Increase of thermoresistance after growth stimulation of resting Reuber H35 hepatoma cells

Dongen, Guus A.M.S. van; Geilenkirchen, W.L.M.; Rijn, J. van; Wijk, R. Van

doi:10.1016/0014-4827(86)90488-x

Cited by 14 publications

(7 citation statements)

References 42 publications

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“…6). Taken together, the observations described in this paper agree with previous data in the literature in which the different responses to stress depend on the length of duration of the heat stress and also on the metabolic state of the cell (Carvalho and Rebello, 1987;Dongen et al, 1986;Tsuchido et al, 1986). These data also suggest a relation between the presence of 70-kd hsp and the inhibition of cell growth (Fig.…”

Section: Discussionsupporting

confidence: 92%

“…On the other hand, cells in exponential growth phase could reflect a proportional number cells in Gliearly S phase, mid-S, and SiG2 phase, showing a thermosensitivity different from cells in the other culture growth phases. Dongen et al (1986) have demonstrated an increase in the thermoresistance of resting H35 cells upon growth stimulation by serum-containing medium. They also observed that a basal synthesis of proteins inducible by heat shock (hsp 65 kd, hsp 68 kd, and hsp of 84 kd) was enhanced in thermoresistant late Gliearly S-phase cells as compared with thermosensitive Go-phase cells.…”

Section: Discussionmentioning

confidence: 95%

“…Cells in the lag growth phase were more sensitive to this temperature shift than were cells in the exponential growth phase. These differences could be related to the different metabolic states of the cells (Carvalho and Rebello, 1987;Dongen et al, 1986;Tsuchido et al, 1986). Cells in the lag growth phase, incubated at 37"C, could be more susceptible to detachment than cells growing exponentially.…”

Section: Effect Of Continuous Heat Stress Onmentioning

confidence: 99%

“…Because the response to heat shock could be changed with the metabolic state of the cell (Carvalho and Rebello, 1987;Dongen et al, 1986;Tsuchido et al, 1986), we also studied the stability of hsps in confluent cells. As shown in the data of Figure 5A (lanes 2 to 4), a stability for hsps of 82 kd and 70 kd, similar to cells in lag phase (Fig.…”

Section: Stability Of Hsps In Confluent Cellsmentioning

confidence: 99%

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Effect of continuous heat stress on cell growth and protein synthesis in Aedes albopictus

Carvalho¹,

Freitas²

1988

Journal Cellular Physiology

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Aedes albopictus (clone C6/36) cells, which normally grow at 28 degrees C, were maintained at a supraoptimal temperature of 37 degrees C. The effect of continuous heat stress (37 degrees C) on cell growth was analyzed as were the modifications occurring with protein synthesis during short- and long-term heat stress. We observed that cells in lag or exponential growth phase, present inhibition of cell growth, and cells in the lag phase showed more sensitivity to death than cells growing exponentially. During the first hour of exposing the cells to 37 degrees C, they synthesized two heat shock proteins (hsps) of 82 kd and 70 kd, respectively, concomitant with inhibition of normally produced proteins at control temperature (28 degrees C). However, for incubations longer than 2 hr at 37 degrees C, a shift to the normal pattern of protein synthesis occurred. During these transitions, two other hsps of 76 kd and 90 kd were synthesized. Pulse chase experiments showed that the 70-kd hsp is stable at least for 18 hr, when the cells are returned to 28 degrees C. However, if cells were incubated at 37 degrees C, the 70-kd hsp is stable for at least 48 hr. The 70-kd hsp was localized in the cytoplasmic and in the nuclear compartment. Our results indicate a possible role of hsp 70-kd protein in the regulation of cell proliferation.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 95%

Section: Effect Of Continuous Heat Stress Onmentioning

confidence: 99%

Section: Stability Of Hsps In Confluent Cellsmentioning

confidence: 99%

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Effect of continuous heat stress on cell growth and protein synthesis in Aedes albopictus

Carvalho¹,

Freitas²

1988

Journal Cellular Physiology

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“…Increased thermotolerance of hepatoma cells (Reuber H35 cells) in late G1/early S-phase as compared to G0 phase correlated with enhanced basal synthesis of HSP65, HSP68 and HSP90AB1 as well as with increased phosphorylation of non-histone chromosomal proteins (van Dongen et al 1986). Not only heat stress but also cold stress can induce HSPs.…”

Section: Inductors Of Hsp90(ab1)mentioning

confidence: 99%

HSP90AB1: Helping the good and the bad

Haase

Fitze

2016

Gene

111

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HSP90AB1 (heat shock protein 90 kDA alpha, class B, member 1), also known as HSP90beta, is a member of the large family of HSPs which function as molecular chaperones. Chaperones, by binding to client proteins, support proper protein folding and maintain protein stability, especially after exposure to various kinds of cellular stress. Client proteins belong to various protein families including kinases, ubiquitin ligases and transcription factors. HSP90 proteins act as dimers and bind clients with the help of co-chaperones. The cochaperones influence many functions including client binding, ATPase activity or ATP binding of HSP90. HSPs are necessary for a large scale of cellular processes and therefore essential for cell survival. Since client proteins can be mutant proteins that would be degraded without the help of chaperones, HSPs also promote tumor formation and cancer cell proliferation. As such, they are also targets for new therapeutic approaches in cancer treatment. This review focuses on recent studies on HSP90AB1, if possible in comparison with its close homologue HSP90AA1.

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Serum‐stimulated cell cycle progression and stress protein synthesis in C3H10T1/2 fibroblasts treated with sodium arsenite

Wijk

Welters

Souren

et al. 1993

Journal Cellular Physiology

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In this work, we demonstrated that a nonlethal dose of arsenite administered to quiescent C3H10T1/2 fibroblasts can enhance the mitogenic effect of suboptimal concentrations of serum. The mitogenic effect was dependent on the serum concentration and on the time interval between the administration of arsenite and that of serum. This suggests that mitogen sensitivity changes in time after arsenite treatment. It is shown that the concentrations of arsenite that enhance the mitogenic effect of serum also increase the mRNA levels of c-fos, HSP68, and HSP84 and induce the specific synthesis of Heat Shock Proteins (HSPs). The physiological significance of this phenomenon is most likely to counteract the long-term toxic effect of arsenite by early induction of compensation for cell loss.

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Increase of thermoresistance after growth stimulation of resting Reuber H35 hepatoma cells

Cited by 14 publications

References 42 publications

Effect of continuous heat stress on cell growth and protein synthesis in Aedes albopictus

Effect of continuous heat stress on cell growth and protein synthesis in Aedes albopictus

HSP90AB1: Helping the good and the bad

Serum‐stimulated cell cycle progression and stress protein synthesis in C3H10T1/2 fibroblasts treated with sodium arsenite

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