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Hsp90 inhibitor geldanamycin increases hsp70 mRNA stabilisation but fails to activate HSF1 in cells exposed to hydrostatic pressure.
Department of Anatomy, University of Kuopio, Kuopio, Finland.
Department of Opthalmology, Kuopio University Hospital, Kuopio, Finland.
Department of Anatomy, University of Kuopio, Kuopio, Finland.
Department of Anatomy, University of Kuopio, Kuopio, Finland. (Chondrogenic and Osteogenic Differentiation Group)ORCID iD: 0000-0002-6181-9904
2005 (English)In: Biochimica et Biophysica Acta, ISSN 0006-3002, E-ISSN 1878-2434, Vol. 1743, no 1-2, 115-119 p., 15777846Article in journal (Refereed) Published
Abstract [en]

High hydrostatic pressure (HP) increases Hsp70 protein and mRNA levels by increasing the mRNA half-life without activation of HSF1 transcription factor. We investigated whether this change in gene expression requires Hsp90, previously shown to regulate hsp70 genes via HSF1. In HeLa cells, both HP and Hsp90 inhibitor geldanamycin (GA) up-regulated Hsp70 expression through mRNA stabilisation. GA, unlike HP, increased HSF1 activation. However, when exposures were used together a marked Hsp70 response was observed with mRNA stabilisation without coincidence of HSF1 activation. Our data suggests that Hsp90 is involved in hsp70 mRNA stabilisation and the HSF1 activation can be suppressed by high HP.

Place, publisher, year, edition, pages
Elsevier, 2005. Vol. 1743, no 1-2, 115-119 p., 15777846
Keyword [en]
Heat shock protein, geldanamycin, hydrostatic pressure, stress response, mRNA stabilization
National Category
Cell and Molecular Biology Biochemistry and Molecular Biology
Research subject
Biochemistry; cellforskning
Identifiers
URN: urn:nbn:se:umu:diva-106660DOI: 10.1016/j.bbamcr.2004.09.004PubMedID: 15777846OAI: oai:DiVA.org:umu-106660DiVA: diva2:843257
Available from: 2015-07-28 Created: 2015-07-28 Last updated: 2017-12-04

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CiteExportLink to record
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