scholarly journals Effects of detergents on Na+ + K+-dependent ATPase activity in plasma-membrane fractions prepared from frog muscles. Studies of insulin action on Na+ and K+ transport

1987 ◽  
Vol 246 (3) ◽  
pp. 583-588 ◽  
Author(s):  
M Omatsu-Kanbe ◽  
H Kitasato
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Skeletal Muscles ◽  
Rana Catesbeiana ◽  
Insulin Binding ◽  
Maximum Activity ◽  
Detergent Concentration ◽  
Control Value ◽  
Dependent Atpase ◽  
K Transport

The increase in Na+/K+ transport activity in skeletal muscles exposed to insulin was analysed. Plasma-membrane fractions were prepared from frog (Rana catesbeiana) skeletal muscles, and examination of the Na,K-ATPase (Na+ + K+-dependent ATPase) activity showed that it was insensitive to ouabain. In contrast, plasma-membrane fractions prepared from ouabain-pretreated muscles, by the same procedures, showed extremely low Na,K-ATPase activity. On adding saponin to the membrane suspension, the Na,K-ATPase activity increased, according to the detergent concentration. The maximum activity was about twice the control value, at 0.33 mg of saponin/mg of protein. Thus saponin makes vesicle membranes leaky, allowing ouabain in assay solutions to reach receptors on the inner surface of vesicles. Addition of insulin to saponin-treated membrane suspensions had no effect on the Na,K-ATPase activity, whereas the maximum activity of Na,K-ATPase in whole muscles was stimulated by exposure to insulin. The results show that the stimulation of Na+/K+ transport by insulin is not directly due to insulin binding to receptors on the cell surface, but rather support the view that the increase in the Na,K-ATPase induced by insulin requires an alteration of intracellular events.

scholarly journals Cytochemical localization of ecto-ATPases in rat neurohypophysis.

1996 ◽  
Vol 44 (2) ◽  
pp. 103-111 ◽  
Author(s):  
S Thirion ◽  
J D Troadec ◽  
G Nicaise
Keyword(s):  
Electron Microscopy ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Outer Surface ◽  
Nerve Endings ◽  
Glutaraldehyde Fixation ◽  
Cytochemical Localization ◽  
Cytochemical Method ◽  
Ca Pump ◽  
Dependent Atpase

We studied the distribution of Ca(2+)- or Mg(2+)-dependent ATPase activity in rat neurohypophysis using the lead cytochemical method of Ando et al. In electron microscopy, precipitates were found lining the outer surface of the plasma membrane surrounding nerve endings and pituicytes. These precipitates were believed to represent the activity of ecto-ATPases (as opposed to Ca pump ATPases) for the following reasons: there was equal activation by Ca2+ in the absence of Mg2+ or Mg2+ in the absence of Ca2+; the effects of the two ions were not additive; there was activation by ATP or GTP; and there was resistance to glutaraldehyde fixation, to high (10 mM) Ca2+ concentrations, and to various inhibitors such as NEM, vanadate, oligomycin, quercetin, p-chloromercuribenzoate, ouabain, and levamisole. Cytosolic activity observed in certain nerve endings in the same conditions of incubation but more sensitive to NEM is also described and discussed.

scholarly journals Alteration of sarcoplasmic reticulum after denervation of chicken pectoralis muscle

1983 ◽  
Vol 210 (2) ◽  
pp. 339-344 ◽  
Author(s):  
C A Tate ◽  
R J Bick ◽  
T D Myers ◽  
B J R Pitts ◽  
W B Van Winkle ◽  
...  
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Atpase Activity ◽  
Protein Profile ◽  
Pectoralis Muscle ◽  
Denervated Muscle ◽  
Single Class ◽  
Adult Chicken ◽  
Control Value ◽  
Dependent Atpase ◽  
Fast Twitch

To determine the neural influence on the function of the sarcoplasmic reticulum (SR) of fast-twitch skeletal muscle, the superior pectoralis muscle of adult chicken was denervated, and the SR was isolated at 20 days post-denervation. The isolated SR was probably derived from the longitudinal SR and was relatively free of contaminants. The protein profile of the SR was quantitatively changed after denervation with an increase in the M55 and 30000-mol.wt. proteins relative to the Ca2+-ATPase. Ca2+-dependent ATPase activity and phosphoenzyme formation were lower in the denervated-muscle SR; however, the enzyme catalytic-centre activity was similar to the control value. The decrease in Ca2+-ATPase activity in denervated-muscle SR was accompanied by a lower Ca2+ accumulation so that the relationship between Ca2+ accumulation and Ca2+-dependent ATPase activity was well maintained in the SR from denervated muscle. The data imply that denervation may result in a diminution of functional Ca2+ pump sites. Evidence is presented, though, which suggests that denervation affects a single class of Ca2+-binding sites of the Ca2+-ATPase, resulting in a lower affinity for Ca2+.

scholarly journals Inhibitory antibodies to plasmalemmal Ca2+-transporting ATPases. Their use in subcellular localization of (Ca2+ + Mg2+)-dependent ATPase activity in smooth muscle

1985 ◽  
Vol 231 (3) ◽  
pp. 737-742 ◽  
Author(s):  
J Verbist ◽  
F Wuytack ◽  
L Raeymaekers ◽  
R Casteels
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Muscle ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Membrane Fraction ◽  
Transport Atpase ◽  
Calmodulin Binding ◽  
Dependent Atpase ◽  
Inhibitory Antibodies ◽  
Stimulation Of

Antibodies directed against the purified calmodulin-binding (Ca2+ + Mg2+)-ATPase [(Ca2+ + Mg2+)-dependent ATPase] from pig erythrocytes and from smooth muscle of pig stomach (antral part) were raised in rabbits. Both the IgGs against the erythrocyte (Ca2+ + Mg2+)-ATPase and against the smooth-muscle (Ca2+ + Mg2+)-ATPase inhibited the activity of the purified calmodulin-binding (Ca2+ + Mg2+)-ATPase from smooth muscle. Up to 85% of the total (Ca2+ + Mg2+)-ATPase activity in a preparation of KCl-extracted smooth-muscle membranes was inhibited by these antibodies. The (Ca2+ + Mg2+)-ATPase activity and the Ca2+ uptake in a plasma-membrane-enriched fraction from this smooth muscle were inhibited to the same extent, whereas in an endoplasmic-reticulum-enriched membrane fraction the (Ca2+ + Mg2+)-ATPase activity was inhibited by only 25% and no effect was observed on the oxalate-stimulated Ca2+ uptake. This supports the hypothesis that, in pig stomach smooth muscle, two separate types of Ca2+-transport ATPase exist: a calmodulin-binding ATPase located in the plasma membrane and a calmodulin-independent one present in the endoplasmic reticulum. The antibodies did not affect the stimulation of the (Ca2+ + Mg2+)-ATPase activity by calmodulin.

Ca2+-dependent ATPase activity of alveolar macrophage plasma membrane

1979 ◽  
Vol 567 (1) ◽  
pp. 238-246 ◽  
Author(s):  
R. Gennaro ◽  
C. Mottola ◽  
C. Schneider ◽  
D. Romeo
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Alveolar Macrophage ◽  
Dependent Atpase

Tricyclic Antidepressants Inhibit the Ca2+-Dependent ATPase Activity from Plasma Membrane

1999 ◽  
Vol 370 (1) ◽  
pp. 119-125 ◽  
Author(s):  
Fernando Plenge-Tellechea ◽  
Fernando Soler ◽  
Francisco Fernandez-Belda
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Tricyclic Antidepressants ◽  
Dependent Atpase

Localization of Adenosine Triphosphatase Activity in the Phleom of Nicotiana Tabacum

1972 ◽  
Vol 30 ◽  
pp. 230-231
Author(s):  
James Cronshaw ◽  
Jamison E. Gilder
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Higher Plants ◽  
High Surface ◽  
Root Tip ◽  
Animal Cells ◽  
Physiological Processes ◽  
Tip Cells ◽  
Atpase Localization

Adenosine triphosphatase (ATPase) activity has been shown to be associated with numerous physiological processes in both plants and animal cells. Biochemical studies have shown that in higher plants ATPase activity is high in cell wall preparations and is associated with the plasma membrane, nuclei, mitochondria, chloroplasts and lysosomes. However, there have been only a few ATPase localization studies of higher plants at the electron microscope level. Poux (1967) demonstrated ATPase activity associated with most cellular organelles in the protoderm cells of Cucumis roots. Hall (1971) has demonstrated ATPase activity in root tip cells of Zea mays. There was high surface activity largely associated with the plasma membrane and plasmodesmata. ATPase activity was also demonstrated in mitochondria, dictyosomes, endoplasmic reticulum and plastids.

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