Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility

van Zoelen, E. J. J. ; Mummery, C. L. ; Boonstra, J. ; van der Saag, P. T. ; de Laat, S. W.

New York, N.Y. : Wiley-Blackwell
Published 1983
ISSN:
0730-2312
Keywords:
Na+, K+-ATPase ; cell cycle ; protein lateral mobility ; regulation ; neuroblastoma cells ; ouabain binding ; Life and Medical Sciences ; Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
Chemistry and Pharmacology
Medicine
Notes:
The pumping activity of the plasma membrane-bound Na+, K+-ATPase shows considerable variation during the cell cycle of mouse neuroblastoma Neuro-2A cells. Addition of external ATP at millimolar concentrations, which selectively enhances the plasma membrane permeability of Neuro-2A cells for sodium ions, stimulates the Na+, K+-ATPase pumping activity at all phases of the cell cycle from a factor of 1.05 in mitosis up to 2.2 in G1 phase. Determination of the number of Na+, K+-ATPase copies per cell by direct 3H-ouabain binding studies in the presence of external ATP shows a gradual increase in the number of pump sites on passing from mitosis to the late S/G2-phase by approximately a factor of 2. From these data the pumping activity per copy of Na+, K+-ATPase, optimally stimulated with respect to its various substrate ions, has been determined during the various phases of the cell cycle. This optimally stimulated pumping activity per enzyme copy, which is a reflection of the physicochemical state of the plasma membrane, is high in mitosis, almost twofold lower in early G1 phase, and increases gradually again during the other phases of the cell cycle. This shows that the observed regulation of Na+, K+-ATPase activity during the cell cycle is caused by a combination of three independent factors-namely variation in intracellular substrate availability (Na+), changes in number of enzyme copies per cell, and modulation of the plasma membrane environment of the protein molecules. The modulation of the optimal pumping activity per enzyme copy shows a good correlation (ρ = 0.96) with the known modulation of protein lateral mobility during the cell cycle, such that a high protein lateral mobility correlates with a low enzyme activity. It is concluded that changes in plasma membrane properties take place during the Neuro-2A cell cycle that result in changes in the rate of protein lateral diffusion and Na+, K+-ATPase activity in a directly correlated way.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
_version_ 1798297838782775296
addmaterial 6 Ill.
autor van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
autorsonst van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
book_url http://dx.doi.org/10.1002/jcb.240210109
datenlieferant nat_lic_papers
hauptsatz hsatz_simple
identnr NLM15984388X
issn 0730-2312
journal_name Journal of Cellular Biochemistry
materialart 1
notes The pumping activity of the plasma membrane-bound Na+, K+-ATPase shows considerable variation during the cell cycle of mouse neuroblastoma Neuro-2A cells. Addition of external ATP at millimolar concentrations, which selectively enhances the plasma membrane permeability of Neuro-2A cells for sodium ions, stimulates the Na+, K+-ATPase pumping activity at all phases of the cell cycle from a factor of 1.05 in mitosis up to 2.2 in G1 phase. Determination of the number of Na+, K+-ATPase copies per cell by direct 3H-ouabain binding studies in the presence of external ATP shows a gradual increase in the number of pump sites on passing from mitosis to the late S/G2-phase by approximately a factor of 2. From these data the pumping activity per copy of Na+, K+-ATPase, optimally stimulated with respect to its various substrate ions, has been determined during the various phases of the cell cycle. This optimally stimulated pumping activity per enzyme copy, which is a reflection of the physicochemical state of the plasma membrane, is high in mitosis, almost twofold lower in early G1 phase, and increases gradually again during the other phases of the cell cycle. This shows that the observed regulation of Na+, K+-ATPase activity during the cell cycle is caused by a combination of three independent factors-namely variation in intracellular substrate availability (Na+), changes in number of enzyme copies per cell, and modulation of the plasma membrane environment of the protein molecules. The modulation of the optimal pumping activity per enzyme copy shows a good correlation (ρ = 0.96) with the known modulation of protein lateral mobility during the cell cycle, such that a high protein lateral mobility correlates with a low enzyme activity. It is concluded that changes in plasma membrane properties take place during the Neuro-2A cell cycle that result in changes in the rate of protein lateral diffusion and Na+, K+-ATPase activity in a directly correlated way.
package_name Wiley-Blackwell
publikationsjahr_anzeige 1983
publikationsjahr_facette 1983
publikationsjahr_intervall 8019:1980-1984
publikationsjahr_sort 1983
publikationsort New York, N.Y.
publisher Wiley-Blackwell
reference 21 (1983), S. 77-91
schlagwort Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
search_space articles
shingle_author_1 van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
shingle_author_2 van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
shingle_author_3 van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
shingle_author_4 van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
shingle_catch_all_1 van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
The pumping activity of the plasma membrane-bound Na+, K+-ATPase shows considerable variation during the cell cycle of mouse neuroblastoma Neuro-2A cells. Addition of external ATP at millimolar concentrations, which selectively enhances the plasma membrane permeability of Neuro-2A cells for sodium ions, stimulates the Na+, K+-ATPase pumping activity at all phases of the cell cycle from a factor of 1.05 in mitosis up to 2.2 in G1 phase. Determination of the number of Na+, K+-ATPase copies per cell by direct 3H-ouabain binding studies in the presence of external ATP shows a gradual increase in the number of pump sites on passing from mitosis to the late S/G2-phase by approximately a factor of 2. From these data the pumping activity per copy of Na+, K+-ATPase, optimally stimulated with respect to its various substrate ions, has been determined during the various phases of the cell cycle. This optimally stimulated pumping activity per enzyme copy, which is a reflection of the physicochemical state of the plasma membrane, is high in mitosis, almost twofold lower in early G1 phase, and increases gradually again during the other phases of the cell cycle. This shows that the observed regulation of Na+, K+-ATPase activity during the cell cycle is caused by a combination of three independent factors-namely variation in intracellular substrate availability (Na+), changes in number of enzyme copies per cell, and modulation of the plasma membrane environment of the protein molecules. The modulation of the optimal pumping activity per enzyme copy shows a good correlation (ρ = 0.96) with the known modulation of protein lateral mobility during the cell cycle, such that a high protein lateral mobility correlates with a low enzyme activity. It is concluded that changes in plasma membrane properties take place during the Neuro-2A cell cycle that result in changes in the rate of protein lateral diffusion and Na+, K+-ATPase activity in a directly correlated way.
0730-2312
07302312
Wiley-Blackwell
shingle_catch_all_2 van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
The pumping activity of the plasma membrane-bound Na+, K+-ATPase shows considerable variation during the cell cycle of mouse neuroblastoma Neuro-2A cells. Addition of external ATP at millimolar concentrations, which selectively enhances the plasma membrane permeability of Neuro-2A cells for sodium ions, stimulates the Na+, K+-ATPase pumping activity at all phases of the cell cycle from a factor of 1.05 in mitosis up to 2.2 in G1 phase. Determination of the number of Na+, K+-ATPase copies per cell by direct 3H-ouabain binding studies in the presence of external ATP shows a gradual increase in the number of pump sites on passing from mitosis to the late S/G2-phase by approximately a factor of 2. From these data the pumping activity per copy of Na+, K+-ATPase, optimally stimulated with respect to its various substrate ions, has been determined during the various phases of the cell cycle. This optimally stimulated pumping activity per enzyme copy, which is a reflection of the physicochemical state of the plasma membrane, is high in mitosis, almost twofold lower in early G1 phase, and increases gradually again during the other phases of the cell cycle. This shows that the observed regulation of Na+, K+-ATPase activity during the cell cycle is caused by a combination of three independent factors-namely variation in intracellular substrate availability (Na+), changes in number of enzyme copies per cell, and modulation of the plasma membrane environment of the protein molecules. The modulation of the optimal pumping activity per enzyme copy shows a good correlation (ρ = 0.96) with the known modulation of protein lateral mobility during the cell cycle, such that a high protein lateral mobility correlates with a low enzyme activity. It is concluded that changes in plasma membrane properties take place during the Neuro-2A cell cycle that result in changes in the rate of protein lateral diffusion and Na+, K+-ATPase activity in a directly correlated way.
0730-2312
07302312
Wiley-Blackwell
shingle_catch_all_3 van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
The pumping activity of the plasma membrane-bound Na+, K+-ATPase shows considerable variation during the cell cycle of mouse neuroblastoma Neuro-2A cells. Addition of external ATP at millimolar concentrations, which selectively enhances the plasma membrane permeability of Neuro-2A cells for sodium ions, stimulates the Na+, K+-ATPase pumping activity at all phases of the cell cycle from a factor of 1.05 in mitosis up to 2.2 in G1 phase. Determination of the number of Na+, K+-ATPase copies per cell by direct 3H-ouabain binding studies in the presence of external ATP shows a gradual increase in the number of pump sites on passing from mitosis to the late S/G2-phase by approximately a factor of 2. From these data the pumping activity per copy of Na+, K+-ATPase, optimally stimulated with respect to its various substrate ions, has been determined during the various phases of the cell cycle. This optimally stimulated pumping activity per enzyme copy, which is a reflection of the physicochemical state of the plasma membrane, is high in mitosis, almost twofold lower in early G1 phase, and increases gradually again during the other phases of the cell cycle. This shows that the observed regulation of Na+, K+-ATPase activity during the cell cycle is caused by a combination of three independent factors-namely variation in intracellular substrate availability (Na+), changes in number of enzyme copies per cell, and modulation of the plasma membrane environment of the protein molecules. The modulation of the optimal pumping activity per enzyme copy shows a good correlation (ρ = 0.96) with the known modulation of protein lateral mobility during the cell cycle, such that a high protein lateral mobility correlates with a low enzyme activity. It is concluded that changes in plasma membrane properties take place during the Neuro-2A cell cycle that result in changes in the rate of protein lateral diffusion and Na+, K+-ATPase activity in a directly correlated way.
0730-2312
07302312
Wiley-Blackwell
shingle_catch_all_4 van Zoelen, E. J. J.
Mummery, C. L.
Boonstra, J.
van der Saag, P. T.
de Laat, S. W.
Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
Na+, K+-ATPase
cell cycle
protein lateral mobility
regulation
neuroblastoma cells
ouabain binding
Life and Medical Sciences
Cell & Developmental Biology
The pumping activity of the plasma membrane-bound Na+, K+-ATPase shows considerable variation during the cell cycle of mouse neuroblastoma Neuro-2A cells. Addition of external ATP at millimolar concentrations, which selectively enhances the plasma membrane permeability of Neuro-2A cells for sodium ions, stimulates the Na+, K+-ATPase pumping activity at all phases of the cell cycle from a factor of 1.05 in mitosis up to 2.2 in G1 phase. Determination of the number of Na+, K+-ATPase copies per cell by direct 3H-ouabain binding studies in the presence of external ATP shows a gradual increase in the number of pump sites on passing from mitosis to the late S/G2-phase by approximately a factor of 2. From these data the pumping activity per copy of Na+, K+-ATPase, optimally stimulated with respect to its various substrate ions, has been determined during the various phases of the cell cycle. This optimally stimulated pumping activity per enzyme copy, which is a reflection of the physicochemical state of the plasma membrane, is high in mitosis, almost twofold lower in early G1 phase, and increases gradually again during the other phases of the cell cycle. This shows that the observed regulation of Na+, K+-ATPase activity during the cell cycle is caused by a combination of three independent factors-namely variation in intracellular substrate availability (Na+), changes in number of enzyme copies per cell, and modulation of the plasma membrane environment of the protein molecules. The modulation of the optimal pumping activity per enzyme copy shows a good correlation (ρ = 0.96) with the known modulation of protein lateral mobility during the cell cycle, such that a high protein lateral mobility correlates with a low enzyme activity. It is concluded that changes in plasma membrane properties take place during the Neuro-2A cell cycle that result in changes in the rate of protein lateral diffusion and Na+, K+-ATPase activity in a directly correlated way.
0730-2312
07302312
Wiley-Blackwell
shingle_title_1 Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
shingle_title_2 Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
shingle_title_3 Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
shingle_title_4 Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
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source_archive Wiley InterScience Backfile Collection 1832-2000
timestamp 2024-05-06T10:14:21.933Z
titel Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
titel_suche Membrane regulation of the Na+, K+-ATPase during the neuroblastoma cell cycle: Correlation with protein lateral mobility
topic W
V
WW-YZ
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