Neuronal cells show regulatory differences in the hsp70 gene response

Kaarniranta, Kai; Oksala, Niku; Karjalainen, Hannu M.; Suuronen, Tiina; Sistonen, Lea; Helminen, Heikki J.; Salminen, Antero; Lammi, Mikko J.

doi:10.1016/s0169-328x(02)00179-1

Cited by 41 publications

(29 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…3 and 4). In support of the HN10 cell data, a previous study on rat primary hippocampal neurons documented a lack of Hsf1 and Hsp70 induction after heat shock in contrast to several other neuronal cell types investigated (35). Inhibition of protein synthesis with cycloheximide or overexpression of dominant negative Hsf1 attenuated Hsp70 induction in HdhQ150 cells but did not inhibit NVP-AUY922-induced mHtt degradation (Fig.…”

Section: Discussionsupporting

confidence: 74%

A Screen for Enhancers of Clearance Identifies Huntingtin as a Heat Shock Protein 90 (Hsp90) Client Protein

Baldo

Weiss

Parker

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Molecular chaperones assist in the folding of metastable proteins implicated in neurodegenerative diseases. Results: Huntingtin is a heat shock protein 90 (Hsp90) client protein. Conclusion:Hsp90 inhibition-mediated degradation of soluble mutant huntingtin is independent of a cellular heat shock response. Significance: Mechanisms targeting Hsp90 chaperone function may provide new treatments for Huntington disease.

show abstract

Section: Discussionsupporting

confidence: 74%

A Screen for Enhancers of Clearance Identifies Huntingtin as a Heat Shock Protein 90 (Hsp90) Client Protein

Baldo

Weiss

Parker

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…The induction of heat shock proteins is largely regulated at the transcriptional level (Kaarniranta et al, 2002). However, in the present study, the transcription of hsp60 mRNA in heat stressed rat myocardial cells differed in vivo and in vitro.…”

Section: Discussioncontrasting

confidence: 59%

Association of Hsp60 expression with damage to rat myocardial cells exposed to heat stress in vivo and in vitro

et al. 2014

View full text Add to dashboard Cite

ABSTRACT. To investigate the protective role of Hsp60 against stress damage and its role in the sudden death of stressed animals, changes in the levels of Hsp60 protein and hsp60 mRNA of myocardial cells in vivo and in vitro were studied. In addition, the relationship between Hsp60 expression and heat-induced damage was also studied. Rats were exposed to a temperature of 42° ± 1°C for 0, 20, 40, 60, 80, or 100 min. More than 50% of the rats died suddenly within 100 min. With increasing heat stress duration, hsp60 mRNA levels significantly increased in both in vivo and in vitro rat myocardial cells; however, a similar trend was not observed for Hsp60 protein levels. Although the changes observed in Hsp60 expression in myocardial cells in vitro were inconsistent with those of rat heart tissues in vivo, Hsp60 expression levels were consistent with the histopathological damage observed in myocardial cells both in vivo and in vitro. Differences in Hsp60 expression may reflect the degree of injury sustained by myocardial cells in vivo and in vitro. As a mitochondrial protein, Hsp60 represents a potential biomarker of heat stress, and may protect against heat stress induced myocardial cellular damage both in vivo and in vitro.

show abstract

“…The analysis was performed as described previously by our group [9,10,26,27]. Briefly, the tissue samples were homogenized and sonicated and protein extracts (30 Ìg protein per lane) were electrophoresed on SDS-PAGE and transferred to a nitrocellulose membrane (Millipore, Bedford, Mass., USA) which was stained with Ponceau S solution (Sigma, St. Louis, Mo., USA), and checked for an even loading and transfer.…”

Section: Western Blot Analysis Of Hsp60mentioning

confidence: 99%

Heat Shock Preconditioning and Eicosanoid Pathways Modulate Caspase 3-Like Activity in Superficially Injured Isolated Guinea Pig Gastric Mucosa

Oksala

Alhava²,

Paimela³

2004

Eur Surg Res

Self Cite

View full text Add to dashboard Cite

Background: After superficial mucosal injury, the disturbed gastric epithelial continuity is restored by cellular migration. Caspase-3 is an enzyme responsible for the execution of stress-induced apoptosis. Interestingly, heat shock proteins (Hsp) including Hsp60 are capable of modulating caspase-3 activity. Interestingly, we have demonstrated that heat shock preconditioning upregulates Hsp synthesis and inhibits restitution and cell proliferation via mechanisms related to de novo protein synthesis and eicosanoid pathways, both of which are crucial in the regulation of apoptosis and gastric mucosal defense systems. Aims: To assess whether caspase-3 activity is affected by heat shock preconditioning and associated pharmacological modulations after standard superficial injury to allow development of cytoprotective strategies. Methods: Guinea pig gastric mucosae were mounted and perfused in paired Ussing chambers. After heat shock (HS) preconditioning (42°C) for 30 min, a superficial injury was induced (1.25 mol/l NaCl) followed by 3 h recovery. For mechanistic studies, the mucosa was exposed to 30 µmol/l arachidonic acid (AA) as a substrate for eicosanoid pathways, to 50 µmol/l quercetin (Q) to inhibit lipoxygenases, to 50 µmol/l indomethacin (In) to inhibit cyclo-oxygenases, or to 150 µmol/l cycloheximide (CHX) to inhibit de novo protein synthesis. After the experiment, the mucosa was prepared for analysis of caspase-3 activity. Hsp60 expression was analyzed to monitor the induction of heat shock response. Results: HS upregulated Hsp60 expression, indicating induction of the heat shock response without an effect on basal caspase-3 activity. Superficial injury itself did not affect caspase-3 activity nor Hsp60 synthesis. In all the experiments, exposure to CHX abolished caspase-3 activity and Hsp60 synthesis. AA+Q increased, Q decreased, while In+AA and In+AA+Q abolished caspase-3 activity independent of alterations in Hsp60 synthesis. Upon exposure to In+Q, HS decreased caspase-3 activity and upregulated Hsp60 synthesis. Conclusion: Caspase-3 activity in isolated guinea pig gastric mucosa is regulated by mechanisms dependent on de novo protein synthesis and eicosanoid pathways but is not strictly related to Hsp synthesis. Upon modulation of the eicosanoid pathways, HS may be utilized to simultaneously decrease caspase-3 activity and increase Hsp synthesis. Modulations of the eicosanoid pathways may be utilized to reduce caspase-3 activity also upon normothermic conditions suggesting a novel mechanism by which caspase-3 is regulated in the gastric mucosa.

show abstract

Neuronal cells show regulatory differences in the hsp70 gene response

Cited by 41 publications

References 30 publications

A Screen for Enhancers of Clearance Identifies Huntingtin as a Heat Shock Protein 90 (Hsp90) Client Protein

A Screen for Enhancers of Clearance Identifies Huntingtin as a Heat Shock Protein 90 (Hsp90) Client Protein

Association of Hsp60 expression with damage to rat myocardial cells exposed to heat stress in vivo and in vitro

Heat Shock Preconditioning and Eicosanoid Pathways Modulate Caspase 3-Like Activity in Superficially Injured Isolated Guinea Pig Gastric Mucosa

Contact Info

Product

Resources

About