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  • 1
    Electronic Resource
    Electronic Resource
    ERRATUM: Molecular modeling of human MT2 melatonin receptor: the role of Val204, Leu272 and Tyr298 in ligand binding (2004)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 91 (2004), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.2004.02965.x
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular modeling of human MT2 melatonin receptor: the role of Val204, Leu272 and Tyr298 in ligand binding (2004)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 91 (2004), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: A model of the helical part of the human MT2 melatonin (hMT2) receptor, a member of the G protein-coupled receptors superfamily has been generated, based on the structure of bovine rhodopsin. Modeling has been combined with site-directed mutagenesis to investigate the role of the specific amino acid residues within the transmembrane domains (TM) numbers V, VI and VII of hMT2 receptor in the interaction with 2-iodomelatonin. Saturation binding assays with 2-iodomelatonin demonstrated that the substitution V204A (TMV) resulted in total loss of binding while the mutation V205A had no effect. The replacement of F209 with alanine led to a significant decrease in the Bmax value of receptor binding while mutations V205A and F209A also within TM V did not significantly change binding properties of the hMT2 receptor. In the case of TM VI, the substitution G271T caused substantial decrease in 2-iodomelatonin binding to the hMT2 receptor. The change L272A (TM VI) as well as mutation Y298A within TM VII completely abolished ligand binding to the receptor. These data suggest that several new amino acid residues within TM V, VI and VII are involved in ligand–MT2 receptor interaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.2004.02758.x
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular and functional properties of synaptically activated NMDA receptors in neonatal motoneurons in rat spinal cord slices (2000)
    Oxford, UK : Blackwell Science Ltd
    European journal of neuroscience 12 (2000), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The functional properties of N-methyl- d-aspartate (NMDA) receptor-mediated excitatory postsynaptic currents (EPSC) were studied in fluorescence-labelled motoneurons in thin spinal cord slices. The deactivation of NMDA receptor EPSCs in motoneurons voltage-clamped at +40 mV was independent of intensity or location of stimulation and of postnatal age [τfast = 28.5 ± 4.6 ms (63.6 ± 8.8%) and τslow = 165.6 ± 49.6 ms]. In the presence of 1 m m Mg2+ the amplitude of NMDA receptor EPSCs was voltage-dependent. Boltzmann analysis of the relationship between peak NMDA receptor EPSC amplitude and membrane potential suggested an apparent Kd of Mg2+ (at 0 mV) of 0.87 m m. Nonstationary variance analysis of NMDA receptor EPSCs gave an estimated single-channel conductance of 59 ± 14 pS. Direct measurement of the NMDA receptor channel openings in outside-out patches isolated from motoneurons indicated the presence of single-channel conductance levels of 21.8 ± 2.8 pS, 37.1 ± 3.2 pS, 49.6 ± 5.1 pS and 69.6 ± 4.2 pS. Single-cell RT-PCR analysis of mRNA revealed that NR1, NR2A–D and NR3A transcripts were expressed in motoneurons. These results suggest that specific assembly of NMDA receptor subunits in motoneurons determines the functional and pharmacological properties of the receptors in these cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1460-9568.2000.00989.x
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  • 4
    Electronic Resource
    Electronic Resource
    Importance of cardiac cell membranes in vanadate-induced NADH oxidation (reply) (1981)
    [s.l.] : Nature Publishing Group
    Nature 294 (1981), S. 288-288 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] VYSKOCIL ET AL. REPLY-The following remarks are pertinent to the discrepancies between our experimental data1 and those of Erdmann et al.2. First, the preparation of the vanadate solutions may well have caused some of the differences. In previous papers2, Erdmann et al. did not describe the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/294288b0
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  • 5
    Electronic Resource
    Electronic Resource
    On the mechanism of catecholamine-induced hyperpolarization of skeletal muscle cells (1985)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 329 (1985), S. 18-23 
    Details
    ISSN: 1432-1912
    Keywords: Noradrenaline ; Hyperpolarization ; Electrogenic Na+/K+ pump ; Ca2+-activated K+-channel ; Mouse diaphragm
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. 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 noradenaline-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. 2. 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00695186
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  • 6
    Electronic Resource
    Electronic Resource
    Enzyme activity patterns of energy supplying metabolism in the quadriceps femoris muscle(Vastus lateralis) (1976)
    Springer
    Pflügers Archiv 361 (1976), S. 169-173 
    Details
    ISSN: 1432-2013
    Keywords: Enzyme patterns ; Muscle enzymes ; Sedentary men ; Trained men ; Trained muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. In 3 groups of men, differing as to the amount and intensity of physical training loads, increasing in the order “sedentary”:“sporting”:“athletic”, enzyme activities were estimated in biopsy samples of m. quadriceps femoris (vastus lateralis). The enzymes were: Hexokinase (HK), NAD: glycerol-3-phosphate dehydrogenase (GPDH), triosephosphate dehydrogenase (TPDH), lactate dehydrogenase (LDH), citrate synthase (CS), NAD: malate dehydrogenase (MDH), and 3-hydroxyacyl-CoA dehydrogenase (HOADH). Indicators of laboratory performance and whole-body metabolic capacities (maximal oxygen consumption etc.) were estimated in the “sporting” and “athletic” groups. 2. In the 2 latter groups, distinguished by greater physical activity, the atypical enzyme activity pattern, remarkable by a low activity of LDH and high relative activities of GPDH and HK, as reported earlier in a sedentary group (Basset al., 1975a), disappeared. The possibility of the atypical low LDH enzyme activity pattern as resulting from lack of bodily exertion is discussed. 3. The moderately trained “sporting” group distinguishes itself from the “sedentary” one mainly by a higher activity of LDH and by lower activities of GPDH and MDH. In the intensively trained “athletic” group, enzymes connected to aerobic oxidation (MDH, CS, HOADH) and GPDH also show higher activities than in the “sporting” group. The difference between the two more active groups is further borne out by a higher maximum oxygen uptake and carbon dioxide release of the well-trained “athletic” group. This difference of enzyme activity pattern may not be confined to the quadriceps femoris muscle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00583462
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  • 7
    Electronic Resource
    Electronic Resource
    Effects of ischaemia on enzyme-activities in the soleus muscle of the rat (1979)
    Springer
    Pflügers Archiv 379 (1979), S. 203-208 
    Details
    ISSN: 1432-2013
    Keywords: Muscle ischaemia ; Muscle enzymes ; Energy metabolism ; Acid phosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract 1. The changes with the time of the activities of some energy-supplying enzymes and of the hydrolytic enzyme, acid phosphatase, were studied over 2 weeks of complete ischaemia, produced in the rat soleus muscle by section of the abdominal aorta and terminal devascularization, leaving nerve and tendon intact. 2. Activities of glycolytic enzymes, oxidative enzymes, hexokinase and acid phosphatase are affected in a different manner. Activities of the glycolytic enzymes, lactate dehydrogenase, triosephosphate dehydrogenase and glycerolphosphate dehydrogenase, are lowest on the 1st day and increase thereafter. The first two reach the control values again on the 4th and 14th day, respectively, while glycerolphosphate dehydrogenase reaches about 50% of the control value on the 14th day. The maximum decrease in activity of the oxidative enzymes, citrate synthase, β-hydroxyacyl-CoA-dehydrogenase and malate dehydrogenase occurs later (4th day); thereafter their activity returns slowly to control values, but does not reach them even on the 14th day. Hexokinase activity is slightly decreased on the 1st day; then it increased and reached on the 7th day twice the control value. Thus on the 1st day the activity of the enzymes of aerobic metabolism prevail, and on the 4th day those of anaerobic carbohydrate (glucose) metabolism; the recovery of enzyme activity of aerobic oxidation occurs later. 3. Acid phosphatase activity increased from the 2nd day onwards, reaching up to 3 times the control value on the 4th day and still twice that value on the 14th day. This agrees well with the histochemical picture of acid phosphatase. 4. Histochemical changes of alkaline phosphatase activity reveal destruction of capillary endothelial cells during the first few days after operation and their later proliferation from the periphery, correlating with the loss and recovery of oxidative enzyme activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00586949
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  • 8
    Electronic Resource
    Electronic Resource
    Different sensitivity of ATP + Mg + Na (I) and Pi + Mg (II) dependent types of ouabain binding to phospholipase A2 (1988)
    Springer
    The journal of membrane biology 104 (1988), S. 211-221 
    Details
    ISSN: 1432-1424
    Keywords: ouabain binding ; phospholipase A2 ; Na,K-ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The effect of phospholipase A2 and of related agents on ouabain binding and Na,K-ATPase activity were studied in intact and detergent-treated membrane preparations of rat brain cortex and pig kidney medulla. It was found that phospholipase A2 (PLA2) may distinguish or dissociate ouabain binding complexes I (ATP+Mg+Na) and II (Pi+Mg), stimulating the former and inhibiting the latter. Procedures which break the permeability barriers of vesicular membrane preparations, such as repeated freezing-thawing, sonication or hypoosmotic shock failed to mimic the effect of PLA2, indicating that it was not acting primarily by opening the inside-out oriented vesicles. The detergent digitonin exhibited similar effects on ouabain binding in both ATP+Mg+Na and Pi+Mg media. Other detergents were ineffective. The ability of PLA2 to distinguish between ouabain binding type I and II can be manifested even in SDS-treated, purified preparations of Na,K-ATPase. The number of ATP+Mg+Na-dependent sites is unchanged, while the Pi+Mg-dependent sites are decreased in number in a manner similar to that seen in original membranes. This inhibition is completely lost in the reconstituted Na,K-ATPase system, where the ATP- as well as Pi-oriented ouabain sites are inhibited by PLA2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01872323
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  • 9
    Electronic Resource
    Electronic Resource
    Enzyme activity patterns of energy metabolism in skiers of different performance levels (M. quadriceps femoris) (1982)
    Springer
    European journal of applied physiology 48 (1982), S. 315-322 
    Details
    ISSN: 1439-6327
    Keywords: Muscle enzyme activities ; VO2 max ; O2-pulse ; % Body fat ; Performance ; Skiers ; Seasonal changes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Changes in the activity of muscle enzymes of energy metabolism were studied in two groups of skiers (A, B) with a different sports performance (triosephosphate dehydrogenase-TPDH, lactate dehydrogenase-LDH, glycerol-3-phosphate dehydrogenase-GPDH, hexokinase-HK, malate dehydrogenase-MDH, citrate synthase-CS, hydroxyacyl, CoA dehydrogenase-HOADH). 1. In a group of ski-runners (A) significantly higher activities of CS, MDH, HOADH in the preparatory period (October) and also at the end of the competition period (March) were found in athletes with higher sports performance. 2. Significantly lower activities of LDH, GPDH, MDH, CS, HOADH were found in downhill skiers (group B). 3. Some significant correlations were established, both between the activities of individual enzymes (TPDH, GPDH, HK, CS, HOADH) and between the enzymes and indicators of functional capacity (MDH, CS, HOADH, VO2 max, HR max, O2-pulse max, body fat, laboratory performance).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00430221
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  • 10
    Electronic Resource
    Electronic Resource
    Changes in maximal aerobic power, aerobic capacity, and muscle enzyme activities at two stages of the annual training cycle in ski-runners (1980)
    Springer
    European journal of applied physiology 44 (1980), S. 17-23 
    Details
    ISSN: 1439-6327
    Keywords: Maximal aerobic power ; Aerobic capacity ; Muscle enzyme activities ; Ski runners
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Changes of cardiorespiratory capacity, of the activity of seven enzymes involved in energy metabolism and of laboratory endurance were investigated in a group of nine male ski-runners before and after exhausting training and a competing period during the winter. Despite the decrease in laboratory endurance and total work oxygen consumption between the investigations, $$\dot V$$ O2 max, O2-pulse max and O2 debt did not change; and O2-pulse per kg b.w. showed a significant increase. In biopsy samples of the vastus lateralis muscle, the activity of enzymes of carbohydrate metabolism, both anaerobic and total (triose phosphate dehydrogenase — TPDH, lactate dehydrogenase — LDH, hexokinase — HK), and of total aerobic metabolism (citrate synthetase — CS, malate dehydrogenase — MDH), was decreased during this period by 27 to 59% (mean values for different enzymes). The mean activity of cytoplasmic glycerol phosphate dehydrogenase (GPDH) and of hydroxyacyl — CoA dehydrogenase (HOADH) did not change, although the activity of the latter enzyme was decreased in the muscle of those ski-runners who were trained predominantly for speed, and it was increased in those trained mainly for endurance. The changes in activity of the muscle enzymes associated with glycolysis (TPDH and LDH) and of MDH, connected with metabolism and hydrogen transport between cytoplasmic and aerobic mitochondrial compartments, correlate inversely with those of aerobic capacity (total work O2 consumption).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00421759
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