Heat-induced Alterations in DNA Polymerase Activity of HeLa Cells and of Isolated Nuclei. Relation to Cell Survival

Kampinga, Harm H.; Jorritsma, J. B. M.; Konings, Awt

doi:10.1080/09553008514550051

Cited by 44 publications

(25 citation statements)

References 17 publications

(11 reference statements)

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“…It has been shown previously by us (Kampinga et al, 1985(Kampinga et al, , 1987(Kampinga et al, , 1989b and other investigators (Warters and Roti Roti, 1982;Roti Roti and Wilson, 1984;Higashikubo et al, 1986;McConnell et al, 1987) that hyperthermic treatment of cells increases the protein mass of nuclei isolated from these heated cells (TX-100 insoluble fraction). This is most likely due to an intranuclear protein aggregation as a result of the heat treatment (Kampinga et al, 1985(Kampinga et al, ,1987(Kampinga et al, ,1989bMcConnell et al, 1987).…”

Section: Resultsmentioning

confidence: 83%

“…This is most likely due to an intranuclear protein aggregation as a result of the heat treatment (Kampinga et al, 1985(Kampinga et al, ,1987(Kampinga et al, ,1989bMcConnell et al, 1987). It has been shown that such changes may be related to thermal cell killing, also for conditions of heat-induced thermotolerance (Kampinga et al, 1987, 198913).…”

Section: Resultsmentioning

confidence: 94%

“…Survival of cells without any pretreatment (control) or treated for 5 hours with CHX alone (CHX) is also shown. Survival was determined using the soft agar cloning technique (Kampinga et al, 1985(Kampinga et al, , 1987 . Thermotolerance ratios were calculated by dividing the average survival (mean values of at least five independent experiments) of the pretreated samples by the survival of non-pretreated control cells.…”

Section: Resultsmentioning

confidence: 99%

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Acquisition of thermotolerance induced by heat and arsenite in HeLa S3 cells: Multiple pathways to induce tolerance?

Kampinga

Brunsting

Konings

1992

Journal Cellular Physiology

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Recent data indicate that cells may acquire thermotolerance via more than one route. In this study, we observed differences in thermotolerance development in HeLa S3 cells induced by prior heating (15 minutes at 44 degrees C) or pretreatment with sodium-arsenite (1 hour at 37 degrees C, 100 microM). Inhibition of overall protein and heat shock protein (HSP) synthesis (greater than 95%) by cycloheximide (25 micrograms/ml) during tolerance development nearly completely abolished thermotolerance induced by arsenite, while significant levels of heat-induced thermotolerance were still apparent. The same dependence of protein synthesis was found for resistance against sodium-arsenite toxicity. Toxic heat, but not toxic arsenite treatments caused heat damage in the cell nucleus, measured as an increase in the protein mass of nuclei isolated from treated cells (intranuclear protein aggregation). Recovery from this intranuclear protein aggregation was observed during post-heat incubations of the cells at 37 degrees C. The rate of recovery was faster in heat-induced tolerant cells than in nontolerant cells. Arsenite-induced tolerant cells did not show an enhanced rate of recovery from the heat-induced intranuclear protein aggregation. In parallel, hyperthermic inhibition of RNA synthesis was the same in tolerant and nontolerant cells, whereas post-heat recovery was enhanced in heat-induced, but not arsenite-induced thermotolerant cells. The more rapid recovery from heat damage in the nucleus (protein aggregation and RNA synthesis) in cells made tolerant by a prior heat treatment seemed related to the ability of heat (but not arsenite) to induce HSP translocations to the nucleus.

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Section: Resultsmentioning

confidence: 83%

Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

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Acquisition of thermotolerance induced by heat and arsenite in HeLa S3 cells: Multiple pathways to induce tolerance?

Kampinga

Brunsting

Konings

1992

Journal Cellular Physiology

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“…This has been suggested to play a role in cell survival, DNA synthesis and repair, and transcription [Kampinga et al, 1985;Roti Roti and Laszlo, 1988;Fisher, 1990]. Recent studies have clearly documented that changes in the nuclear proteins in response to heat shock are significantly reflected in the nuclear matrix, and further, the modifications in the association of specific proteins with the nuclear matrix is of a differential nature [VanderWaal et al, 1996, Roti Roti et al, 1998].…”

mentioning

confidence: 97%

Heat shock mediated modulation of protein kinase CK2 in the nuclear matrix*

Davis

Wang

Zhang

et al. 2002

J of Cellular Biochemistry

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Nuclear matrix, a key structure in the nuclear framework, appears to be a particularly responsive target during heat shock treatment of cells. We have previously shown that nuclear matrix is a preferential target for protein kinase CK2 signaling in the nucleus. The levels of CK2 in the nuclear matrix undergo dynamic changes in response to altered growth status in the cell. Here, we have demonstrated that CK2 targeting to the nuclear matrix is profoundly influenced by treatment of the cells to temperatures higher than 37 degrees C. Rapid increase in the nuclear matrix association of CK2 is observed when cells are placed at temperatures of 41 and 45 degrees C. This effect at 45 degrees C was higher than at 41 degrees C, and was time-dependent. Also, different cell lines behaved in a qualitatively similar manner though the quantitative responses differed. The modulations in the nuclear matrix associated CK2 in response to heat shock appear to be due to trafficking of the enzyme between cytosolic and nuclear compartments. In addition, it was noted that isolated nuclei subjected to heat shock also responded by a shuttling of the intrinsic CK2 to the nuclear matrix compartment. These results suggest that modulations in CK2 in the nuclear compartment in response to the heat stress occur not only by a translocation of the enzyme from the cytoplasmic compartment to the nuclear compartment, but also that there is a redistribution of the kinase within the nuclear compartment resulting in a preferential association with the nuclear matrix. The results support the notion that CK2 association with the nuclear matrix in response to heat shock may serve a protective role in the cell response to stress.

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“…There is uncertainty, however, as to how much of the increase in nuclear protein content of nuclei isolated from heated cells is due to cytoplasmic proteins moving into the nucleus, adsorption of cytoplasmic proteins to nuclei during their isolation, and less extraction of nuclear proteins during the nuclear isolation procedure. For example, much of the activity of DNA polymerase a and p, almost exclusively nuclear enzymes (Bensch et al, 19831, is lost from the nuclei during their isolation, but this loss is greatly reduced if the cells are heated prior to isolation of the nuclei (Kampinga et al, 1985; also our unpublished data). Heat would be expected to reduce the loss of activity of nuclear enzymes during isolation of nuclei, if heat caused an increase in the binding or trapping of proteins within nuclear components.…”

mentioning

confidence: 85%

Content of nonhistone protein in nuclei after hyperthermic treatment

Chu

Ross

Wong

et al. 1993

Journal Cellular Physiology

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When nuclei were isolated from Chinese hamster ovary cells after being heated, there was a large increase in the amount of 3H-tryptophan labeled nonhistone protein in the nucleus relative to the whole cell. After 15 min or 30 min of heating at 45.5 degrees C, the nuclear nonhistone protein content increased by 1.6 or 1.8, respectively. In contrast, when the nuclear nonhistone protein content was determined in the intact cell by using autoradiography to quantify 3H-tryptophan labeled protein in the nucleus and cytoplasm in sections of fixed cells, the nuclear nonhistone protein content increased by only 1.14 or 1.28 for 15 or 30 min at 45.5 degrees C, respectively. Therefore, heat does not induce a massive movement of cytoplasmic protein into the nucleus.

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Heat-induced Alterations in DNA Polymerase Activity of HeLa Cells and of Isolated Nuclei. Relation to Cell Survival

Cited by 44 publications

References 17 publications

Acquisition of thermotolerance induced by heat and arsenite in HeLa S3 cells: Multiple pathways to induce tolerance?

Acquisition of thermotolerance induced by heat and arsenite in HeLa S3 cells: Multiple pathways to induce tolerance?

Heat shock mediated modulation of protein kinase CK2 in the nuclear matrix*

Content of nonhistone protein in nuclei after hyperthermic treatment

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