Hyperosmolarity-induced stress proteins in chick embryo fibroblasts

Petronini, Pier Giorgio; Tramacere, Mariarosaria; Mazzini, Alberto; Piedimonte, Giuseppe; Silvotti, Lucia; Borghetti, Angelo F.

doi:10.1016/0014-4827(87)90403-4

Cited by 32 publications

(22 citation statements)

References 17 publications

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“…For example, continuous cell exposure to hypertonicity induced by extracellular NaCl addition increases the expression of HSP70 [5,6,9,10]. Increased expression of the HSP70 gene is presumably triggered by denaturation of cell proteins induced by hyperthermia, and there is evidence that denatured or abnormal proteins are responsible for the induction of HSP synthesis [31].…”

Section: Discussionmentioning

confidence: 99%

“…HSP gene regulation by heat shock is well documented at all levels of expression, and it has been regarded as a paradigm for inducible genomic responses [7,8], whereas HSP induction by hypertonicity has been evaluated at the mRNA level and from the synthesis and accumulation of specific proteins [5,6,9,10]. Moreover, HSP induction by hypertonicity has been examined in long-term experiments, whereas HSP induction by hyperthermia Abbreviations used : HSE, heat-shock element ; HSF, heat-shock transcription factor ; HSP, heat-shock protein ; [K + ] i and [Na + ] i , intracellular concentrations of K + and Na + respectively ; RVI, regulatory volume increase.…”

Section: Introductionmentioning

confidence: 99%

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Activation of heat-shock transcription factor 1 by hypertonic shock in 3T3 cells

Alfieri

Petronini

Urbani

et al. 1996

Biochemical Journal

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The exposure of 3T3 cells to a medium made hypertonic by the addition of NaCl induced activation of a heat-shock transcription factor (HSF). This activation, as monitored by gel-mobility-shift assays, occurred within 10 min of hypertonic shock and was dose-dependent in relation to the osmotic strength of the medium up to 0.7 osM. Competition analysis indicated that the effect of hypertonic shock on HSF binding activity was specific. The magnitude of the heat-shock element (HSE)-HSF binding induced by incubating the cells in a 0.7 osM medium was comparable in intensity and time course with that induced by a 44 mC heat shock. Following removal of the stressors, the decrease in HSF-HSE binding was more rapid in hypertonicity-shocked than in heat-shocked cells. Treatment of the cells with cycloheximide did not inhibit HSF-HSE binding, indicating that the activation was independent of new protein synthesis. By using a

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Activation of heat-shock transcription factor 1 by hypertonic shock in 3T3 cells

Alfieri

Petronini

Urbani

et al. 1996

Biochemical Journal

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“…HUVEC were cultured as previously described (20). Cells used in this study were all of early passages and were checked for the expression of von Willebrand factor by immunocytochemistry using a rabbit anti-human von Willebrand Factor (Dako, Milan, Italy) as primary antibody (30).…”

Section: Methodsmentioning

confidence: 99%

Change in Conformation with Reduction of α-Helix Content Causes Loss of Neutrophil Binding Activity in Fully Cytotoxic Shiga Toxin 1

Brigotti

Carnicelli

Arfilli

et al. 2011

Journal of Biological Chemistry

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Background:The role of Shiga toxins/neutrophils interactions in the pathogenesis of hemolytic uremic syndrome has been greatly debated. Results: We show that limited toxin unfolding induces loss of neutrophil binding activity while maintaining toxicity. Conclusion:The data indicate that Trp-203-related A chain moieties are recognized by neutrophils. Significance: We gain new insights into the structure/function relationship of these well known toxins, explaining some conflicting results.

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“…Protein synthesis was measured as the rate of incorporation of labeled leucine during a 30-minute incubation of the subconfluent cell monolayers in complete medium containing 50 mg/L leucine and trace amounts of [ 3 H]leucine as previously described (24).…”

Section: Analysis Of Protein Synthesis In Cellsmentioning

confidence: 99%

Novel Dyskerin-Mediated Mechanism of p53 Inactivation through Defective mRNA Translation

et al. 2010

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In up to 60% of human cancers, p53 gene mutations are responsible for direct inactivation of the tumor suppressor function of p53. Alternative mechanisms of p53 inactivation described thus far mainly affect its posttranslational regulation. In X-linked dyskeratosis congenita, a multisystemic syndrome characterized by increased cancer susceptibility, mutations of the DKC1 gene encoding dyskerin cause a selective defect in the translation of a subgroup of internal ribosome entry site (IRES)-containing cellular mRNAs. In this study, we show that impairment of dyskerin function can cause p53 inactivation due to a defect in p53 mRNA translation. siRNA-mediated reduction of dyskerin levels caused a decrease of p53 mRNA translation, protein levels, and functional activity, both in human breast cancer cells and in primary mammary epithelial progenitor cells. These effects seemed to be independent of the known role of dyskerin in telomerase function, and they were associated with a specific impairment of translation initiation mediated by IRES elements present in p53 mRNA. In a series of human primary breast cancers retaining wild-type p53, we found that low levels of dyskerin expression were associated with reduced expression of p53-positive target genes. Our findings suggest that a dyskerin-mediated mechanism of p53 inactivation may occur in a subset of human tumors. Cancer Res; 70(11); 4767-77. ©2010 AACR.

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Hyperosmolarity-induced stress proteins in chick embryo fibroblasts

Cited by 32 publications

References 17 publications

Activation of heat-shock transcription factor 1 by hypertonic shock in 3T3 cells

Activation of heat-shock transcription factor 1 by hypertonic shock in 3T3 cells

Change in Conformation with Reduction of α-Helix Content Causes Loss of Neutrophil Binding Activity in Fully Cytotoxic Shiga Toxin 1

Novel Dyskerin-Mediated Mechanism of p53 Inactivation through Defective mRNA Translation

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