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2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells

Approximately 23% of the glycolytic enzyme aldolase in the perinuclear region of Swiss 3T3 cells is immobile as measured by FRAP. Previous studies suggest that the immobile fraction may be associated with the actin cytoskeleton (Pagliaro, L. and D. L. Taylor. 1988. J. Cell Biol. 107:981-991), and it...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1992
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289572/
https://www.ncbi.nlm.nih.gov/pubmed/1500428
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collection PubMed
description Approximately 23% of the glycolytic enzyme aldolase in the perinuclear region of Swiss 3T3 cells is immobile as measured by FRAP. Previous studies suggest that the immobile fraction may be associated with the actin cytoskeleton (Pagliaro, L. and D. L. Taylor. 1988. J. Cell Biol. 107:981-991), and it has been proposed that the association of some glycolytic enzymes with the cytoskeleton could have functional significance, perhaps involving a fundamental relationship between glycolysis, cytoplasmic organization, and cell motility. We have tested the effect of a key glycolytic inhibitor and an actin cytoskeletal modulator on the mobility of aldolase in living cells directly, using fluorescent analog cytochemistry and FRAP. We report here that the competitive hexokinase inhibitor 2-deoxyglucose releases the bound fraction of aldolase in 3T3 cells within 10 min, and that this process is reversible upon washout of the inhibitor. A similar result is produced with the actin-binding agent, cytochalasin D. These results are consistent with models in which glycolytic enzymes are not exclusively diffusion-limited, soluble proteins, but may exist partially in the solid phase of cytoplasm. Such organization has significant implications for both the modulation of cytoplasmic structure and for cellular metabolism.
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spelling pubmed-22895722008-05-01 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells J Cell Biol Articles Approximately 23% of the glycolytic enzyme aldolase in the perinuclear region of Swiss 3T3 cells is immobile as measured by FRAP. Previous studies suggest that the immobile fraction may be associated with the actin cytoskeleton (Pagliaro, L. and D. L. Taylor. 1988. J. Cell Biol. 107:981-991), and it has been proposed that the association of some glycolytic enzymes with the cytoskeleton could have functional significance, perhaps involving a fundamental relationship between glycolysis, cytoplasmic organization, and cell motility. We have tested the effect of a key glycolytic inhibitor and an actin cytoskeletal modulator on the mobility of aldolase in living cells directly, using fluorescent analog cytochemistry and FRAP. We report here that the competitive hexokinase inhibitor 2-deoxyglucose releases the bound fraction of aldolase in 3T3 cells within 10 min, and that this process is reversible upon washout of the inhibitor. A similar result is produced with the actin-binding agent, cytochalasin D. These results are consistent with models in which glycolytic enzymes are not exclusively diffusion-limited, soluble proteins, but may exist partially in the solid phase of cytoplasm. Such organization has significant implications for both the modulation of cytoplasmic structure and for cellular metabolism. The Rockefeller University Press 1992-08-02 /pmc/articles/PMC2289572/ /pubmed/1500428 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells
title 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells
title_full 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells
title_fullStr 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells
title_full_unstemmed 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells
title_short 2-Deoxyglucose and cytochalasin D modulate aldolase mobility in living 3T3 cells
title_sort 2-deoxyglucose and cytochalasin d modulate aldolase mobility in living 3t3 cells
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2289572/
https://www.ncbi.nlm.nih.gov/pubmed/1500428