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    Wyświetlanie 1-19 z 19
    Tytuł:
    Spectrophotometric assay of renal ouabain-resistant Na+-ATPase and its regulation by leptin and dietary-induced obesity.
    Autorzy:
    Bełtowski, Jerzy
    Jamroz-Wiśniewska, Anna
    Nazar, Jarosław
    Wójcicka, Grażyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1041514.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    leptin
    obesity
    Na+,K+-ATPase
    Na+-ATPase
    Opis:
    Apart from Na+,K+-ATPase, a second sodium pump, Na+-stimulated, K+-independent ATPase (Na+-ATPase) is expressed in proximal convoluted tubule of the mammalian kidney. The aim of this study was to develop a method of Na+-ATPase assay based on the method previously used by us to measure Na+,K+-ATPase activity (Acta Biochim Polon.; 2002, 49: 515-27). The ATPase activity was assayed as the amount of inorganic phosphate liberated from ATP by isolated microsomal fraction. Na+-ATPase activity was calculated as the difference between the activities measured in the presence and in the absence of 50 mM NaCl. Na+-ATPase activity was detected in the renal cortex (3.5 ± 0.2 μmol phosphate/h per mg protein), but not in the renal medulla. Na+-ATPase was not inhibited by ouabain or an H+,K+-ATPase inhibitor, Sch 28080, but was almost completely blocked by 2 mM furosemide. Leptin administered intraperitoneally (1 mg/kg) decreased the Na+,K+-ATPase activity in the renal medulla at 0.5 and 1 h by 22.1% and 27.1%, respectively, but had no effect on Na+-ATPase in the renal cortex. Chronic hyperleptinemia induced by repeated subcutaneous leptin injections (0.25 mg/kg twice daily for 7 days) increased cortical Na+,K+-ATPase, medullary Na+,K+-ATPase and cortical Na+-ATPase by 32.4%, 84.2% and 62.9%, respectively. In rats with dietary-induced obesity, the Na+,K+- ATPase activity was higher in the renal cortex and medulla by 19.7% and 34.3%, respectively, but Na+-ATPase was not different from control. These data indicate that both renal Na+-dependent ATPases are separately regulated and that up-regulation of Na+-ATPase may contribute to Na+ retention and arterial hypertension induced by chronic hyperleptinemia.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 4; 1003-1014
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Spectrophotometric method for the determination of renal ouabain-sensitive H+,K+ -ATPase activity.
    Autorzy:
    Bełtowski, Jerzy
    Wójcicka, Grażyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1043791.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    leptin
    kidney
    H+,K+-ATPase
    ouabain
    Sch 28080
    Na+,K+-ATPase
    Opis:
    The aim of this work was to develop a method for renal H+,K+-ATPase measurement based on the previously used Na+,K+-ATPase assay (Bełtowski et al.: J Physiol Pharmacol.; 1998, 49: 625-37). ATPase activity was assessed by measuring the amount of inorganic phosphate liberated from ATP by isolated microsomal fraction. Both ouabain-sensitive and ouabain-resistant K+-stimulated and Na+-independent ATPase activity was detected in the renal cortex and medulla. These activities were blocked by 0.2 mM imidazolpyridine derivative, Sch 28080. The method for ouabain- sensitive H+,K+-ATPase assay is characterized by good reproducibility, linearity and recovery. In contrast, the assay for ouabain-resistant H+,K+-ATPase was unsatisfactory, probably due to low activity of this enzyme. Ouabain-sensitive H+,K+-ATPase was stimulated by K+ with Km of 0.26 ± 0.04 mM and 0.69 ± 0.11 mM in cortex and medulla, respectively, and was inhibited by ouabain (Ki of 2.9 ± 0.3 μM in the renal cortex and 1.9 ± 0.4 μM in the renal medulla) and by Sch 28080 (Ki of 1.8 ± 0.5 μM and 2.5 ± 0.9 μM in cortex and medulla, respectively). We found that ouabain-sensitive H+,K+-ATPase accounted for about 12% of total ouabain-sensitive activity in the Na+,K+-ATPase assay. Therefore, we suggest to use Sch 28080 during Na+,K+-ATPase measurement to block H+,K+-ATPase and improve the assay specificity. Leptin administered intraperitoneally (1 mg/kg) decreased renal medullary Na+,K+-ATPase activity by 32.1% at 1 h after injection but had no effect on H+,K+-ATPase activity suggesting that the two renal ouabain-sensitive ATPases are separately regulated.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 2; 515-527
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    A new method to precipitate myosin v from rat brain soluble fraction
    Autorzy:
    Melo, Hugo
    Coelho, Milton
    Powiązania:
    https://bibliotekanauki.pl/articles/1041042.pdf
    Data publikacji:
    2007
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    myosin V
    ATPase
    F-actin
    Opis:
    Myosin can be precipitated from soluble fraction under different assay conditions. This paper describes a new method for precipitating myosin V from rat brain soluble fraction. Brains were homogenized in 50 mM imidazole/HCl buffer, pH 8.0, containing 10 mM EDTA/EGTA, 250 mM sucrose, 1 mM DTT and 1 mM benzamidine, centrifuged at 45000 × g for 40 min and the supernatant was frozen at -20 °C. Forty-eight hours later, the supernatant was thawed, centrifuged at 45000 × g for 40 min and the precipitate was washed in 20 mM imidazole buffer pH 8.0. SDS/PAGE analysis showed four polypeptides in the precipitate: 205, 150, 57 and 43 kDa. The precipitate presented high Mg2+-ATPase activity, which co-purifies with p205. This polypeptide was recognized by a specific myosin V antibody and was proteolised by calpain, generating two stable polypeptides: p130 and p90. The Mg2+-ATPase activity was not stimulated by calcium in both the absence and presence of exogenous calmodulin and the K+/EDTA-ATPase activity represented 25% of the Mg2+-ATPase activity. In this work, myosin V from rat brain was precipitated by freezing the soluble fraction and was co-purificated with a 45 kDa polypeptide.
    Źródło:
    Acta Biochimica Polonica; 2007, 54, 3; 575-581
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Nitric oxide - superoxide cooperation in the regulation of renal Na+,K+-ATPase.
    Autorzy:
    Bełtowski, Jerzy
    Marciniak, Andrzej
    Jamroz-Wiśniewska, Anna
    Borkowska, Ewelina
    Powiązania:
    https://bibliotekanauki.pl/articles/1041505.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    H+,K+-ATPase
    Sch 28080
    superoxide anion
    Na+,K+-ATPase
    nitric oxide
    oxidative stress
    Opis:
    The aim of this study was to investigate whether endogenous superoxide anion is involved in the regulation of renal Na+,K+-ATPase and ouabain-sensitive H+,K+-ATPase activities. The study was performed in male Wistar rats. Compounds modulating superoxide anion concentration were infused under general anaesthesia into the abdominal aorta proximally to the renal arteries. The activity of ATPases was assayed in isolated microsomal fraction. We found that infusion of a superoxide anion-generating mixture, xanthine oxidase (1 mU/min per kg) + hypoxanthine (0.2 μmol/min per kg), increased the medullary Na+,K+-ATPase activity by 49.5% but had no effect on cortical Na+,K+-ATPase and either cortical or medullary ouabain-sensitive H+,K+-ATPase. This effect was reproduced by elevating endogenous superoxide anion with a superoxide dismutase inhibitor, diethylthiocarbamate. In contrast, a superoxide dismutase mimetic, TEMPOL, decreased the medullary Na+,K+-ATPase activity. The inhibitory effect of TEMPOL was abolished by inhibitors of nitric oxide synthase (L-NAME), soluble guanylate cyclase (ODQ) and protein kinase G (KT5823). The stimulatory effect of diethylthiocarbamate was not observed in animals pretreated with a synthetic cGMP analogue, 8-bromo-cGMP. An inhibitor of NAD(P)H oxidase, apocynin (1 μmol/min per kg), decreased the Na+,K+-ATPase activity in the renal medulla and its effect was prevented by L-NAME, ODQ or KT5823. In contrast, a xanthine oxidase inhibitor, oxypurinol, administered at the same dose was without effect. These data suggest that NAD(P)H oxidase-derived superoxide anion increases Na+,K+-ATPase activity in the renal medulla by reducing the availability of NO. Excessive intrarenal generation of superoxide anion may upregulate medullary Na+,K+-ATPase leading to sodium retention and blood pressure elevation.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 4; 933-942
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Characterization of ATPase activity of the AAA ARC from Bifidobacterium longum subsp. infantis
    Autorzy:
    Guzmán-Rodríguez, Mabel
    de la Rosa, Ana
    Santos, Leticia
    Powiązania:
    https://bibliotekanauki.pl/articles/1039095.pdf
    Data publikacji:
    2015
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Bifidobacterium longum
    ARC
    AAA ATPase
    probiotic
    Opis:
    Bifidobacteria are considered to be probiotics that exist in the large intestine and are helpful to maintain human health. Oral administration of bifidobacteria may be effective in improving the intestinal flora and environment, stimulating the immune response and possibly preventing cancer. However, for consistent and positive results, further well-controlled studies are urgently needed to describe the basic mechanisms of this microorganism. Analysis of the proteasome-lacking Bifidobacterium longum genome reveals that it possesses a gene, IPR003593 AAA ATPase core, which codes a 56 kDa protein containing one AAA ATPase domain. Phylogenetic classification made by CLANS, positioned this sequence into the ARC divergent branch of the AAA ATPase family of proteins. N-terminal analysis of the sequence indicates this protein is closely related to other ATPases such as the Rhodococcus erythropolis ARC, Archaeoglobus fulgidus PAN, Mycobacterium tuberculosis Mpa and the human proteasomal Rpt1 subunit. This gene was cloned, the full-length recombinant protein was overexpressed in Escherichia coli, purified as a high-molecular size complex and named Bl-ARC. Enzymatic characterization showed that Bl-ARC ATPase is active, Mg+2-dependent and sensitive to N-ethylmaleimide. Gene organization positions bl-arc in a region flanked by a cluster of genes that includes pup, dop and pafA genes. These findings point to a possible function as a chaperone in the degradation pathway via pupylation.
    Źródło:
    Acta Biochimica Polonica; 2015, 62, 2; 221-227
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Regulation of renal Na+,K+ -ATPase and ouabain-sensitive H+,K+ -ATPase by the cyclic AMP-protein kinase A signal transduction pathway.
    Autorzy:
    Bełtowski, Jerzy
    Marciniak, Andrzej
    Wójcicka, Grażyna
    Górny, Dionizy
    Powiązania:
    https://bibliotekanauki.pl/articles/1043651.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    kidney
    cyclic AMP
    protein kinase A
    cytochrome P450-dependent arachidonate metabolites
    Na+,K+ -ATPase
    H+,K+ -ATPase
    Opis:
    We investigated the effect of the cyclic AMP-protein kinase A (PKA) signalling pathway on renal Na+,K+-ATPase and ouabain-sensitive H+,K+-ATPase. Male Wistar rats were anaesthetized and catheter was inserted through the femoral artery into the abdominal aorta proximally to the renal arteries for infusion of the investigated substances. Na+,K+-ATPase activity was measured in the presence of Sch 28080 to block ouabain-sensitive H+,K+-ATPase and improve specificity of the assay. Dibutyryl-cyclic AMP (db-cAMP) administered at a dose of 10-17 mol/kg per min and 10-6 mol/kg per min increased Na+,K+-ATPase activity in the renal cortex by 34% and 42%, respectively, and decreased it in the renal medulla by 30% and 44%, respectively. db-cAMP infused at 10-6 mol/kg per min increased the activity of cortical ouabain-sensitive H+,K+-ATPase by 33%, and medullary ouabain-sensitive H+,K+-ATPase by 30%. All the effects of db-cAMP were abolished by a specific inhibitor of protein kinase A, KT 5720. The stimulatory effect on ouabain-sensitive H+,K+-ATPase and on cortical Na+,K+-ATPase was also abolished by brefeldin A which inhibits the insertion of proteins into the plasma membranes, whereas the inhibitory effect on medullary Na+,K+-ATPase was partially attenuated by 17-octadecynoic acid, an inhibitor of cytochrome P450-dependent arachidonate metabolism. We conclude that the cAMP-PKA pathway stimulates Na+,K+-ATPase in the renal cortex as well as ouabain-sensitive H+,K+-ATPase in the cortex and medulla by a mechanism requiring insertion of proteins into the plasma membrane. In contrast, medullary Na+,K+-ATPase is inhibited by cAMP through a mechanism involving cytochrome P450-dependent arachidonate metabolites.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 1; 103-114
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Reducing effect of atrial natriuretic factor on Na, K-ATPase activity in rat kidney
    Autorzy:
    Gorny, D
    Korzeniowska, J.
    Marciniak, A.
    Pielecki, J.
    Powiązania:
    https://bibliotekanauki.pl/articles/69375.pdf
    Data publikacji:
    1994
    Wydawca:
    Polskie Towarzystwo Fizjologiczne
    Tematy:
    atrial natriuretic factor
    sodium
    potassium
    ATPase
    kidney
    rat
    Źródło:
    Journal of Physiology and Pharmacology; 1994, 45, 1
    0867-5910
    Pojawia się w:
    Journal of Physiology and Pharmacology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The effects of the interaction of myosin essential light chain isoforms with actin in skeletal muscles.
    Autorzy:
    Nieznańska, Hanna
    Nieznański0, Krzysztof
    Stępkowski, Dariusz
    Powiązania:
    https://bibliotekanauki.pl/articles/1043740.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    skeletal muscle biochemistry
    thin filament regulatory proteins
    myofibrillar ATPase
    Opis:
    In order to compare the ability of different isoforms of myosin essential light chain to interact with actin, the effect of the latter protein on the proteolytic susceptibility of myosin light chains (MLC-1S and MLC-1V - slow specific and same as ventricular isoform) from slow skeletal muscle was examined. Actin protects both slow muscle essential light chain isoforms from papain digestion, similarly as observed for fast skeletal muscle myosin (Nieznańska et al., 1998, Biochim. Biophys. Acta 1383: 71). The effect of actin decreases as ionic strength rises above physiological values for both fast and slow skeletal myosin, confirming the ionic character of the actin-essential light chain interaction. To better understand the role of this interaction, we examined the effect of synthetic peptides spanning the 10-amino-acid N-terminal sequences of myosin light chain 1 from fast skeletal muscle (MLC-1F) (MLCFpep: KKDVKKPAAA), MLC-1S (MLCSpep: KKDVPVKKPA) and MLC-1V (MLCVpep: KPEPKKDDAK) on the myofibrillar ATPase of fast and slow skeletal muscle. In the presence of MLCFpep, we observed an about 19% increase, and in the presence of MLCSpep about 36% increase, in the myofibrillar ATPase activity of fast muscle. On the other hand, in myofibrillar preparations from slow skeletal muscle, MLCSpep as well as MLCVpep caused a lowering of the ATPase activity by about 36%. The above results suggest that MLCSpep induces opposite effects on ATPase activity, depending on the type of myofibrils, but not through its specific N-terminal sequence - which differs from other MLC N-terminal peptides. Our observations lead to the conclusion that the action of different isoforms of long essential light chain is similar in slow and fast skeletal muscle. However the interaction of essential light chains with actin leads to different physiological effects probably depending on the isoforms of other myofibrillar proteins.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 3; 709-719
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Plasma membrane Ca2+ -ATPase in excitable and nonexcitable cells.
    Autorzy:
    Żylińska, Ludmiła
    Soszyński, Mirosław
    Powiązania:
    https://bibliotekanauki.pl/articles/1044284.pdf
    Data publikacji:
    2000
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    calcium homeostasis
    brain
    erythrocytes
    plasma membrane Ca2+ -ATPase
    Opis:
    There is a significant number of data confirming that the maintenance of calcium homeostasis in a living cell is a complex, multiregulated process. Calcium efflux from excitable cells (i.e., neurons) occurs through two main systems - an electrochemically driven Na+/Ca2+ exchanger with a low Ca2+ affinity (K0.5 = 10-15 μM), and a plasmalemmal, specific Ca2+-ATPase, with a high Ca2+ affinity (K0.5 < 0.5-1 μM), whereas in nonexcitable cells (i.e., erythrocytes) the calcium pump is the sole system responsible for the extrusion of calcium ions. The plasma membrane Ca2+-ATPase (PMCA) is a ubiquitously expressed protein, and more than 26 transcripts of four PMCA genes are distributed in a tissue specific manner. Differences in the structure and localization of PMCA variants are thought to correlate with specific regulatory properties and may have consequences for proper cellular Ca2+ signaling. The regulatory mechanisms of calcium pump activity have been studied extensively, resulting in a new view of the functioning of this important molecule in the membranes.
    Źródło:
    Acta Biochimica Polonica; 2000, 47, 3; 529-539
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Cucumber HMA5A and HMA5B are two tonoplast-localized homologs of Arabidopsis thaliana heavy metal ATPase HMA5 involved in cellular heavy metal homeostasis
    Autorzy:
    Migocka, M.
    Papierniak, A.
    Posyniak, E.
    Powiązania:
    https://bibliotekanauki.pl/articles/81291.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    Arabidopsis thaliana
    ATPase
    homeostasis
    heavy metal
    gene encoding
    tonoplast membrane
    Źródło:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
    0860-7796
    Pojawia się w:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    The involvement of Na+/K+-ATPase in the development of platelet procoagulant response
    Autorzy:
    Tomasiak, Marian
    Stelmach, Halina
    Rusak, Tomasz
    Ciborowski, Michał
    Radziwon, Piotr
    Powiązania:
    https://bibliotekanauki.pl/articles/1041052.pdf
    Data publikacji:
    2007
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cardiac glycosides
    ouabain
    Na+/K+-ATPase
    atrial fibrillation
    platelets
    procoagulant activity
    Opis:
    In circulation, platelets may come into contact with both exogenous (cardiac glycoside treatment) and endogenously produced inhibitors of Na+/K+-ATPase. We examined whether blocking of platelet Na+/K+-ATPase by ouabain results in generation of procoagulant activity. It was shown that an in vitro treatment of platelets with ouabain (20-200 µM for 20 to 60 min) is associated with an intracellular accumulation of sodium ([Na+]i), generation of a weak calcium signal, and expression of procoagulant activity. The ouabain-induced procoagulant response was dose- and time-related, less pronounced than that evoked by collagen and similar to that produced by gramicidin, not affected by EDTA or aspirin, and strongly reduced in the absence of extracellular Na+ or by hyperosmolality. Flow cytometry studies revealed that ouabain treatment results in a unimodal left shift in the forward and side scatter of the entire platelet population indicating morphological changes of the plasma membrane. The shift was dose related, weaker than that evoked by collagen and similar to that produced by gramicidin. Ouabain-treated platelets express phosphatidylserine (PS). The ouabain-evoked PS expression was dose- and time-dependent, weaker than that produced by collagen and similar to that evoked by gramicidin. Electronic cell sizing measurements showed a dose-dependent increase in mean platelet volume upon treatment with ouabain. Hypoosmotically-evoked platelet swelling resulted in the appearance of procoagulant activity. Thromboelastography measurements indicate that, in whole blood, nanomolar (50-1000 nM, 15 min) concentrations of ouabain significantly accelerate the rate of clot formation initiated by contact and high extracellular concentration of calcium. We conclude that inefficiently operating platelet Na+/K+-ATPase results in a rise in [Na+]i. An increase in [Na+]i and the swelling associated with it may produce PS exposure and a rise in membrane curvature leading to the generation of a procoagulant activity.
    Źródło:
    Acta Biochimica Polonica; 2007, 54, 3; 625-639
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Protective role of L-methionine against free radical damage of rat brain synaptosomes
    Autorzy:
    Slyshenkov, Vyacheslav
    Shevalye, Anna
    Liopo, Anton
    Wojtczak, Lech
    Powiązania:
    https://bibliotekanauki.pl/articles/1043695.pdf
    Data publikacji:
    2002
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    (Na+,K+)-ATPase
    oxygen free radicals
    brain
    synaptosomes
    tert-butylhydroperoxide
    L-methionine
    Opis:
    Incubation of rat brain synaptosomal/mitochondrial fraction with tert-butylhydroperoxide resulted in accumulation of the lipid peroxidation product, conjugated dienes, damage of the synaptosomal membrane as evidenced by leakage of lactate dehydrogenase, and decrease of the total content of glutathione and of the GSH/GSSG ratio. This treatment also produced a considerable decrease of the ouabain-sensitive ATPase activity and a much smaller diminution of the activities of glutathione reductase and glutathione transferase. Preincubation of the synaptosomal/mitochondrial fraction with 0.5 or 1.0 mM L-methionine significantly protected against lipid peroxidation, membrane damage and changes in the glutathione system produced by low (1 mM) concentrations of tert-butylhydroperoxide and completely prevented inactivation of ouabain-sensitive ATPase, glutathione reductase and glutathione transferase by such treatment. The importance of L-methionine in antioxidant protection is discussed.
    Źródło:
    Acta Biochimica Polonica; 2002, 49, 4; 907-916
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Effects of benzo(a)pyrene exposure on the ATPase activity and calcium concentration in the hippocampus of neonatal rats
    Autorzy:
    Yang, Kai
    Chen, Chengzhi
    Cheng, Shuqun
    Cao, Xianqing
    Tu, Baijie
    Powiązania:
    https://bibliotekanauki.pl/articles/2161850.pdf
    Data publikacji:
    2017-03-30
    Wydawca:
    Instytut Medycyny Pracy im. prof. dra Jerzego Nofera w Łodzi
    Tematy:
    hippocampus
    neurodevelopment
    ATPase activity
    Ca2+ concentration
    neonatal rats
    Benzo(a)pyrene
    Opis:
    Objectives To investigate whether postnatal benzo(a)pyrene (B(a)P) exposure caused the impairments on the process of neurodevelopment and the alteration in the calcium medium in the neonatal rats. Material and Methods Eighty neonatal Sprague Dawley (SD) rats were randomly divided into 5 groups (untreated control group, vehicle group, 0.02 mg/kg, 0.2 mg/kg and 2 mg/kg B(a)P-exposed group). Rats were treated with B(a)P by the intragastric administration from postnatal day (PND) 4 to 25. Morris water maze (MWM) was employed to observe the spatial memory of rats. The activity of calcium adenosine triphosphatase (Ca2+-ATPase), sodium-potassium adenosine triphosphatase (Na+-K+-ATPase) and calcium-magnesium adenosine triphosphatase (Ca2+-Mg2+-ATPase) in the hippocampus were detected by commercial kits. Fura-2 pentakis(acetoxymethyl) (Fura-2/AM) probe and reactive oxygen species (ROS) reagent kit were used for measuring the concentration of Ca2+ and ROS in the hippocampus synapse, respectively. Results Rats exposed to B(a)P resulted in the deficits in the spatial memory manifested by the increased escape latency and decreased number of crossing platform and time spent in target quadrant in comparison with the control groups. Benzo(a)pyrene exposure caused the significant decrease in the ATPase activity in the hippocampus and caused Ca2+ overload in the synaptic, besides, the ROS concentration increased significantly which may further induce neurobehavioral impairment of the neonatal rats. Conclusions Our findings suggest that postnatal B(a)P exposure may cause the neurobehavioral impairments in the neonatal rats, which were mediated by the decreased ATPase activity and elevated Ca2+ concentration. Int J Occup Med Environ Health 2017;30(2):203–211
    Źródło:
    International Journal of Occupational Medicine and Environmental Health; 2017, 30, 2; 203-211
    1232-1087
    1896-494X
    Pojawia się w:
    International Journal of Occupational Medicine and Environmental Health
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Time-dependent effect of leptin on renal Na+,K+-ATPase activity
    Autorzy:
    Marciniak, Andrzej
    Jamroz-Wiśniewska, Anna
    Borkowska, Ewelina
    Bełtowski, Jerzy
    Powiązania:
    https://bibliotekanauki.pl/articles/1041321.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    mitogen-activated protein kinases
    leptin
    obesity
    arterial hypertension
    hydrogen peroxide
    Na+,K+-ATPase
    Opis:
    Leptin, secreted by adipose tissue, is involved in the pathogenesis of arterial hypertension, however, the mechanisms through which leptin increases blood pressure are incompletely elucidated. We investigated the effect of leptin, administered for different time periods, on renal Na+,K+-ATPase activity in the rat. Leptin was infused under anesthesia into the abdominal aorta proximally to the renal arteries for 0.5-3 h. Leptin administered at doses of 1 and 10 µg/min per kg for 30 min decreased the Na+,K+-ATPase activity in the renal medulla. This effect disappeared when the hormone was infused for ≥1 h. Leptin infused for 3 h increased the Na+,K+-ATPase activity in the renal cortex and medulla. The stimulatory effect was abolished by a specific inhibitor of Janus kinases (JAKs), tyrphostin AG490, as well as by an NAD(P)H oxidase inhibitor, apocynin. Leptin increased urinary excretion of hydrogen peroxide (H2O2) between 2 and 3 h of infusion. The effect of leptin on renal Na+,K+-ATPase and urinary H2O2 was augmented by a superoxide dismutase mimetic, tempol, and was abolished by catalase. In addition, infusion of H2O2 for 30 min increased the Na+,K+-ATPase activity. Inhibitors of extracellular signal regulated kinases (ERKs), PD98059 or U0126, prevented Na+,K+-ATPase stimulation by leptin and H2O2. These data indicate that leptin, by acting directly within the kidney, has a delayed stimulatory effect on Na+,K+-ATPase, mediated by JAKs, H2O2 and ERKs. This mechanism may contribute to the abnormal renal Na+ handling in diseases associated with chronic hyperleptinemia such as diabetes and obesity.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 4; 803-809
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Constitutively active guard cell plasma membrane Hplus-ATPase impairs ozone – elevated CO2־ and darkness-induced stomatal closur
    Autorzy:
    Nuhkat, M.
    Roelfsema, M.R.G.
    Kollist, H.
    Powiązania:
    https://bibliotekanauki.pl/articles/81254.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    air pollutant
    plasma membrane
    guard cell
    ATPase
    ozone
    reactive oxygen species
    stomatal conductance
    Źródło:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
    0860-7796
    Pojawia się w:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Reconstitution of ventricular myosin with atrial light chains 1 improves its functional properties.
    Autorzy:
    Khalina, Yana
    Bartsch, Holger
    Petzhold, Daria
    Haase, Hannelore
    Podlubnaya, Zoya
    Shpagina, Mila
    Morano, Ingo
    Powiązania:
    https://bibliotekanauki.pl/articles/1041425.pdf
    Data publikacji:
    2005
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    myosin light chains
    cardiac myosin
    dilated cardiomyopathy
    myosin filaments
    reconstituted myosin
    actin-activated ATPase activity
    Opis:
    Atrial light chain 1 (ALC-1) is expressed in embryonic and hypertrophied human ventricles but not in normal adult human ventricles. We investigated the effects of recombinant human atrial light chains (hALC-1) on the structure and enzymatic activity of synthetic filaments of ventricular myosin. The endogenous ventricular myosin light chain 1 (VLC-1) was partially replaced by recombinant hALC-1 yielding hALC-1 levels of 12%, 24% and 42%. This reconstitution of ventricular myosin with hALC-1 did not change the length of synthetic myosin filaments but led to more rounded myosin heads in comparison with those of control filaments. Actin-activated ATPase activity of myosin, a parameter of functional activity of molecular motor, amounted to 79.5 nmol Pi/mg per min in control myosin filaments. Reconstitution with hALC-1 caused a profound increase of the actin-activated myosin ATPase activity in a dose dependent manner, for example, synthetic myosin filaments formed with 12%, 24% and 42% hALC-1 reconstituted myosin revealed the actin-activated ATPase activity increased by 18%, 26% and 36%, respectively, as compared to control. These results strongly suggest that in vivo expression of ALC-1 enhances ventricular myosin function, thereby contributing to cardiac compensation.
    Źródło:
    Acta Biochimica Polonica; 2005, 52, 2; 443-448
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Bidirectional regulation of renal cortical Na+,K+-ATPase by protein kinase C.
    Autorzy:
    Bełtowski, Jerzy
    Marciniak, Andrzej
    Jamroz-Wiśniewska, Anna
    Borkowska, Ewelina
    Wójcicka, Grażyna
    Powiązania:
    https://bibliotekanauki.pl/articles/1041555.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    phosphatidylinositol-3-kinase
    protein kinase C
    cytochrome P450-dependent arachidonate metabolites
    Na+,K+-ATPase
    Opis:
    We examined the role of protein kinase C (PKC) in the regulation of Na+,K+- ATPase activity in the renal cortex. Male Wistar rats were anaesthetized and the investigated reagents were infused into the abdominal aorta proximally to the renal arteries. A PKC-activating phorbol ester, phorbol 12,13-dibutyrate (PDBu), had a dose-dependent effect on cortical Na+,K+-ATPase activity. Low dose of PDBu (10-11 mol/kg per min) increased cortical Na+,K+-ATPase activity by 34.2%, whereas high doses (10-9 and 10-8 mol/kg per min) reduced this activity by 22.7% and 35.0%, respectively. PDBu administration caused changes in Na+,K+-ATPase Vmax without affecting K0.5 for Na+, K+ and ATP as well as Ki for ouabain. The effects of PDBu were abolished by PKC inhibitors, staurosporine, GF109203X, and Gö 6976. The inhibitory effect of PDBu was reversed by pretreatment with inhibitors of cytochrome P450-dependent arachidonate metabolism, ethoxyresorufin and 17-octadecynoic acid, inhibitors of phosphatidylinositol 3-kinase (PI3K), wortmannin and LY294002, and by actin depolymerizing agents, cytochalasin D and latrunculin B. These results suggest that PKC may either stimulate or inhibit renal cortical Na+,K+-ATPase. The inhibitory effect is mediated by cytochrome P450-dependent arachidonate metabolites and PI3K, and is caused by redistribution of the sodium pump from the plasma membrane to the inactive intracellular pool.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 3; 757-772
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Functional conservation between yeast and plant mitochondrial m-AAA proteases
    Autorzy:
    Skibior, R.
    Kolodziejczak, M.
    Janska, H.
    Powiązania:
    https://bibliotekanauki.pl/articles/80313.pdf
    Data publikacji:
    2013
    Wydawca:
    Polska Akademia Nauk. Czytelnia Czasopism PAN
    Tematy:
    conference
    FtsH protease
    bifunctional enzyme
    ATPase
    plant mitochondrion
    yeast
    AAA protease
    Arabidopsis
    ribosomal subunit
    immunoblotting
    biogenesis
    Źródło:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
    0860-7796
    Pojawia się w:
    BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Structural basis of the interspecies interaction between the chaperone DnaK(Hsp70) and the co-chaperone GrpE of archaea and bacteria
    Autorzy:
    Żmijewski, Michał
    Skórko-Glonek, Joanna
    Tanfani, Fabio
    Banecki, Bogdan
    Kotlarz, Agnieszka
    Macario, Alberto
    Lipińska, Barbara
    Powiązania:
    https://bibliotekanauki.pl/articles/1041069.pdf
    Data publikacji:
    2007
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    substrate-binding domain
    DnaK-GrpE complex
    archaeal Hsp70(DnaK)
    archaeal DnaK structure
    molecular chaperones
    ATPase domain
    Opis:
    Hsp70s are chaperone proteins that are conserved in evolution and present in all prokaryotic and eukaryotic organisms. In the archaea, which form a distinct kingdom, the Hsp70 chaperones have been found in some species only, including Methanosarcina mazei. Both the bacterial and archaeal Hsp70(DnaK) chaperones cooperate with a GrpE co-chaperone which stimulates the ATPase activity of the DnaK protein. It is currently believed that the archaeal Hsp70 system was obtained by the lateral transfer of chaperone genes from bacteria. Our previous finding that the DnaK and GrpE proteins of M. mazei can functionally cooperate with the Escherichia coli GrpE and DnaK supported this hypothesis. However, the cooperation was surprising, considering the very low identity of the GrpE proteins (26%) and the relatively low identity of the DnaK proteins (56%). The aim of this work was to investigate the molecular basis of the observed interspecies chaperone interaction. Infrared resolution-enhanced spectra of the M. mazei and E. coli DnaK proteins were almost identical, indicating high similarity of their secondary structures, however, some small differences in band position and in the intensity of amide I' band components were observed and discussed. Profiles of thermal denaturation of both proteins were similar, although they indicated a higher thermostability of the M. mazei DnaK compared to the E. coli DnaK. Electrophoresis under non-denaturing conditions demonstrated that purified DnaK and GrpE of E. coli and M. mazei formed mixed complexes. Protein modeling revealed high similarity of the 3-dimensional structures of the archaeal and bacterial DnaK and GrpE proteins.
    Źródło:
    Acta Biochimica Polonica; 2007, 54, 2; 245-252
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
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