Thermal stress as an inducer of differentiation of U937 cells

Cellier, Mathieu; Taimi, Mohammed; Château, Marie-Thérèse; Cannat, A; Marti, Jacques

doi:10.1016/0145-2126(93)90069-w

Cited by 18 publications

(6 citation statements)

References 40 publications

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“…These conditions frequently include the imposition of a stress, for example, a heat shock. It has been suggested that a heat shock or some other form of stress and possibly the heat shock proteins themselves may be important in the morphological changes observed in other systems, including fungi, protozoa, and mammalian cells (7,22,28,43,52). Heat shock proteins play a key role in protein biogenesis: they include essential components of the chaperone apparatus that promotes protein folding in vivo (9,18,19).…”

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confidence: 99%

Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans

et al. 1995

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Candida albicans HSP90 sequences were isolated by screening cDNA and genomic libraries with a probe derived from the Saccharomyces cerevisiae homolog, HSP82, which encodes a member of the heat shock protein 90 family of molecular chaperones. Identical sequences were obtained for the 2,197-bp overlap of the cDNA and gene sequences, which were derived from C. albicans 3153A and ATCC 10261, respectively. The C. albicans HSP90 gene contained no introns, and it showed strong homology (61 to 79% identity) to HSP90 sequences from other fungi, vertebrates, and plants. The C-terminal portion of the predicted Hsp90 amino acid sequence was identical to the 47-kDa protein which is thought to be immunoprotective during C. albicans infections (R. C. Matthews, J. Med. Microbiol. 36:367-370, 1992), confirming that this protein represents the C-terminal portion of the 81-kDa Hsp90 protein. Quantitative Northern (RNA) analyses revealed that C. albicans HSP90 mRNA was heat shock inducible and that its levels changed during batch growth, with its maximum levels being reached during the mid-exponential growth phase. HSP90 mRNA levels increased transiently during the yeast-to-hyphal transition but did not correlate directly with germ tube production per se. These data do not exclude a role for Hsp90 in the dimorphic transition. Southern blotting revealed only one HSP90 locus in the diploid C. albicans genome. Repeated attempts to disrupt both alleles and generate a homozygous C. albicans ⌬hsp90/⌬hsp90 null mutant were unsuccessful. These observations suggest the existence of a single HSP90 locus which is essential for viability in C. albicans.

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Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans

et al. 1995

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“…However, this transition is hard to characterize, and the heat shock effects might also be interpreted as delays in G1 progression. In agreement with a G0/G1 block, heat shock induces differentiation markers or differentiated phenotypes and enhances the effectivity of cell-type-specific inducers of differentation in HL60 cells, neuroblastoma cells, U937 leukemia cells, malignant human thyroid cancer cells, and embryonic carcinoma cells [65][66][67][68][69][70]. Lethal effects.…”

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confidence: 99%

Heat shock effects on cell cycle progression

Kühl¹,

Rensing²

2000

CMLS, Cell. Mol. Life Sci.

120

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In mammalian cells, short-term (acute) exposure to a moderate heat shock leads to a transient arrest of cells at mainly two cell cycle checkpoints, the G1/S and G2/M transitions. This is documented by the more or less synchronous resumption of cell cycle progression from these checkpoints during recovery. The reason for the accumulation of cells at these checkpoints may be found in activity thresholds of cyclin-dependent kinases (Cdks) at both transitions which are determined by (i) the amounts of the responsible cyclins, (ii) regulatory phosphorylation of the Cdks and (iii) the inhibition of Cdks by associated regulatory proteins (Ckis). All three regulatory systems may be subject to heat-shock-dependent changes, the amounts of Ckis, in particular, being increased. Cdk-dependent phosphorylation of the retinoblastoma protein and the subsequent release of active S-phase-specific transcription factors E2F/DP are considered as major heat-sensitive steps in cell cycle progression. Furthermore, high acute heat shock and long-term (chronic) heat treatment may lead to cell-type-specific forms of cell death. All types of responses to heat treatment are subject to adaptation after a 'priming' treatment, probably due to higher levels of heat shock proteins.

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“…Hyperthermic treatment of malignant tumours is one cancer therapy by which the possible mechanism of the proliferation of tumour cells is relatively inhibited (Urano et al, 1983;Cellier et al, 1993). In addition, Toyota et al (1997) reported that a wholebody hyperthermia inhibits metastasis of breast cancer cells in rat in vivo.…”

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Anti-angiogenic action of hyperthermia by suppressing gene expression and production of tumour-derived vascular endothelial growth factor in vivo and in vitro

Sawaji

Sato

Takeuchi³

et al. 2002

Br J Cancer

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Vascular endothelial growth factor is an important angiogenic factor for tumour progression because it increases endothelialcell proliferation and remodels extracellular matrix in blood vessels. We demonstrated that hyperthermia at 428C, termed heat shock, suppressed the gene expression and production of vascular endothelial growth factor in human fibrosarcoma HT-1080 cells and inhibited its in vitro angiogenic action on human umbilical vein endothelial cells. The gene expression of alternative splicing variants for vascular endothelial growth factor, VEGF 121 , VEGF 165 and VEGF 189 , was constitutively detected in HT-1080 cells, but the VEGF 189 transcript was less abundant than VEGF 121 and VEGF 165 . When HT-1080 cells were treated with heat shock at 428C for 4 h and then maintained at 378C for another 24 h, the gene expression of all vascular endothelial growth factor variants was suppressed. In addition, HT-1080 cells were found to produce abundant VEGF 165 , but much less VEGF 121 , both of which were inhibited by heat shock. Furthermore, the level of vascular endothelial growth factor in sera from six cancer patients was significantly diminished 2 -3 weeks after completion of whole-body hyperthermia at 428C (49.9+36.5 pg ml 71 , P50.01) as compared with that prior to the treatment (177.0+77.5 pg ml 71). On the other hand, HT-1080 cell-conditioned medium showed vascular endothelial growth factor-dependent cell proliferative activity and the augmentation of pro-matrix metalloproteinase-1 production in human umbilical vein endothelial cells. The augmentation of endothelial-cell proliferation and pro-matrix metalloproteinase-1 production was poor when human umbilical vein endothelial cells were treated with conditioned medium from heat-shocked HT-1080 cells. These results suggest that hyperthermia acts as an anti-angiogenic strategy by suppressing the expression of tumour-derived vascular endothelial growth factor production and thereby inhibiting endothelial-cell proliferation and extracellular matrix remodelling in blood vessels.

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Thermal stress as an inducer of differentiation of U937 cells

Cited by 18 publications

References 40 publications

Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans

Structure and regulation of the HSP90 gene from the pathogenic fungus Candida albicans

Heat shock effects on cell cycle progression

Anti-angiogenic action of hyperthermia by suppressing gene expression and production of tumour-derived vascular endothelial growth factor in vivo and in vitro

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