umu.sePublikasjoner
Endre søk
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Geldanamycin activates Hsp70 response and attenuates okadaic acid-induced cytotoxicity in human retinal pigment epithelial cells.
Department of Ophthalmology, University of Kuopio, Kuopio, Finland; Department of Ophthalmology, Kuopio University Hospital, Kuopio, Finland.
Department of Ophthalmology, University of Kuopio, Kuopio, Finland.
Department of Anatomy, University of Kuopio, Kuopio, Finland.
Department of Neuroscience and Neurology, University of Kuopio, Kuopio, Finland.
Vise andre og tillknytning
2005 (engelsk)Inngår i: Brain Research. Molecular Brain Research, ISSN 0169-328X, E-ISSN 1872-6941, Vol. 137, nr 1-2, s. 126-131, artikkel-id 15950770Artikkel i tidsskrift (Fagfellevurdert) Published
Fritextbeskrivning
Abstract [en]

Reversible protein phosphorylation regulates the biological activities of many human proteins involved in crucial cellular processes, e.g., protein-protein interactions, cell signaling, gene transcription, cell growth, and death. A malfunction of cellular homeostasis in retinal pigment epithelial (RPE) cells is involved in the age-related retinal degeneration. In this study, we examined cytotoxicity in human RPE cells subjected to the protein phosphatase inhibitor, okadaic acid (OA). Moreover, the influence of Hsp90 inhibitor geldanamycin (GA), a benzoquinone ansamycin, in cytoprotection was assessed. Hsp70 protein levels were analyzed by Western blot. Cellular viability was determined by LDH and MTT assays. To study apoptotic cell death, caspase-3 enzyme activity was measured by assaying the cleavage of a fluorescent peptide substrate and Hoechst dye was used to visualize nuclear morphology. OA treatment caused morphological changes and induced cytotoxicity by caspase-3-independent manner in the RPE cells. No evidence of nuclear fragmentation was observed in response to OA. Interestingly, GA treatment accumulated Hsp70 protein and attenuated OA-induced cytotoxicity. This study suggests that Hsp70 and Hsp90 are closely related to cytoprotection of RPE cells in response to protein phosphatase inhibition.

sted, utgiver, år, opplag, sider
Elsevier, 2005. Vol. 137, nr 1-2, s. 126-131, artikkel-id 15950770
Emneord [en]
Opthalmology, retinal pigment epithelial cells, geldanamycin, heat shock protein, cell viability
HSV kategori
Forskningsprogram
biokemi; cellforskning; oftalmiatrik
Identifikatorer
URN: urn:nbn:se:umu:diva-106656DOI: 10.1016/j.molbrainres.2005.02.027PubMedID: 15950770OAI: oai:DiVA.org:umu-106656DiVA, id: diva2:843222
Tilgjengelig fra: 2015-07-27 Laget: 2015-07-27 Sist oppdatert: 2018-06-07

Open Access i DiVA

Fulltekst mangler i DiVA

Andre lenker

Forlagets fulltekstPubMedArticle web page

Personposter BETA

Lammi, Mikko

Søk i DiVA

Av forfatter/redaktør
Lammi, Mikko
I samme tidsskrift
Brain Research. Molecular Brain Research

Søk utenfor DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric

doi
pubmed
urn-nbn
Totalt: 137 treff
RefereraExporteraLink to record
Permanent link

Direct link
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annet format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annet språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf