Stress response decreases the interleukin-1β-induced production of complement component C3 in human intestinal epithelial cells

1999 ◽  
Vol 97 (3) ◽  
pp. 331-337 ◽  
Author(s):  
Ryan MOON ◽  
Timothy A. PRITTS ◽  
Alexander A. PARIKH ◽  
Josef E. FISCHER ◽  
Andrew L. SALZMAN ◽  
...  
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Blot Analysis ◽  
Sodium Arsenite ◽  
Cell Types ◽  
Complement Component ◽  
Interleukin 1Β ◽  
Epithelial Cell Line ◽  
Intestinal Epithelial ◽  
Complement Component C3

Interleukin-1β (IL-1β) increases the production of complement component C3 in enterocytes. Heat shock regulates the response to cytokines and other inflammatory mediators in various cell types. We tested the hypothesis that the heat-shock response regulates IL-1β-induced C3 production in the enterocyte. Cultured Caco-2 cells, a human intestinal epithelial cell line, were treated with sodium arsenite (10–500 µM) for 1 h or subjected to hyperthermia (43 °C) for 1–4 h, and allowed to recover for 1 h. The cells were then treated with IL-1β (0.5 ng/ml) for up to 24 h, whereafter C3 levels were measured by ELISA and C3 mRNA by Northern blot analysis. Heat-shock protein of 72 kDa (hsp72) was determined by Western blot analysis. Treatment of the cells with sodium arsenite or subjecting them to hyperthermia induced the expression of hsp72. The IL-1β-induced expression of C3 mRNA and C3 production were down-regulated by hyperthermia and sodium arsenite in a dose-dependent fashion. The results suggest that the stress response induced by hyperthermia or sodium arsenite decreases IL-1β-induced C3 production in human enterocytes.

Proteasome inhibitors induce heat shock response and increase IL-6 expression in human intestinal epithelial cells

2002 ◽  
Vol 282 (4) ◽  
pp. R1016-R1026 ◽  
Author(s):  
Timothy A. Pritts ◽  
Eric S. Hungness ◽  
Dan D. Hershko ◽  
Bruce W. Robb ◽  
Xiaoyan Sun ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Proteasome Inhibitors ◽  
Proteasome Inhibition ◽  
Cell Types ◽  
Epithelial Cell Line ◽  
Intestinal Epithelial ◽  
Heat Shock Factors ◽  
Gene And Protein Expression ◽  
Shock Response

In previous studies, the heat shock response, induced by hyperthermia or sodium arsenite, increased interleukin (IL)-6 production in intestinal mucosa and cultured human enterocytes. A novel way to induce the heat shock response, documented in other cell types, is treatment with proteasome inhibitors. It is not known if proteasome inhibition induces heat shock in enterocytes or influences IL-6 production. Here we tested the hypothesis that treatment of cultured Caco-2 cells, a human intestinal epithelial cell line, with proteasome inhibitors induces the heat shock response and stimulates IL-6 production. Treatment of Caco-2 cells with one of the proteasome inhibitors MG-132 or lactacystin activated the transcription factor heat shock factors (HSF)-1 and -2 and upregulated cellular levels of the 72-kDa heat shock protein HSP-72. The same treatment resulted in increased gene and protein expression of IL-6, a response that was blocked by quercetin. Additional experiments revealed that the IL-6 gene promoter contains a HSF-responsive element and that the IL-6 gene may be regulated by the heat shock response. The present results suggest that proteasome inhibition induces heat shock response and IL-6 production in enterocytes and that IL-6 may be a heat shock-responsive gene, at least under certain circumstances. The observations are important considering the multiple biological roles of IL-6, both locally in the gut mucosa and systemically, and considering recent proposals in the literature to use proteasome inhibitors in the clinical setting to induce the heat shock response.

scholarly journals Extrathymic production of thymulin induced by oxidative stress, heat shock, apoptosis, or necrosis

2017 ◽  
Vol 30 (1) ◽  
pp. 58-69 ◽  
Author(s):  
Sergey M Lunin ◽  
Maxim O Khrenov ◽  
Olga V Glushkova ◽  
Elena V Vinogradova ◽  
Valery A Yashin ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Molecular Weight ◽  
Stress Response ◽  
Heat Shock ◽  
Cell Types ◽  
Cell Nuclei ◽  
Sequence Comparisons ◽  
Blast Search ◽  
Thymic Peptides ◽  
Thymic Peptide

Thymic peptides are immune regulators produced mainly in the thymus. However, thymic peptides such as thymosin-α and thymopoietin have precursors widely expressed outside the thymus, localized in cell nuclei, and involved in vital nuclear functions. In stress-related conditions, they can relocalize. We hypothesized that another thymic peptide, thymulin, could be similarly produced by non-thymic cells during stress and have a precursor therein. Non-thymic cells, including macrophages and fibroblasts, were exposed to oxidative stress, heat, apoptosis, or necrosis. Extracellular thymulin was identified in media of both cell types 2 h after exposure to stress or lethal signals. Therefore, thymulin is released by non-thymic cells. To examine possible thymulin precursors in non-thymic cells, macrophage lysates were analyzed by western blotting. Bands stained with anti-thymulin antibody were detected in two locations, approximately 60 kDa and 10 kDa, which may be a possible precursor and intermediate. All of the exposures except for heat were effective for induction of the 10 kDa protein. BLAST search using thymulin sequence identified SPATS2L, an intranucleolar stress-response protein with molecular weight of 62 kDa, containing thymulin-like sequence. Comparisons of blots stained with anti-thymulin and anti-SPATS2L antibodies indicate that SPATS2L may be a possible candidate for the precursor of thymulin.

scholarly journals Candida albicansinfection leads to barrier breakdown and a MAPK/NF-κB mediated stress response in the intestinal epithelial cell line C2BBe1

2016 ◽  
Vol 18 (7) ◽  
pp. 889-904 ◽  
Author(s):  
Michael Böhringer ◽  
Susann Pohlers ◽  
Sylvie Schulze ◽  
Daniela Albrecht-Eckardt ◽  
Judith Piegsa ◽  
...  
Keyword(s):  
Stress Response ◽  
Epithelial Cell ◽  
Cell Line ◽  
Intestinal Epithelial Cell ◽  
Epithelial Cell Line ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Cell Line ◽  
Barrier Breakdown

scholarly journals Mammalian orthoreovirusinfection is enhanced in cells pre-treated with sodium arsenite

2019 ◽  
Author(s):  
Michael M. Lutz ◽  
Megan P. Worth ◽  
Meleana M. Hinchman ◽  
John S. L. Parker ◽  
Emily D. Ledgerwood
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Protein Expression ◽  
Stress Responses ◽  
Sodium Arsenite ◽  
Integrated Stress Response ◽  
Reovirus Infection ◽  
Cellular Stress Responses ◽  
Pre Treatment ◽  
Reovirus Replication

ABSTRACTFollowing reovirus infection, cells activate stress responses that repress canonical cellular translation as a mechanism to limit production of progeny virions. This includes the formation of stress granules (SG) that sequester translationally-stalled cellular transcripts, translation initiation factors, ribosomal proteins, and RNA binding proteins until conditions improve and translation can resume. Work by others suggests that these cellular stress responses, which are part of the integrated stress response, may benefit rather than repress reovirus replication. In agreement with this, we report that stressing cells prior to infection with sodium arsenite (SA), a robust inducer of SG and activator of eIF2α kinases, enhanced viral protein expression, percent infectivity and viral titer in SA-treated cells compared to untreated cells. SA-mediated enhancement of reovirus replication was not strain-specific, but was cell-type specific. While pre-treatment of cells with SA offered the greatest enhancement, treatment of infected cultures as late as 4 h post infection resulted in an increase in the percent of cells infected. SA activates the HRI kinase, which phosphorylates eIF2α and subsequently induces SG formation. Other stresses, such as heat shock (HS) and osmotic shock also activate HRI. Heat shock of cells prior to reovirus infection readily induced SG in greater than 85% of cells. Although HS pre-treatment had no effect on the percentage of infected cells or viral yield, it did enhance viral protein expression. These data suggest that SA pre-treatment perturbs the cell in a way that is beneficial for reovirus and that neither HRI activation nor SG induction is sufficient for reovirus infection enhancement.SIGNIFICANCEAll viruses rely on the host translational machinery for the synthesis of viral proteins. In response to viral infection, cells activate the integrated stress response resulting in the phosphorylation of eIF2α and translation shutoff. Despite this, reovirus replicates to reduced titers in the absence of this response. In this work, we report that sodium arsenite activation of the integrated stress response prior to virus inoculation enhances virus infectivity, protein expression and titer. Together, these data suggest that modulation of conserved cellular stress responses can alter reovirus replication.

Heat shock gene expression in Xenopus laevis A6 cells in response to heat shock and sodium arsenite treatments

1988 ◽  
Vol 66 (8) ◽  
pp. 862-870 ◽  
Author(s):  
S. Darasch ◽  
D. D. Mosser ◽  
N. C. Bols ◽  
J. J. Heikkila
Keyword(s):  
Heat Shock ◽  
Xenopus Laevis ◽  
Sodium Arsenite ◽  
Polyacrylamide Gel Electrophoresis ◽  
Heat Shock Gene ◽  
Epithelial Cell Line ◽  
Continuous Exposure ◽  
Mrna Levels ◽  
Hsp 70 ◽  
Mrna Accumulation

Continuous exposure of a Xenopus laevis kidney epithelial cell line, A6, to either heat shock (33 °C) or sodium arsenite (50 μM) resulted in transient but markedly different temporal patterns of heat-shock protein (HSP) synthesis and HSP 70 and 30 mRNA accumulation. Heat-shock-induced synthesis of HSPs was detectable within 1 h and reached maximum levels by 2–3 h. While sodium arsenite induced the synthesis of some HSPs within 1 h, maximal HSP synthesis did not occur until 12 h. The pattern of HSP 70 and 30 mRNA accumulation was similar to the response observed at the protein level. During recovery from heat shock, a coordinate decline in HSPs and HSP 70 and 30 mRNA was observed. During recovery from sodium arsenite, a similar phenomenon occurred during the initial stages. However, after 6 h of recovery, HSP 70 mRNA levels persisted in contrast to the declining HSP 30 mRNA levels. Two-dimensional polyacrylamide gel electrophoresis revealed the presence of 5 HSPs in the HSP 70 family, of which two were constitutive, and 16 different stress-inducible proteins in the HSP 30 family. In conclusion, heat shock and sodium arsenite induce a similar set of HSPs but maximum synthesis of the HSP is temporally separated by 12–24 h.

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