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Fluorescein isothiocyanate staining intensity as a probe of hyperthermia‐induced changes in chromatin conformation

Fluorescein isothiocyanate staining intensity as a probe of hyperthermia‐induced changes in... In a previous report we presented evidence for large increases in fluorescein isothiocyanate (FITC) fluorescent intensity caused by hyperthermia which were not associated with synthesis of heat‐shock proteins. We have now refined and considerably extended the measurements of increases in FITC fluorescent intensity caused by hyperthermia within the range 41.0°C to 50.0deg;C, and associated these with the extent of cell death caused by the hyperthermia. It appears that cell death ensues when the FITC fluorescent intensity has not returned to its baseline value within the time of one cell cycle. If thermotolerance is induced, there is a concomitant reduction in the increase in FITC staining intensity and the extent of cell death. When hyperthermia is followed by acid extraction, an additional increase in FITC staining intensity (above that due to hyperthermia alone) is observed, indicating separate sites of action on basic nuclear proteins. Hyperthermia and acid extraction have related effects on the relationship between FITC and propidium iodide staining. Hyperthermia‐induced increases in FITC staining intensity are almost completely reversed by 6.7 mM formaldehyde with a marginal effect on the control FITC staining at this formaldehyde concentration. We suggest that hyperthermia causes extensive dissociation of basic protein‐protein binding within nuclear chromatin, and that this may be a contributory cause of hyperthermia‐in‐duced cell death. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cytometry Part A Wiley

Fluorescein isothiocyanate staining intensity as a probe of hyperthermia‐induced changes in chromatin conformation

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References (23)

Publisher
Wiley
Copyright
Copyright © 1989 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1552-4922
eISSN
1552-4930
DOI
10.1002/cyto.990100208
pmid
2469557
Publisher site
See Article on Publisher Site

Abstract

In a previous report we presented evidence for large increases in fluorescein isothiocyanate (FITC) fluorescent intensity caused by hyperthermia which were not associated with synthesis of heat‐shock proteins. We have now refined and considerably extended the measurements of increases in FITC fluorescent intensity caused by hyperthermia within the range 41.0°C to 50.0deg;C, and associated these with the extent of cell death caused by the hyperthermia. It appears that cell death ensues when the FITC fluorescent intensity has not returned to its baseline value within the time of one cell cycle. If thermotolerance is induced, there is a concomitant reduction in the increase in FITC staining intensity and the extent of cell death. When hyperthermia is followed by acid extraction, an additional increase in FITC staining intensity (above that due to hyperthermia alone) is observed, indicating separate sites of action on basic nuclear proteins. Hyperthermia and acid extraction have related effects on the relationship between FITC and propidium iodide staining. Hyperthermia‐induced increases in FITC staining intensity are almost completely reversed by 6.7 mM formaldehyde with a marginal effect on the control FITC staining at this formaldehyde concentration. We suggest that hyperthermia causes extensive dissociation of basic protein‐protein binding within nuclear chromatin, and that this may be a contributory cause of hyperthermia‐in‐duced cell death.

Journal

Cytometry Part A – Wiley

Published: Mar 1, 1989

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