited the Na,K-ATPase activity with high affinity -Ki (vanadate) = 3 X 10(-7)M and Ki (vanadyl = 1 X 10(-6)M. The stability of V4+ in ATPase reaction media (Tris buffers) was measured by electron spin resonance spectroscopy. Without any reducing agent, V4+ was quickly oxidised by atmospheric oxygen. When a reducing agent such as dithiothreitol was added, the V4+ was stable for at least 30 min and the inhibition pattern of Na,K-ATPase by V4+ was not changed. The blocking effect of V4+ in the presence of dithiothreitol was counteracted by pre-incubation with equimolar concentrations of transferrin or 100 times excess of noradrenaline. The regulation of brain Na,K-ATPase by vanadate may be represented by competition between low-capacity inhibitory binding sites localized on the enzyme molecule and high-capacity sites of intracellular proteins. Preferential binding of vanadyl to the latter type of sites will decrease the intracellular concentration of the free metal and thus eliminate the enzyme inhibition.

Animals↗

PubMed1984

Vanadyl (VO2+) induced lipoperoxidation in the brain microsomal fraction is not related to VO2+ inhibition of Na,K-ATPase.

Vanadyl (VO2+) is a potent inductor of the lipid peroxidation in brain microsomes. This effect, however, is obtained at concentrations by two orders of magnitude higher (10(-4)-10(-3)M) than those which effectively inhibit the brain microsomal Na,K-ATPase. At 10(-6)M VO2+ which inhibits 50% of the Na,K-ATPase activity there is no measurable malonyldialdehyde production. Vanadate (VO-3) which is an equally potent inhibitor of Na,K-ATPase as VO2+ has almost no capacity to induce the lipoperoxidation. The addition of 10(-4)M ascorbate to the brain microsomes stimulates the lipoperoxidation to the maximum level regardless of the presence or absence of exogenous vanadium ions. Ascorbate-induced inhibition of brain Na,K-ATPase which is known to be associated with lipoperoxidation is strictly additive with the vanadyl (VO2+) inhibition of this enzyme. Even at submaximal concentrations there is no indication for any potentiation between these two inhibitory systems. The disparity between the mechanisms of ascorbate and vanadyl-induced inhibition of Na,K-ATPase is also documented by the effect of EDTA which inhibits the former type only. It is concluded, that the vanadium-induced inhibition of brain microsomal Na,K-ATPase is not related to induction of lipoperoxidative capacity of the brain.

Adenosine Triphosphatases↗

PubMed1984

Lysosomal and energy enzyme activities in hypertrophied rat soleus muscle after denervation.

Muscle hypertrophy was induced in the soleus muscle of young rats by tenotomy of the gastrocnemius and plantaris muscles. Three and 7 days afterwards the sciatic nerve was sectioned. The loss of weight of muscles subjected to this combined procedure three days after denervation was 30-40%. Lysosomal enzyme activities (acid phosphatase, alpha-glucosidase, beta-galactosidase and N-acetyl-beta-D-glucosaminidase) and energy enzyme activities (lactate dehydrogenase, LDH, triose-3-phosphate dehydrogenase, TPDH , D-hexokinase, HK and citrate synthase, CS) were determined 3 days after denervation, 3, 7 and 10 days after hypertrophy had been induced and 3 days after denervation of hypertrophying muscles on day 3 and 7. Normal non-operated rats of corresponding body weight served as controls and their enzyme activities were estimated on the same day. In the course of muscle hypertrophy, the 4 lysosomal enzyme activities increased progressively. Although 3 days' denervation of control muscles did not alter lysosomal enzyme activities, denervation of hypertrophying muscles greatly enhanced the activity of these enzymes. Enzymes of energy metabolism were affected to a lesser degree. The results suggest that denervation of hypertrophying muscles causes more extreme changes in muscle weight and lysosomal enzyme activities than denervation alone. The possible implications of this finding are discussed in relation to the rapid atrophy.

Animals↗

PubMed1983

Bleomycin stimulates both membrane (Na+-K+) ATPase and electrogenic (Na+-K+) pump and partially removes the inhibition by vanadium ions.

Bleomycin 2 X 10(-6) and 6 X 10(-6) mol.1(-1) increased the activity of specific (Na+-K+) ATPase of the rat brain microsomes. It also stimulated the electrogenic (Na+-K+) pump in intact skeletal muscle cells. The blocking effect of vanadyl (+4V) on membrane (Na+-K+) ATPase was eliminated completely by the drug, but the action of vanadate (+5V) was counteracted only partially. Electron paramagnetic resonance spectra revealed the formation of a +4V - bleomycin complex which is still able to activate the (Na+-K+) ATPase.

Animals↗

PubMed1983

The effect of five days' fasting on skeletal muscle enzymes in obese men.

The effect of 120 hours' (five days) fasting on the activity of some enzymes of energy metabolism in skeletal muscles was investigated in six obese young men. The results revealed a significant decline in the activity of the following enzymes: triosophosphate dehydrogenase (by 20%), glycerol-3-phosphate dehydrogenase (by 24%), lactate dehydrogenase (by 13%), citrate synthase (by 20%), hydroxyacyl-CoA dehydrogenase (by 40%), while the hexokinase and malate dehydrogenase activities were not significantly altered. Contrary to muscles of non-obese healthy men (Vondra, Bass, Brodan, Kuhn, Andĕl, Veselková and Vítek 1982), a smaller decline of activities of the investigated enzymes occurred together with a paradoxical change of the enzyme pattern, namely a predominance of carbohydrate catabolism and a decline of the role of fatty acids in muscle energy metabolism.

3-Hydroxyacyl CoA Dehydrogenases↗

PubMed1983

Postnatal development of the energy supplying enzyme pattern in the rat brain.

The activity of seven enzymes connected with energy-supplying metabolism was followed from the second day of life till adulthood (87th day). The enzymes selected were: 1. Triosephosphate dehydrogenase (TPDH), 2. Lactate dehydrogenase (LDH), 3. Glycerol-3-phosphate: NAD dehydrogenase (GPDH), 4. Hexokinase (HK), 5. Malate: NAD dehydrogenase (MDH), 6. Citrate syntase (CS) and 7. 3-Hydroxyacyl Co A dehydrogenase. Although some variations occurred, the enzyme profiles were characteristic of those of the nervous tissue from the second day of life onwards until adulthood and displayed relatively high activities of HK, CS and MDH and low activities of TPDH, LDH, GPDH and HOADH. The activities of all enzymes studied here increased during postnatal development and some reached adult values on the 14th day, that of TPDH on the 27th day and HOADH on the 41st day of life. The activities of MDH and GPDH did not attain the adult values still on the 41st day of life. The anaerobic energy supply capacity seems to increase transiently on the 31st day of life, i.e. at a developmental stage where the resistance against hypoxia is known to increase transiently.

3-Hydroxyacyl CoA Dehydrogenases↗

PubMed1983

Enzyme activity pattern in developing mouse brain in situ in embryonic brain aggregated cells at 37 degrees C and 0 degree C.

In aggregates of nervous tissue, cultivated for 1--7 days at 0 degree C and 37 degrees C, respectively, the activities of seven enzymes of energy liberating metabolism were estimated, in order to evaluate their metabolic "profiles" and changes during cultivation. The enzymes used as markers of different pathways of energy liberation from substrates were: lactate dehydrogenase - LDH - (EC 1.1.1.27), triose-3-phosphate dehydrogenase - TPDH - (EC 1.2.1.12), glycerol-3-phosphate dehydrogenase - GPDH - (EC 1.1.1.8), hexokinase - HK - (EC 2.7.1.1.), malate:NAD dehydrogenase - MDH - (EC 1.1.1.37), citrate synthase - CS - (EC 4.1.3.7), and 3-hydroxyacetyl CoA dehydrogenase - HOADH - (EC 1.1.1.35). During the cultivation, some changes in the metabolic "profiles" were observed. Although some of these changes as well as the differences between the cultivation at 0 degree C and 37 degrees C, were statistically significant, they were not greater than the variations between different samples of any tissue taken at different times. They were not, therefore considered to be of major significance. However, all the aggregates exhibited "profiles" characteristic for the nervous tissue, with relatively very high activity of HK, high activity of MDH and CS (carbohydrate breakdown) and low activity of GPDH and HOADH (lipid catabolism).

Animals↗

PubMed1983

Muscle enzyme activities and fibre composition (m. vastus lateralis) and efficiency of the cardiorespiratory system in cross-country skiers.

Fourteen male cross-country skiers (class I and II, average age 20.5 years) were examined by biochemical and histochemical methods. The activity of selected enzymes of energy metabolism and the percentage ratio of different types of muscle fibres (m. vastus lateralis) were assessed. Furthermore, the maximum values of the cardiorespiratory system and post-loading pH and blood lactate were determined after performance on a treadmill. The mitochondrial enzyme activities were relatively high with a considerable scatter in the values of HOADH activity. The glycolytic enzyme activities were on the same level as in subjects not engaged in sports. The percentage composition of muscle fibres was as follows: FG - 7.56 %, FOG - 30.65 % and SO - 61.79 %. Oxygen consumption VO2 max.kg-1 was 67.44 ml.min-1, pulse oxygen 24.76 ml, post-load pH 7.24 and blood lactate concentration 6.98 mmol.l-1. There was positive correlation between CS enzyme activity and oxygen uptake (VO2 max), pulse oxygen and percentage of SO muscle fibres. The mean values found in the athletes examined in the present study corresponded to values of middle distance runners.

Adult↗

PubMed1982

The comparison of vanadyl (IV) and insulin-induced hyperpolarization of the mammalian muscle cell.

Extracellularly applied vanadyl (IV) hyperpolarized the membrane potential of mouse diaphragm muscle from about -74.0 mV up to -81.7 mV. The hyperpolarizing effect of 10(-4) mol.I-1 vanadyl (IV) is comparable with hyperpolarization induced by 100 mU.ml-1 insulin. Both compounds increased the intracellular K+ concentration, the hyperpolarizing effect of vanadyl (IV) and insulin is blocked by ouabain and is unaffected by removal of K+ from the external medium. Triggering of the release of intracellular K+ associated with cellular proteins is proposed as the mechanism of vanadyl (IV) and insulin-induced hyperpolarization.

Animals↗