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排序方式: 共有1556条查询结果,搜索用时 15 毫秒
1.
Charles E. Wenner John C. Cheney L. David Tomei 《Journal of cellular biochemistry》1981,15(2):161-168
The introduction of either PGF2α (10?7 M) or TPA (10?7 M) stimulated, ouabain-sensitive 86Rb+ influx at 30 min in postconfluent 3T3-4 mouse fibroblast cultures by 117% and 124%, respectively. Both TPA and PGF2α at these concentrations stimulated the incorporation of 3H-TdR into DNA. TPA had the greatest stimulatory effect, which was similar to that obtained with 10% fetal calf serum. In accord with the idea that modulation of membrane processes such as Na+/K+ pump activity in fibroblasts may reflect important events related to the initiation of DNA synthesis, it was observed that in both 3T3-4 and C3H-1 0T½ cells there were parallel increases in 3H-TdR incorporation and ouabain-sensitive 86Rb+ influxes with 10?7 M TPA, whereas PGF2α stimulated a significant increase in 3H-TdR incorporation in 3T3-4 but not C3H-10T½ cells and only marginal increases in ouabain-sensitive 86Rb+ influx in both. Therefore, although there appears to be a close correlation between Na+/K+ pump activation and subsequent S-phase entry following TPA stimulation, a similar correlation for PGF2α cannot be confirmed. 相似文献
2.
J. P. Infante 《Molecular and cellular biochemistry》1987,74(2):111-116
A critical review of the experimental literature concerning the metabolism of all-cis-4, 7, 10, 13, 16, 19-docosahexaenoate-containing phospholipids in muscle and retina suggests that it plays an essential role in maximizing the Ca2+/ATP stoichiometry of the Ca2+-ATPase of sarcoplasmic reticulum and retinal photoreceptor disks. Docosahexaenoate-phosphatidylcholine is proposed to participate in oligomerization of Ca2+-ATPase necessary for the establishment of a high Ca2+/ATP coupling ratio of the Ca2+ pump in these tissues. Possible tests of this hypothesis are presented. 相似文献
3.
Arthur H. L. From Dwight S. Fullerton Khalil Ahmed 《Molecular and cellular biochemistry》1990,94(2):157-165
The structure-activity relationships of the genin moieties of digitalis glycosides are commonly elucidated by determining the inhibitory potency of a variety of genins toward the plasma membrane Na+, K+-ATPase; qualitatively these relationships appear to be fairly independent of the specific Na+, K+-ATPase preparation utilized for the analysis. To determine whether this is the case with regard to the sugar moieties of glycosides, the inhibitory effects of 12 monoglycosides of digitoxigenin toward four Na+, K+-ATPase preparations of different origin were measured. It was found that while recognition of the major structural determinants of sugar activity appeared to be independent of enzyme source, recognition of the minor structural determinants of activity showed some source dependence. It was also observed that the intrinsic sensitivity to sugar potentiation may be source dependent and unrelated to intrinsic sensitivity to inhibition by digitoxigenin. These observations are compatible with a model of the Na+, K+-ATPase sugar binding site(s) in which intrinsic sensitivity to sugar attachment as well as recognition characteristics (for sugar structural features) both determine the extent to which a sugar moiety may contribute to the activity of monoglycosides. Further, in these studies one of the Na+, K+-ATPase preparations employed was obtained from rat brain, a tissue known to contain a mixture of ouabain sensitive and insensitive isoforms. We have observed that the rigorous purification techniques employed appear to have selectively removed from or denatured the less ouabain sensitive al isoform found in this enzyme preparation. 相似文献
4.
Summary The two high affinity calcium binding sites of the cardiac (Ca2+ + Mg2+)-ATPase have been identified with the use of Eu3+. Eu3+ competes for the two high affinity calcium sites on the enzyme. With the use of laser-pulsed fluorescent spectroscopy, the environment of the two sites appear to be heterogeneous and contain different numbers of H2O molecules coordinated to the ion. The ion appears to be occluded even further in the presence of ATP. Using non-radiative energy transfer studies, we were able to estimate the distance between the two Ca2+ sites to be between 9.4 to 10.2 A in the presence of ATP. Finally, from the assumption that the calcium site must contain four carboxylic side chains to provide the 6–8 ligands needed to coordinate calcium, and based on our recently published data, we predict the peptidic backbone of the two sites. 相似文献
5.
Kodavanti S. Prasada Rao Sreeramulu C. Chetty Durisala Desaiah 《Journal of biochemical and molecular toxicology》1987,2(2):125-140
Tricyclohexylhydroxytin, commonly known as Plictran® inhibited Na+, K+ -ATPase activity of rat brain synaptosomes in a concentration-dependent manner with median inhibitory concentration (IC-50) of 2 μM. Both K+ -stimulated para-nitrophenylphosphatase and [3-H]-ouabain binding to synaptosomes were also inhibited by Plictran with IC-50 values of 11 and 30 μM, respectively. Altered pH and Na+, K+ -ATPase activity curves demonstrated comparable inhibition in buffered neutral and alkaline pH ranges, and no inhibition was observed in acidic pH. The inhibition of Na+, K+ -ATPase was independent of temperature. Kinetic studies of substrate (ATP) activation of Na+, K+ -ATPase indicated uncompetitive inhibition. Results also showed noncompetitive inhibition for p-nitrophenylphosphate and uncompetitive inhibition for K+ activations of p-nitrophenylphosphatase. Preincubation of synaptosomes with dithiothreitol, a sulfhydryl (SH) agent, resulted in the complete protection of Plictran inhibition of Na+, K+ -ATPase, K+ -para-nitrophenylphosphatase, and [3-H]-ouabain binding. The protection was specific and concentration dependent since cysteine and glutathione did not afford protection. These results indicate that Plictran inhibited Na+, K+ -ATPase by interacting with dephosphorylation of the enzyme-phosphoryl complex and exerted a similar effect to that of SH-blocking agents. 相似文献
6.
Yuh-Jiin Jong Adrian Sheldon Guo H. Zhang Naomi Kraus-Friedmann 《The Journal of membrane biology》1990,118(1):49-53
Summary The Ca2+-ATPase from rat liver microsomes has been solubilized in Triton X-100 and purified to homogeneity by ficollsucrose treatment, column chromatography with agarose-hexane adenosine 5-triphosphate Type 2, and high pressure liquid chromatography (HPLC). The purified enzyme obtained by this sequential procedure exhibited a 183-fold increase in specific activity. After ficoll-sucrose treatment, the activity of the Ca2+-ATPase was stable for at least two weeks when stored at –70°C. In SDS-polyacrylamide gels, several fractions from HPLC chromatography showed a single band at a position corresponding to a molecular weight of about 107 kDa. This value is consistent with the molecular weight of the phosphoenzyme intermediate of endoplasmic reticulum (ER) Ca2+-ATPase. Further characterization of the ER Ca2+-ATPase was performed by western immunoblots. Antiserum raised against the 100-kDa sarcoplasmic reticulum (SR) Ca2+-ATPase cross-reacted with the purified Ca2+-ATPase from rat liver ER membranes. 相似文献
7.
Tadao Hashimoto Yukuo Yoshida Kunio Tagawa 《Journal of bioenergetics and biomembranes》1990,22(1):27-38
An intrinsic ATPase inhibitor inhibits the ATP-hydrolyzing activity of mitochondrial F1F0-ATPase and is released from its binding site on the enzyme upon energization of mitochondrial membranes to allow phosphorylation of ADP. The mitochondrial activity to synthesize ATP is not influenced by the absence of the inhibitor protein. The enzyme activity to hydrolyze ATP is induced by dissipation of the membrane potential in the absence of the inhibitor. Thus, the inhibitor is not responsible for oxidative phosphorylation, but acts only to inhibit ATP hydrolysis by F1F0-ATPase upon deenergization of mitochondrial membranes. The inhibitor protein forms a regulatory complex with two stabilizing factors, 9K and 15K proteins, which facilitate the binding of the inhibitor to F1F0-ATPase and stabilize the resultant inactivated enzyme. The 9K protein, having a sequence very similar to the inhibitor, binds directly to F1 in a manner similar to the inhibitor. The 15K protein binds to the F0 part and holds the inhibitor and the 9K protein on F1F0-ATPase even when one of them is detached from the F1 part. 相似文献
8.
Reconstituted Na+,K+-ATPase from either pig kidney or shark rectal glands was phosphorylated by cAMP dependent protein kinase, PKA. The stoichiometry was 0.9 mole Pi/mole -subunit in the pig kidney enzyme and 0.2 mol Pi/mol -subunit in the shark enzyme. In shark Na+,K+-ATPase PKA phosphorylation increased the maximum hydrolytic activity for cytoplasmic Na+ activation and extracellular K+ activation without affecting the apparent Km values. In contrast, no significant functional effect after PKA phosphorylation was observed in pig kidney Na+,K+-ATPase. 相似文献
9.
G. Benzi A. Gorini B. Ghigini A. Moretti F. Dagani R. F. Villa 《Neurochemical research》1996,21(1):7-18
The changes in the Mg2+-dependent V-type ATPase activity and the Mg2+-ATP-dependent H+ pumping activity of the synaptic vesicles from the cerebral cortex of rats submitted to intermittent chronic (4 weeks) mild
or severe hypoxia were evaluated. The adaptation to the chronic severe hypoxia increases both the ATPase and the H+ pumping activities which are inhibited by NEM with an exponential relationship between the IC50 values and the in vivo O2 concentration. The Mg2+-dependent increase in H+ pumping activity of synaptic vesicles from the rats subjected to in vivo chronic hypoxia may be antagonized by nigericin
(dissipating ΔpH) and by FCCP (dissipating ΔpH and ΔΨSV). In contrast, valinomycin (dissipating the ΔΨSV and facilitating an enhancement in ΔpH) increases in vitro the H+ pumping activity that is inhibited by the addition of high concentration of K gluconate (reducing the rate of K+ efflux). The preincubation of vesicles from hypoxic rats with FCCP, but not with nigericin, inhibits the valinomycin-increased
H+ pumping activity.l-glutamate increases the H+ pumping activity in synaptic vesicles from the cerebral cortex of chronic hypoxic rats, whereas other amino acids (i.e.,l-aspartate andl-homocysteate) and glutamate analogs (i.e., quisqualate and ibotenate) are ineffective. The adaptation to both chronic intermittent
severe hypoxia and in vivo treatment with posatireline causes a decrease in the Mg2+-ATPase activity consistent with the decrease in the H+ pumping one of the synaptic vesicles. The addition of nigericin into incubation medium magnifies the decrease in the H+ pumping activity, while the addition of FCCP is ineffective, suggesting that the treatment with posatireline interferes with
the ΔΨSV component in the
of the synaptic vesicles from rats submitted to chronic hypoxia. The results of the in vivo and in vitro experiments suggest
that in the synaptic vesicles from hypoxic rats the ΔΨSV component in
may be most effective in increasing the Mg2+-ATP-dependent H+ pumping activity. 相似文献
10.
S. Gulati M. Khullar B. K. Sharma N. K. Ganguly 《Molecular and cellular biochemistry》1996,156(1):37-42
Intracellular free Ca2+ concentration has been shown to be elevated in platelets of patients with essential hypertension. This study was designed to characterize Ca2+-pump activity of the platelet membranes (surface and intracellular) in these patients. A double-blind study was carried out. Untreated and treated (on R-blockers) essential hypertensives were studied in comparison with normotensive control subjects. First degree blood relatives of essential hypertensives were also studied. The Ca2+-activation kinetics of the enzyme showed a significant decrease in the Vmax. (for the plasma- and intracellular membranes) and Km (for the intracellular membranes) in the essential hypertensive patients. Increased platelet membrane cholesterol content was observed in these patients. Lowered Ca2+-efflux by Ca2+-ATPase may lead to elevated intracellular free Ca2+-levels in platelets of essential hypertensives. A lowered Ca2+-ATPase activity may emerge as a marker for essential hypertension. 相似文献