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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:
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:
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:
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:
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:
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:
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:
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:
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:
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:
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:
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:
Respiratory surveillance and Caplus-ATPase enzyme activity studies of Clarias gariepinus exposed to acute toxicity of cyanide
Autorzy:
Oseni, K.
Powiązania:
https://bibliotekanauki.pl/articles/10785.pdf
Data publikacji:
2016
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Opis:
Potassium cyanide, a highly contaminating and toxic aquatic ecosystems pollutant was investigated for acute toxicity on the freshwater fish Clarias gariepinus. Its effect on the Ca2+ - ATPase activities in the liver, gills, muscle and intestinal tissues and oxygen consumption index was studied. Short-term toxicity test was carried out by static renewal bioassay test over a 96 h period using a lethal concentration (LC50) value of 0.361mg/mL. Potassium cyanide was highly toxic to the animal tested. Results reveal that normal respiratory activity (O2 consumption) of the fish was significantly affected and there was significant decreased in the Ca2+ - ATPase activities at the end of exposure periods (24, 48, 72 and 96 h). Correlation analysis reveals a strong relationship between oxygen consumption index and ATPase enzyme activity of Clarias gariepinus exposed to the toxicant. This study reflects the toxic effect of potassium cyanide to the freshwater fish, Clarias gariepinus and suggestion on the possible application of Ca2+ -ATPase activities and oxygen consumption index as possible biomarkers for early detection of cyanide poisoning in aquatic bodies.
Źródło:
International Letters of Natural Sciences; 2016, 50
2300-9675
Pojawia się w:
International Letters of Natural Sciences
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:
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:
Na^+K^+-ATPase activity of rabbit kidney cortex membranes in ischemia and reperfusion
Autorzy:
Aydin, Selvin
Aricioglu, Aysel
Turkozkan, Nurten
Bingol, Fuat
Aydin, Coskun
Powiązania:
https://bibliotekanauki.pl/articles/1045448.pdf
Data publikacji:
1993
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1993, 40, 4; 545-547
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Na+, K+ -ATPase activity and ATP concentration in horses of the Wielkopolski breed in relation to age
Autorzy:
Suska, M.
Brucka-Jastrzebska, E.
Kawczuga, D.
Powiązania:
https://bibliotekanauki.pl/articles/32121.pdf
Data publikacji:
2011
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Opis:
This study aimed at determining relationships between the age of the Wielkopolski horses, ATP in whole blood and in the erythrocytes, and between erythrocyte Na+, K+-ATPase activity, and serum concentrations of mineral components. ATP was measured in whole blood and in erythrocytes by HPLC method. Serum concentrations of Ca²⁺ and Mg²⁺ were measured spectrophotometrically, while Na+ and K+ by flame photometry. In horses aged from 4 to 48 months, a dynamic decrease in ATP activity was found. Erythrocyte Na+, K+-ATPase activity decreased proportionally with the decrease in ATP activity. The results of this study may enable planning physical effort of horses at optimum use of energetic efficiency of their erythrocytes and mineral components in relation to their age.
Źródło:
Polish Journal of Veterinary Sciences; 2011, 14, 4
1505-1773
Pojawia się w:
Polish Journal of Veterinary Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Interactions between the gene products of pma1 encoding plasma membrane H^+-ATPase, and pdr1 controlling multiple drug resistance in Saccharomyces cereivisiae
Autorzy:
Ułaszewski, Stanisław
Powiązania:
https://bibliotekanauki.pl/articles/1045440.pdf
Data publikacji:
1993
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1993, 40, 4; 487-496
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Acute and sub lethal effect of potassium cyanide on the behaviour and ATPase enzyme activity in the freshwater fish, Clarias gariepinus (Catfish)
Autorzy:
Oseni, K.
Powiązania:
https://bibliotekanauki.pl/articles/11608.pdf
Data publikacji:
2015
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Opis:
The Present research studies the acute sub lethal toxicity of potassium cyanide (KCN) in the fresh water, Clarias gariepinus and the effects on its behaviour and the Na+ - K+ ATPase enzyme activity. Acute toxicity of potassium cyanide (free cyanide) to the freshwater fish was studied using static bioassay method over a period of 96 h. Different concentrations of the toxicant (KCN) were used and LC50 value was found to be 361μg/L. Behavioural changes when exposed to lethal concentration of KCN showed increased feed intake, cannibalism, irregular swimming activity, rapid jerk movement, aggressiveness, loss of balance, opercula movement, surface behaviour, loss of equilibrium, change in body colour and convulsion. The effect of potassium on the Na+ - K+ ATPase of various physiological tissues which includes the gill, liver, muscles and intestinal over duration 0f 12 h- 35 days were also studied. Cyanide intoxication resulted in marked changes in ATPase, shown by significant decrease in the enzyme activities. The result shows that ATPase enzyme together could be employed as a sensitive and useful biomarkers for cyanide pollution while the behavioural changes could be an early signal of toxicity.
Źródło:
International Letters of Natural Sciences; 2015, 49
2300-9675
Pojawia się w:
International Letters of Natural Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Is the glutathione conjugate of trans-4-hydroxy-2-nonenal transported by the multispecific organic anion transporting-ATPase of human erythrocytes?
Autorzy:
Dygas, Anna
Makowski, Piotr
Pikuła, Sławomir
Powiązania:
https://bibliotekanauki.pl/articles/1044853.pdf
Data publikacji:
1998
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1998, 45, 1; 59-65
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Circular dichroism and fluorescence studies on interaction of calmodulin (CaM) with purified (Ca^2+-Mg^2+) ATPase of erythrocyte ghosts
Autorzy:
Wrzosek, Antoni
Famulski, Konrad
Pikuła, Sławomir
Powiązania:
https://bibliotekanauki.pl/articles/1045812.pdf
Data publikacji:
1990
Wydawca:
Polskie Towarzystwo Biochemiczne
Źródło:
Acta Biochimica Polonica; 1990, 37, 1; 173-176
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The structure of the Ca2+-ATPase of sarcoplasmic reticulum.
Autorzy:
Martonosi, Anthony
Pikula, Slawomir
Powiązania:
https://bibliotekanauki.pl/articles/1043610.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
calcium pump
calcium homeostasis
calcium transport
skeletal and cardiac muscles
sarcoplasmic reticulum
excitation-contraction coupling
Opis:
In this article the morphology of sarcoplasmic reticulum, classification of Ca2+-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology will be reviewed. The focus is on the structure and interactions of Ca2+-ATPase determined by electron and X-ray crystallography, lamellar X-ray and neutron diffraction analysis of the profile structure of Ca2+-ATPase in sarcoplasmic reticulum multilayers. In addition, targeting of the Ca2+-ATPase to the sarcoplasmic reticulum is discussed.
Źródło:
Acta Biochimica Polonica; 2003, 50, 2; 337-365
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Kinetic properties of the (Ca²+ + Mg²+)-ATPase bound to and extracted from the pig erythrocyte membrane
Własności kinetyczne (Ca²+ + Mg²+)-ATPazy związanej z błonami erytrocytów świni i ekstrahowanej z nich
Autorzy:
Błasiak, Janusz
Powiązania:
https://bibliotekanauki.pl/articles/945007.pdf
Data publikacji:
1996
Wydawca:
Uniwersytet Łódzki. Wydawnictwo Uniwersytetu Łódzkiego
Źródło:
Acta Universitatis Lodziensis. Folia Biochimica et Biophysica; 1996, 11
0208-614X
Pojawia się w:
Acta Universitatis Lodziensis. Folia Biochimica et Biophysica
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:
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
Wyświetlanie 1-25 z 33

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