scholarly journals D11 Cell membrane cation transport systems during aldosterone antagonism

1997 ◽  
Vol 10 (4) ◽  
pp. 41A
Author(s):  
P LIJNEN
Keyword(s):  
Cell Membrane ◽  
Cation Transport ◽  
Transport Systems ◽  
Aldosterone Antagonism

Bumetanide inhibits (Na + K + 2Cl) co-transport at a chloride site

1983 ◽  
Vol 245 (3) ◽  
pp. C235-C240 ◽  
Author(s):  
M. Haas ◽  
T. J. McManus
Keyword(s):  
Cell Membrane ◽  
Blood Cell ◽  
Response Curve ◽  
Cation Transport ◽  
Transport Systems ◽  
Constant Ratio ◽  
Common Site ◽  
Transport Pathway ◽  
Maximal Inhibition ◽  
Number Of Cells

Chloride-dependent cation transport systems in a number of cells and tissues are inhibited by 5-sulfamoylbenzoic acid loop diuretics, such as furosemide and bumetanide. Interactions between chloride and bumetanide have been examined in the catecholamine-activated (Na + K + 2Cl) co-transport pathway of the duck red blood cell. Levels of chloride were varied while maintaining a constant ratio of internal to external chloride across the cell membrane. Increasing external chloride from 20 to 100 mM shifted the dose-response curve for the effect of bumetanide on co-transport toward higher concentrations of the drug. The bumetanide concentration producing half-maximal inhibition (IC50) was increased from approximately 6 X 10(-8) to approximately 2 X 10(-7) M. When cells were incubated in the presence of a constant, submaximal inhibitory dose of bumetanide (10(-8) M), increasing external chloride (in increments of 20 mM) from 20 to 140 mM progressively decreased the level of inhibition of the co-transport system. Kinetic analysis of the data demonstrates that bumetanide and chloride compete for a common site.

Erythrocyte Cation Transport Systems and Membrane Lipids in Insulin-Dependent Diabetics

1993 ◽  
Vol 6 (9) ◽  
pp. 763-770 ◽  
Author(s):  
P. Lijnen ◽  
A. Fenyvesi ◽  
M. Bex ◽  
R. Bouillon ◽  
A. Amery
Keyword(s):  
Membrane Lipids ◽  
Cation Transport ◽  
Transport Systems ◽  
Insulin Dependent

scholarly journals CATION TRANSPORT IN YEAST

1956 ◽  
Vol 39 (5) ◽  
pp. 687-704 ◽  
Author(s):  
Ernest C. Foulkes
Keyword(s):  
Cell Membrane ◽  
Dissociation Constant ◽  
Concentration Gradient ◽  
Cation Transport ◽  
K Uptake ◽  
Present Evidence ◽  
Inhibitor Complex ◽  
Maximum Value ◽  
Low Concentrations ◽  
K Transport

1. The distribution of azide added to suspensions of bakers' yeast was studied under various conditions. The recovery of azide was estimated in the volume of water into which low concentrations of electrolytes can readily diffuse (anion space). Considerable azide disappeared from this anion space. 2. The incomplete recovery of azide in the anion space is due to its uptake by the cells. This uptake occurs against a concentration gradient at 0°C., and is attributed to binding of azide by cell constituents. 3. Confirmatory evidence is presented that one such constituent is the K carrier in the cell membrane. The azide inhibition of K transport is not mediated by inhibition of cytochrome oxidase in the mitochondria. 4. From the amount of combined azide and the experimentally determined dissociation constant of the K carrier-inhibitor complex, the maximum value for the concentration of this carrier is calculated as 0.1 µM/gm. yeast. 5. The addition of glucose and PO4 causes a secondary K uptake which is not azide-sensitive and is clearly distinct from the primary, azide-sensitive mechanism. 6. The existence of a separate carrier responsible for Na extrusion is reconsidered. It is concluded that present evidence does not necessitate the assumption that such a carrier is active in yeast.

[24] Mitochondrial cation transport systems

1995 ◽  
pp. 331-348 ◽  
Author(s):  
Keith D. Garlid ◽  
Xiaocheng Sun ◽  
Peter Paucek ◽  
Gebretateos Woldegiorgis
Keyword(s):  
Cation Transport ◽  
Transport Systems

Sympathetic Nervous Function and Erythrocyte Cation Transport Systems in Normotensive Individuals with Family History of Hyperension

1989 ◽  
Vol 11 (sup1) ◽  
pp. 353-361 ◽  
Author(s):  
Toshihiro Saito ◽  
Yuichiro Koshibu ◽  
Noriyuki Kai ◽  
Kazutoshi Yamamoto ◽  
Jiro Iwata ◽  
...  
Keyword(s):  
Family History ◽  
Cation Transport ◽  
Transport Systems ◽  
Nervous Function ◽  
History Of ◽  
Sympathetic Nervous

scholarly journals Cation transport in Escherichia coli. IX. Regulation of K transport.

1978 ◽  
Vol 72 (3) ◽  
pp. 283-295 ◽  
Author(s):  
D B Rhoads ◽  
W Epstein
Keyword(s):  
Escherichia Coli ◽  
Steady State ◽  
Cation Transport ◽  
Transport Systems ◽  
Energy Requirements ◽  
Protonmotive Force ◽  
K Uptake ◽  
Kinetics Of ◽  
K Transport ◽  
External K

Kinetics of K exchange in the steady state and of net K uptake after osmotic upshock are reported for the four K transport systems of Escherichia coli: Kdp, TrkA, TrkD, and TrkF. Energy requirements for K exchange are reported for the Kdp and TrkA systems. For each system, kinetics of these two modes of K transport differ from those for net K uptake by K-depleted cells (Rhoads, D. B. F.B. Walters, and W. Epstein. 1976. J. Gen. Physiol. 67:325-341). The TrkA and TrkD systems are inhibited by high intracellular K, the TrkF system is stimulated by intracellular K, whereas the Kdp system is inhibited by external K when intracellular K is high. All four systems mediate net K uptake in response to osmotic upshock. Exchange by the Kdp and TrkA systems requires ATP but is not dependent on the protonmotive force. Energy requirements for the Kdp system are thus identical whether measured as net K uptake or K exchange, whereas the TrkA system differs in that it is dependent on the protonmotive force only for net K uptake. We suggest that in both the Kpd and TrkA systems formation of a phosphorylated intermediate is necessary for all K transport, although exchange transport may not consume energy. The protonmotive-force dependence of the TrkA system is interpreted as a regulatory influence, limiting this system to exchange except when the protonmotive force is high.

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