Increased Circulating Na+-K+-Atpase Inhibitor in the Young and Adult Milan Hypertensive Strain Rat

1986 ◽  
Vol 70 (s13) ◽  
pp. 58P-58P ◽  
Author(s):  
J. Alaghband-Zadeh ◽  
S.M. Holland ◽  
J.A. Millett ◽  
H.E. de Wardener ◽  
P. Ferrari ◽  
...  
Keyword(s):  
Atpase Inhibitor ◽  
Hypertensive Strain

scholarly journals Characterization and partial purification of the sodium-potassium-ATPase inhibitor released from cultured rat hypothalamic cells.

1985 ◽  
Vol 260 (25) ◽  
pp. 13595-13600 ◽  
Author(s):  
K Morgan ◽  
M D Lewis ◽  
G Spurlock ◽  
P A Collins ◽  
S M Foord ◽  
...  
Keyword(s):  
Partial Purification ◽  
Atpase Inhibitor ◽  
Sodium Potassium ◽  
Hypothalamic Cells ◽  
Potassium Atpase

scholarly journals Multi-Tissue Transcriptomic-Informed In Silico Investigation of Drugs for the Treatment of Dengue Fever Disease

Viruses ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1540
Author(s):  
Beatriz Sierra ◽  
Ana Cristina Magalhães ◽  
Daniel Soares ◽  
Bruno Cavadas ◽  
Ana B. Perez ◽  
...  
Keyword(s):  
Receptor Antagonist ◽  
Dengue Fever ◽  
In Silico ◽  
Serotonin Receptor ◽  
Neglected Tropical Diseases ◽  
Dengue Infection ◽  
Severe Dengue ◽  
Functional Evaluation ◽  
Atpase Inhibitor ◽  
Serotonin Receptor Antagonist

Transcriptomics, proteomics and pathogen-host interactomics data are being explored for the in silico–informed selection of drugs, prior to their functional evaluation. The effectiveness of this kind of strategy has been put to the test in the current COVID-19 pandemic, and it has been paying off, leading to a few drugs being rapidly repurposed as treatment against SARS-CoV-2 infection. Several neglected tropical diseases, for which treatment remains unavailable, would benefit from informed in silico investigations of drugs, as performed in this work for Dengue fever disease. We analyzed transcriptomic data in the key tissues of liver, spleen and blood profiles and verified that despite transcriptomic differences due to tissue specialization, the common mechanisms of action, “Adrenergic receptor antagonist”, “ATPase inhibitor”, “NF-kB pathway inhibitor” and “Serotonin receptor antagonist”, were identified as druggable (e.g., oxprenolol, digoxin, auranofin and palonosetron, respectively) to oppose the effects of severe Dengue infection in these tissues. These are good candidates for future functional evaluation and clinical trials.

Regulation of cytosolic free Ca2+ concentration in acinar cells of rat pancreas

1983 ◽  
Vol 245 (3) ◽  
pp. G347-G357 ◽  
Author(s):  
H. Streb ◽  
I. Schulz
Keyword(s):  
Steady State ◽  
Incubation Medium ◽  
Minimal Medium ◽  
Acinar Cells ◽  
Pancreatic Acinar Cells ◽  
Atpase Inhibitor ◽  
Rat Pancreas ◽  
Mitochondrial Inhibitors ◽  
Pancreatic Cells ◽  
State Concentration

Ca2+ uptake into isolated exocrine pancreatic cells with highly permeable plasma membrane was determined by measuring the decrease in free Ca2+ concentration of the surrounding incubation medium with a Ca2+-specific electrode. In the presence of Mg-ATP and respiratory substrates the free Ca2+ concentration of the incubation medium decreased rapidly after addition of leaky cells until a stable medium free Ca2+ concentration of 4.2 +/- 0.1 X 10(-7) mol/l was obtained. Changes in the medium free Ca2+ concentration at steady state by addition of Ca2+ or EGTA were buffered by cellular uptake or release, respectively, until the steady-state free Ca2+ concentration was reestablished. When nonmitochondrial Ca2+ uptake was determined in the presence of a combination of mitochondrial inhibitors (10(-5) mol/l antimycin, 5 X 10(-6) mol/l oligomycin, and 10(-2) mol/l azide), the rate of uptake was considerably reduced, while the steady-state concentration was unaltered. In contrast, mitochondrial uptake that could be observed in the presence of the ATPase inhibitor vanadate (2 X 10(-3) mol/l) proceeded at the same rate as the control, but the minimal medium free Ca2+ concentration reached was 2.4 +/- 0.1 X 10(-7) mol/l higher than the control. Addition of secretagogues at steady-state free Ca2+ concentration resulted in a Ca2+ release of 0.73 +/- 0.08 nmol/mg protein. The increase in medium free Ca2+ concentration was entirely transient and followed by reuptake to the prestimulation level. The data indicate that a cytosolic free Ca2+ concentration of 4 X 10(-7) mol/l can be regulated in pancreatic acinar cells by a nonmitochondrial Mg2+-dependent Ca2+ pool.

Contraction-related stimuli regulate GLUT4 traffic in C2C12-GLUT4myc skeletal muscle cells

2010 ◽  
Vol 298 (5) ◽  
pp. E1058-E1071 ◽  
Author(s):  
Wenyan Niu ◽  
Philip J. Bilan ◽  
Shuhei Ishikura ◽  
Jonathan D. Schertzer ◽  
Ariel Contreras-Ferrat ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Surface ◽  
Glucose Uptake ◽  
Nicotinic Acetylcholine Receptors ◽  
Cell Model ◽  
Cytosolic Calcium ◽  
Atpase Inhibitor ◽  
Cellular Models ◽  
Compound C

Muscle contraction stimulates glucose uptake acutely to increase energy supply, but suitable cellular models that faithfully reproduce this complex phenomenon are lacking. To this end, we have developed a cellular model of contracting C2C12 myotubes overexpressing GLUT4 with an exofacial myc-epitope tag (GLUT4 myc) and explored stimulation of GLUT4 traffic by physiologically relevant agents. Carbachol (an acetylcholine receptor agonist) induced a gain in cell surface GLUT4 myc that was mediated by nicotinic acetylcholine receptors. Carbachol also activated AMPK, and this response was sensitive to the contractile myosin ATPase inhibitor N-benzyl- p-toluenesulfonamide. The gain in surface GLUT4 myc elicited by carbachol or by the AMPK activator 5-amino-4-carboxamide-1 β-ribose was sensitive to chemical inhibition of AMPK activity by compound C and partially reduced by siRNA-mediated knockdown of AMPK catalytic subunits or LKB1. In addition, the carbachol-induced gain in cell surface GLUT4 myc was partially sensitive to chelation of intracellular calcium with BAPTA-AM. However, the carbachol-induced gain in cell surface GLUT4 myc was not sensitive to the CaMKK inhibitor STO-609 despite expression of both isoforms of this enzyme and a rise in cytosolic calcium by carbachol. Therefore, separate AMPK- and calcium-dependent signals contribute to mobilizing GLUT4 in response to carbachol, providing an in vitro cell model that recapitulates the two major signals whereby acute contraction regulates glucose uptake in skeletal muscle. This system will be ideal to further analyze the underlying molecular events of contraction-regulated GLUT4 traffic.

Inhibition of muscle actomyosin ATPase activity by mitochondrial ATPase inhibitor

1977 ◽  
Vol 75 (4) ◽  
pp. 1104-1110 ◽  
Author(s):  
Shojiro Yamazaki ◽  
Hiroshi Hasebe ◽  
Haruhiko Takisawa ◽  
Yutaka Tamaura ◽  
Yuji Inada
Keyword(s):  
Atpase Activity ◽  
Mitochondrial Atpase ◽  
Atpase Inhibitor ◽  
Actomyosin Atpase

scholarly journals Retrograde Transport from the Pre-Golgi Intermediate Compartment and the Golgi Complex Is Affected by the Vacuolar H+-ATPase Inhibitor Bafilomycin A1

1998 ◽  
Vol 9 (12) ◽  
pp. 3561-3578 ◽  
Author(s):  
Harri Palokangas ◽  
Ming Ying ◽  
Kalervo Väänänen ◽  
Jaakko Saraste
Keyword(s):  
Brefeldin A ◽  
Retrograde Transport ◽  
Small Gtpase ◽  
Bafilomycin A1 ◽  
Atpase Inhibitor ◽  
Marker Proteins ◽  
Golgi Region ◽  
Intermediate Compartment ◽  
Acidic Compartments

The effect of the vacuolar H+-ATPase inhibitor bafilomycin A1 (Baf A1) on the localization of pre-Golgi intermediate compartment (IC) and Golgi marker proteins was used to study the role of acidification in the function of early secretory compartments. Baf A1 inhibited both brefeldin A- and nocodazole-induced retrograde transport of Golgi proteins to the endoplasmic reticulum (ER), whereas anterograde ER-to-Golgi transport remained largely unaffected. Furthermore, p58/ERGIC-53, which normally cycles between the ER, IC, and cis-Golgi, was arrested in pre-Golgi tubules and vacuoles, and the number of p58-positive ∼80-nm Golgi (coatomer protein I) vesicles was reduced, suggesting that the drug inhibits the retrieval of the protein from post-ER compartments. In parallel, redistribution of β-coatomer protein from the Golgi to peripheral pre-Golgi structures took place. The small GTPase rab1p was detected in short pre-Golgi tubules in control cells and was efficiently recruited to the tubules accumulating in the presence of Baf A1. In contrast, these tubules showed no enrichment of newly synthesized, anterogradely transported proteins, indicating that they participate in retrograde transport. These results suggest that the pre-Golgi structures contain an active H+-ATPase that regulates retrograde transport at the ER–Golgi boundary. Interestingly, although Baf A1 had distinct effects on peripheral pre-Golgi structures, only more central, p58-containing elements accumulated detectable amounts of 3-(2,4-dinitroanilino)-3′-amino-N-methyldipropylamine (DAMP), a marker for acidic compartments, raising the possibility that the lumenal pH of the pre-Golgi structures gradually changes in parallel with their translocation to the Golgi region.

scholarly journals Biological activity of partially purified digitalis-like substance and Na-K-ATPase inhibitor in rats.

1988 ◽  
Vol 52 (11) ◽  
pp. 1309-1316 ◽  
Author(s):  
TOSHIO MORISE ◽  
SHINYA OKAMOTO ◽  
HIDEAKI TAKASAKI ◽  
MASATOSHI IKEDA ◽  
RYOYU TAKEDA ◽  
...  
Keyword(s):  
Biological Activity ◽  
Atpase Inhibitor

scholarly journals Amplification of the thapsigargin-evoked increase in the cytosolic free Ca2+ concentration by acetylcholine in acutely isolated mouse submandibular acinar cells

1996 ◽  
Vol 317 (3) ◽  
pp. 779-783 ◽  
Author(s):  
Peter. M. SMITH ◽  
Helen. E. REED
Keyword(s):  
Plasma Membrane ◽  
Time Course ◽  
Acinar Cells ◽  
Fold Increase ◽  
Extrusion Process ◽  
Significant Alteration ◽  
Atpase Inhibitor ◽  
Fura 2

The intracellular Ca2+ concentration was measured in single, acutely isolated, mouse submandibular acinar cells loaded with fura-2 AM. All experiments were performed in the absence of extracellular Ca2+ in order to eliminate Ca2+ influx. The microsomal ATPase inhibitor, thapsigargin, was used to release Ca2+ from intracellular stores and simultaneously prevent re-uptake into the stores. Sequential application of thapsigargin (2 μM) and the Ca2+ ionophore ionomycin (500 nM) indicated that thapsigargin was able to mobilize practically all intracellular Ca2+. Furthermore, in comparison with results obtained following inhibition of the plasma membrane Ca2+-ATPase by La3+ (2 mM), it may be shown that slowly unloading the intracellular Ca2+ stores using thapsigargin does not normally cause a massive, cytotoxic, increase in the cytosolic Ca2+ concentration, because Ca2+ is rapidly extruded from the cell across the plasma membrane. Application of a submaximal dose of acetylcholine (500 nM) during the rising phase of the response to thapsigargin caused a 3–4-fold increase in the amplitude of the rise in the cytosolic Ca2+ concentration without any significant alteration of the time course of the response. As thapsigargin alone is capable of mobilizing all releasable Ca2+, this increase in amplitude is most likely the result of inhibition of the Ca2+ extrusion process by acetylcholine.

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