Heat-regulated expression of the hepatitis B virus surface antigen in the human Wish cell line

Dréano, Michel; Fouillet, X.; Brochot, Jean; Vallet, Jean-Marie Philippe; Michel, Marie‐Louise; Rungger, Duri; Bromley, Peter

doi:10.1016/0168-1702(87)90039-6

Cited by 11 publications

(5 citation statements)

References 24 publications

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“…3, B and 6"). Although some difference was observed between the different cell lines (HEp3: metastatic [Ossowski and Reich, 1980], Wish and HeLa: tumorigenic [Dreano et al, 1987;Noguchi et al, 1978]), all three cell lines showed relatively high efficiency (25-50% of inoculum) of mesenchyme invasion (Figs. 1, 2, 4, 7, and 10).…”

Section: Discussionmentioning

confidence: 99%

“…HEp3 cells (Toolan, 1954) were obtained by collagenase dissociation of HEp3 tumors, serially passaged on CAMs of 10-d-old chick embryos, using previously described techniques (Ossowski and Reich, 1980). HeLa cells maintained in our laboratory were originally obtained from Dr. J. Nevins (Rockefeller University), and Wish-mUK, a human cell line transfected with mouse uPA cDNA (Belin et al, 1985), under the transcrptional control of a human heat shock promoter using a previously described vector (Dreano et al, 1987), was generously donated by Dr. D. Belin (University of Geneva Medical School, Switzerland).…”

Section: Cell Linesmentioning

confidence: 99%

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In vivo invasion of modified chorioallantoic membrane by tumor cells: the role of cell surface-bound urokinase.

Ossowski

1988

The Journal of Cell Biology

262

144

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Abstract. The ability of the chick embryo chorioallantoic membrane (CAM) to withstand invasion by tumor ceils can be intentionally compromised by altering its morphological integrity. Using a newly developed quantitative assay of invasion we showed that intact CAMs were completely resistant to invasion by tumor cells, wounded CAMs did not pose a barrier to penetration, and CAMs that were wounded and then allowed to reseal displayed partial susceptibility to invasion. The invasion of resealed CAMs required catalytically active plasminogen activator (PA) of the urokinase type (uPA); the invasive efficiency of tumor cells was reduced by 75% when tumor uPA activity or tumor uPA production was inhibited. The invasive ability of human tumor cells, which have surface uPA receptors but which do not produce the enzyme, could be augmented by saturating their receptors with exogenous uPA. The mere stimulation of either uPA or tissue plasminogen activator production, in absence of binding to cell receptors, did not result in an enhancement of invasiveness.These findings suggest that the increased invasive potential of tumor cells is correlated with cell surface-associated proteolytic activity stemming from the interaction between uPA and its surface receptor.

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Section: Discussionmentioning

confidence: 99%

Section: Cell Linesmentioning

confidence: 99%

In vivo invasion of modified chorioallantoic membrane by tumor cells: the role of cell surface-bound urokinase.

Ossowski

1988

The Journal of Cell Biology

262

144

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“…The mutants were identified by restriction analysis and confirmed by sequencing the entire inserts, which were then reintroduced in the murine expression vector pSPHSneo. 50 Transfection of WISH cells, which do not produce detectable amounts of plasminogen activators or their inhibitors, selection of UPA-producing clones, and analysis of the conditioned media were performed as described. 44 …”

Section: Cell Culturementioning

confidence: 99%

Binding of Human Urokinase-Type Plasminogen Activator to Its Receptor

Quax¹,

Grimbergen²,

Lansink³

et al. 1998

ATVB

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Abstract-Urokinase-type plasminogen activator (UPA), particularly when bound to its receptor (UPAR), is thought to play a major role in local proteolytic processes, thus facilitating cell migration as may occur during angiogenesis, neointima and atherosclerotic plaque formation, and tumor cell invasion. To facilitate understanding of the need and function of the UPA/UPAR interaction in cell migration and vascular remodeling, we changed several amino acid residues in UPA so as to interfere with its interaction with its receptor. The receptor-binding domain of UPA has been localized to a region in the growth factor domain between residues 20 and 32. Since the binding of UPA to UPAR appears to be species specific, we used the differences in amino acid sequences in the growth factor domain of UPA between various species to construct a human UPA variant that does not bind to the human UPAR. We substituted Asn22 for its mouse equivalent Tyr by site-directed mutagenesis. This mutant UPA had similar plasminogen activator characteristics as wild-type UPA, including its specific activity and interaction with plasminogen activator inhibitor-1. However, no UPA/UPAR complexes could be observed in cross-linking experiments using DFP-treated 125 I-labeled mutant UPA and lysates of various cells, including U937 histiocytic lymphoma cells, phorbol myristate acetate-treated human ECs, and mouse LB6 cells transfected with human UPAR cDNA. In direct binding experiments, DFP-treated 125 I-labeled mutant UPA could not bind to phorbol myristate acetate-treated ECs, whereas wild-type UPA did bind. Furthermore, a 25-fold excess of wild-type UPA completely prevented the binding of DFP-treated 125 I-labeled wild-type UPA to the human receptor on transfected LB6 cells, whereas an equal amount of mutant UPA had only a very small effect. In ligand blotting assays, very weak binding of mutant UPA to human UPAR could be observed. Changing Asn22 into the other amino acid residues alanine or glutamine had no effect on binding to UPAR on human ECs. The functional integrity of the growth factor domain in the non-receptor binding Asn22Tyr mutant is suggested by the fact that binding of this mutant to a murine UPAR can be restored after additional mutations in the growth factor domain, Asn27,His29,Trp30 to Arg27,Arg29,Arg30. We conclude that Asn22 and Asn27,His29,Trp30 in human UPA are key determinants in the species-specific binding of the enzyme to its receptor and that changing Asn22 into Tyr results in a UPA mutant with strongly reduced binding to UPAR. (Arterioscler Thromb Vasc Biol. 1998;18:693-701.)

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“…L tk-cells were cotransfected with the recombinant plasmid pAG0 (Colbere-Garapin et al, 1979) containing the thymidine kinase gene from herpes virus, and the recombinant plasmid PMZllc; colonies were selected with HAT medium and tested for their capacity to produce HBsAg after a heat-shock. All the colonies tested failed to produce HBsAg at 37°C but synthesized this antigen after being submitted to a heatshock at 42°C or 43°C for 1 h. Similarly, the heatinduced expression of HBsAg was recently obtained with a human amnion cell line (Dreano et al, 1987). We selected one of the colonies expressing the highest levels of HBsAg after an elevation of temperature and then studied in parallel the kinetics of HBsAg expression ( Fig.…”

Section: Expression Of Gene S From Hepatitis B Virus Under the Contromentioning

confidence: 99%

Regulation of the heat‐shock response by interferon in mouse L cells

Dubois¹,

Mezger²,

Morange³

et al. 1988

Journal Cellular Physiology

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Interferon (IFN) is not able to induce heat-shock protein (HSP) synthesis. However IFN pretreatment of mouse L cells has been shown to enhance the decrease of overall protein synthesis which follows a heat shock, and to stimulate the accumulation of HSPs. We show here that the synthesis of a protein (the hepatitis B virus surface antigen) under the control of a Drosophila HSP 70 promoter is also stimulated in IFN-pretreated cells. The regulation by IFN takes place at two levels: first, the rate of HSP gene transcription is increased in nuclei isolated from IFN-treated cells; second, the synthesis of HSPs is prolonged after pretreatment with IFN. Experiments performed in the presence of actinomycin D show that this effect is due to a stabilization by IFN of mRNAs coding for HSPs.

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Heat-regulated expression of the hepatitis B virus surface antigen in the human Wish cell line

Cited by 11 publications

References 24 publications

In vivo invasion of modified chorioallantoic membrane by tumor cells: the role of cell surface-bound urokinase.

In vivo invasion of modified chorioallantoic membrane by tumor cells: the role of cell surface-bound urokinase.

Binding of Human Urokinase-Type Plasminogen Activator to Its Receptor

Regulation of the heat‐shock response by interferon in mouse L cells

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