ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

Ihre Suchhistorie ist leer.
feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
Filter
  • Ca2+-ATPase  (10)
  • calcium transport  (6)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 121 (1993), S. 127-133 
    ISSN: 1573-4919
    Schlagwort(e): calcium transport ; nicotinamide-adenine dinucleotides ; rat liver nuclei
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The effect of nicotinamide-adenine dinucleotides (NAD+ and NADP+) on Ca2+ transport in rat liver nuclei was investigated. Ca2+ uptake and release were determined with a Ca2+ electrode. Ca2+ uptake was dependent on adenosine triphosphate (ATP; 2mM). The presence of NAD+ (2mM) or NADP+ (1 and 2mM) caused a significant inhibition of Ca2+ uptake following addition of 2mM ATP. Ca2+, which accumulated in the nuclei during 6 min after ATP addition, was significantly released by the addition of NAD+ (0.5–2mM) or NADP+ (0.1–2mM). However, the effect of NADH (2mM) or NADPH (2mM) on Ca2+ uptake and release clearly weakened in comparison with the effects of NAD+ and NADP+. Meanwhile, ryanodine (10μM), thapsigargin (10μM) or oxalate (0.5mM) had no effect on Ca2+ uptake and release in rat liver nuclei. These reagents did not significantly alter the effects of 2mM NAD+ on Ca2+ uptake and release. Thus, NAD+ and NADP+ had a potent effect on Ca2+ transport in rat liver nuclei. The present findings suggest that the liver cytosolic NAD+ (NADP+) is a factor in the regulation of the nuclear Ca2+ concentration. (Mol Cell Biochem121: 127–133, 1993)
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 125 (1993), S. 43-49 
    ISSN: 1573-4919
    Schlagwort(e): Ca2+-ATPase ; calcium transport ; calmodulin ; rat liver nuclei
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The role of Ca2+-stimulated adenosine 5′-triphosphatase (Ca2+-ATPase) in Ca2+ sequestering of rat liver nuclei was investigated. Ca2+-ATPase activity was calculated by subtracting Mg2+-ATPase activity from (Ca2+−Mg2+)-ATPase activity. Ca2+ uptake and release were determined with a Ca2+ electrode. Nuclear Ca2+-ATPase activity increased linearly in the range of 10–40 μM Ca2+ addition. With those concentrations, Ca2+ was completely taken up by the nuclei dependently on ATP (2 mM). Nuclear Ca2+-ATPase activity was decreased significantly by the presence of arachidonic acid (25 and 50 μM), nicotinamide-adenine dinucleotide (NAD+; 2 mM) and zinc sulfate (2.5 and 5.0 μM). These reagents caused a significant decrease in the nuclear Ca2+ uptake and a corresponding elevation in Ca2+ release from the nuclei. Moreover, calmodulin (10 μg/ml) increased significantly nuclear Ca2+-ATPase activity, and this increase was not seen in the presence of trifluoperazine (10 μM), an antogonist of calmodulin. The present findings suggest that Ca2+-ATPase plays a role in Ca2+ sequestering by rat liver nuclei, and that calmodulin is an activator. Moreover, the inhibition of Ca2+-ATPase may evoke Ca2+ release from the Ca2+-loaded nuclei.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 146 (1995), S. 179-186 
    ISSN: 1573-4919
    Schlagwort(e): Ca2+-ATPase ; calcium ; nuclear DNA ; DNA fragmentation ; regucalcin ; regenerating rat liver
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The alteration of calcium content, Ca2+-ATPase activity, DNA content and DNA fragmentation in the nuclei of regenerating rat liver was investigated. Liver was surgically removed about 70% of that of sham-operated rats. the reduced liver weight by partial hepatectomy was completely restored at 3 days after the surgery. Regenerating liver significantly increased Ca2+-ATPase activity and DNA content in the nuclei between 1 and 5 days after hepatectomy. The nuclear calcium content was clearly increased from 2 days after hepatectomy. The increase of Ca2+-ATPase activity in regenerating liver was clearly inhibited by the presence of trifluoperazine (10 μM), staurosporine (2.5 μM) and dibucaine (10 μM), which are inhibitors of calmodulin and protein kinase, in the enzyme reaction mixture. However, the nuclear enzyme activity in normal rat liver was not significantly altered by these inhibitors. Meanwhile, the increase of nuclear DNA content in regenerating liver was completely blocked by the administration of trifluoperazine (2.5 mg/100 g body weight), suggesting an involvement of calmodulin. Now, the nuclear DNA fragmentation was significantly decreased in regenerating liver, suggesting that this decrease is partly contributed to the increase in nuclear DNA content. The present study clearly demonstrates that regenerating liver enhances nuclear Ca2+-ATPase activity and induces a corresponding elevation of nuclear calcium content. This Ca2+-signaling system may be involved in the regulation of nuclear DNA functions in regenerating rat liver.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 4
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 148 (1995), S. 33-37 
    ISSN: 1573-4919
    Schlagwort(e): DNA fragmentation ; Ca2+-ATPase ; calcium transport ; rat liver nuclei
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The effect of nuclear Ca2+ uptake inhibitors on the Ca2+-activated DNA fragmentation in rat liver nuclei was investigated. The addition of Ca2+ (40 μM) into the reaction mixture containing liver nuclei in the presence of 2.0 mM ATP caused a remarkable increase in nuclear DNA fragmentation. This Ca2+-activated DNA fragmentation was not seen in the absence of ATP, because nuclear Ca2+ uptake is not initiated without ATP addition. Moreover, the presence of various reagents (10 μM arachidonic acid, 2.0 mM NAD+, 10 μM zinc sulfate and 0.2 mM N-ethylmaleimide), which could inhibit Ca2+-ATPase activity and Ca2+ uptake in the nuclei, produced a significant inhibition of the Ca2+-activated DNA fragmentation in the nuclei. The results show that the Ca2+-activated DNA fragmentation is involved in the uptake of Ca2+ by the nuclei, suggesting a role of Ca2+ transport system in the regulation of liver nuclear functions.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 5
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 113 (1992), S. 63-70 
    ISSN: 1573-4919
    Schlagwort(e): regucalcin ; calcium-binding protein ; calcium transport ; rat liver nuclei
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The effect of regucalcin, a calcium-binding protein isolated from rat liver cytosol, on Ca2+ transport in rat liver nuclei was investigated. Ca2+ uptake and release were determined with a Ca2+ electrode. Ca2+ uptake increased dependent on adenosine triphosphate (ATP; 0.5-2.0 mM), while the uptake was negligible in the presence of 2 mM ADP or AMP. Regucalcin (0.5–2.0 μM) had no effect on Ca2+ uptake following addition of 2.0 mM ATP. Meanwhile, Ca2+, which accumulated in the nuclei during 10 min after ATP addition, was significantly released by the addition of regucalcin. This release was dose-dependent (0.1–2.0 μM). Vanadate (100 μM) and guanosine triphosphate (100 μM) did not cause a significant release of Ca2+ from the nuclei. Trifluoroperazine (TFP; 50 μM), an antagonist of calmodulin, significantly increased Ca2+ release from the nuclei. The presence of regucalcin (0.5 μM) further enhanced the TFP effect. These results indicate that regucalcin stimulates Ca2+ release from liver nuclei, and that the effect is not influenced by calmodulin antagonist. The finding suggests that regucalcin can regulate the Ca2+ transport system in rat liver nuclei.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 6
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 131 (1994), S. 167-172 
    ISSN: 1573-4919
    Schlagwort(e): Ca2+-ATPase ; Ca2+ transport ; Ca2+ channel ; rat liver nuclei
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The regulatory role of Ca2+-stimulated adenosine 5′-triphosphatase (Ca2+-ATPase) in Ca2+ transport system of rat liver nuclei was investigated. Ca2+ uptake and release were determined with a Ca2+ electrode. Ca2+-ATPase activity was calculated by subtracting Mg2+-ATPase activity from (Ca2+−Mg2+)-ATPase activity. The release of Ca2+ from the Ca2+-loaded nuclei was evoked progressively after Ca2+ uptake with 1.0 mM ATP addition, while it was only slightly in the case of 2.0 mM ATP addition, indicating that the consumption of ATP causes a leak of Ca2+ from the Ca2+-loaded nuclei. The presence of N-ethylmaleimide (NEM; 0.1 mM) caused an inhibition of nuclear Ca2+ uptake and induced a promotion of Ca2+ release from the Ca2+-loaded nuclei. NEM (0.1 and 0.2 mM) markedly inhibited nuclear Ca2+-ATPase activity. This inhibition was completely blocked by the presence of dithiothreitol (DTT; 0.1 and 0.5 mM). Also, DTT inhibited the effect of NEM (0.1 mM) on nuclear Ca2+ uptake and release. Meanwhile, verapamil and diltiazem (10 μM), a blocker of Ca2+ channels, did not prevent the NAD+ (1.0 and 2.0 mM), zinc sulfate (1.0 and 2.5 μM) and arachidonic acid (10 μM)-induced increase in nuclear Ca2+ release, suggesting that Ca2+ channels do not involve on Ca2+ release from the nuclei. These results indicates that an inhibition of nuclear Ca2+-ATPase activity causes the decrease in nuclear Ca2+ uptake and the release of Ca2+ from the Ca2+-loaded nuclei. The present finding suggests that Ca2+-ATPase plays a critical role in the regulatory mechanism of Ca2+ uptake and release in rat liver nuclei.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 7
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 166 (1997), S. 183-189 
    ISSN: 1573-4919
    Schlagwort(e): calcium transport ; DNA topoisomerase II inhibitor ; apoptosis ; DNA fragmentation ; rat liver nuclei
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The effect of various inhibitors of DNA topoisomerase II, which has been shown to induce apoptotic cell death, on Ca2+ transport in isolated rat liver nuclei was investigated. Ca2+ uptake and release were determined with a Ca2+ electrode. The presence of aurintricarboxylic acid (ATA; 10-6 to 10-4 M), etoposide (10-4 M), genistein (10-5 and 10-4 M) or amsacrine (10-4 M) in the reaction mixture caused a significant increase in Ca2+ release from the nuclei. Also, these compounds (10-4 M) significantly inhibited Ca2+ uptake by the nuclei. However, the presence of ATA (10-5 and 10-4 M) in the enzyme reaction mixture did not significantly inhibit Ca2+-ATPase activity, which is involved in the nuclear Ca2+ uptake, in the liver nuclei, while etoposide (10-4 M), genistein (10-4 M) and amsacrine (10-4 M) appreciably decreased the enzyme activity. Meanwhile, addition of Ca2+ clearly activated DNA fragmentation in the liver nuclei. The Ca2+ activated DNA fragmentation was significantly prevented by the presence of etoposide, genistein and amsacrine with the concentrations of 10-5 and 10-4 M in the reaction mixture, although ATA (10-5 and 10-4 M) had no effect. The present study demonstrates that some apoptosis inducible compounds used can influence on Ca2+ transport system in isolated rat liver nuclei, suggesting a decrease of nuclear Ca2+ level involved in nuclear functions. (Mol Cell Biochem 166: 183-189, 1997)
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 8
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 169 (1997), S. 149-156 
    ISSN: 1573-4919
    Schlagwort(e): regucalcin ; calmodulin ; Ca2+-ATPase ; Ca2+ pump ; basolateral ; membrane ; rat kidney cortex
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The effect of regucalcin, a calcium-binding protein, on ATP-dependent Ca2+ transport in the basolateral membranes isolated from rat kidney cortex was investigated. The prepared membranes were in inside-out oriented and membrane vesicles. Ca2+-ATPase activity in the basolateral membranes was progressively elevated by increasing concentrations of regucalcin (10-8 to 10-6 M) in the reaction mixture. This increase was dependent on Ca2+ addition. The activatory effect of regucalcin on the enzyme is inhibited by the presence of digitonin (5 × 10-6%) which can solubilize the membranous lipids. Moreover, the regucalcin effect was clearly abolished by the presence of vanadate (0.1 mM) or N-ethylmaleimide (5.0 mM). However, the effect of calmodulin (6 × 10-7 M) to increase Ca2+-ATPase activity was not significantly inhibited by vanadate or N-ethylmaleimide, indicating that the action mode of regucalcin differs from that of calmodulin. Also, the activatory effect of regucalcin on Ca2+-ATPase was appreciably inhibited by addition of dibutyryl cAMP (10-5 and 10-3 M), while inositol 1,4,5-trisphosphate (10-7 and 10-5 M) had no effect. Dibutyryl cAMP itself did not have an effect on the enzyme activity. Furthermore, the 45Ca2+ uptake by the basolateral membranes was clearly increased by the presence of regucalcin (10-7 and 10-6 M). This increase was completely blocked by the presence of vanadate (0.1 mM), N-ethylmaleimide (5.0 mM) or dibutyryl cAMP (10-4 and 10-3 M) in the reaction mixture. These results clearly demonstrate that regucalcin, which is expressed in rat kidney cortex, can increase Ca2+-ATPase activity and Ca2+ uptake in the basolateral membranes. Regucalcin may play a cell physiologic role as an activator in the ATP-dependent Ca2+ pumps in the basolateral membranes from rat kidney cortex.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 9
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 185 (1998), S. 153-159 
    ISSN: 1573-4919
    Schlagwort(e): calcium ; Ca2+-ATPase ; DNA fragmentation ; liver nuclei ; liver injury ; carbon tetrachloride
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The alteration in calcium transport in the liver nuclei of rats orally administered carbon tetrachloride (CCl4) was investigated. Rats received a single oral administration of CCl4(5, 10, and 25%, 1.0ml/100 g body weight), and 5, 24 and 48 h later the animals were sacrificed. The administration of CCl4 (25%) caused a remarkable elevetion of calcium content in the liver tissues and the nuclei of rats. Liver nuclear Ca2+-ATPase activity was markedly decreased by CCl4 (25%) administration. The presence of dibutyryl cyclic AMP(10-4 and 10-3 M) or inositol 1,4,5-trisphosphate (10-6 and 10-5 M) in the enzyme reaction mixture caused a significant decrease in Ca2+-ATPase activity in the liver nuclei obtained from normal rat, while the enzyme activity was significantly increased by calmodulin (1.0 and 2.0 μg/ml). These signaling factor's effects were completely impaired in the liver nuclei obtained from CCl4 (25%)-administered rats. DNA fragmentation in the liver nuclei obtained from CCl4 -administered rats was significantly decreased by the presence of EGTA (2 mM) in the reaction mixture, suggesting that the endogenous calcium activates nuclear DNA fragmentation. The present study demonstrates that calcium transport system in the liver nuclei is impaired by liver injury with CCl4 administration in rats.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 10
    ISSN: 1573-4919
    Schlagwort(e): regucalcin ; calcium-binding protein ; gene expression ; Ca2+-ATPase ; brain microsomes ; aging
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract The expression of calcium-binding protein regucalcin and its effect on the microsomal Ca2+-ATPase activity in rat brain tissues was investigated. The expression of regucalcin mRNA was demonstrated by reverse transcription-polymerase chain reaction (RT-PCR) analysis in brain tissues using rat regucalcin-specific primers. Regucalcin concentration in the brain tissues was about 5 × 10-9 M as measured using enzyme-linked immunoadsorbent assay (ELISA), and this level was lowered with increasing age (50 weeks old). The presence of regucalcin (10-9 to 10-7 M) in the enzyme reaction mixture caused a significant decrease in Ca2+-ATPase activity in the brain microsomes of young rats (5 weeks old). Meanwhile, the enzyme activity was not significantly altered by the addition of calmodulin (1 or 50 μg/ml), calbindin (1 or 10 μg/ml), and S-100 A protein (5 or 25 μg/ml), which are other Ca2+-binding proteins in rat brain. The effect of regucalcin to inhibit microsomal Ca2+-ATPase activity was weakened in the brain of rats with increasing age (50 weeks old). The present study demonstrates that regucalcin is expressed in the brain, and that it can uniquely inhibit Ca2+-ATPase activity in the brain microsomes of rats. The findings suggest that regucalcin plays a role in the regulation of microsomal Ca2+-ATPase activity in rat brain tissues.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...