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Titolo:
Geldanamycin induces heat shock protein expression through activation of HSF1 in K562 erythroleukemic cells
Autore:
Kim, HR; Kang, HS; Kim, HD;
Indirizzi:
Pusan Natl Univ, Dept Mol Biol, Coll Nat Sci, Pusan 609735, South Korea Pusan Natl Univ Pusan South Korea 609735 Sci, Pusan 609735, South Korea
Titolo Testata:
IUBMB LIFE
fascicolo: 4, volume: 48, anno: 1999,
pagine: 429 - 433
SICI:
1521-6543(199910)48:4<429:GIHSPE>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTOR HSF1; COMPLEX; STRESS; OLIGOMERIZATION; VARIETY; GROWTH;
Keywords:
geldanamycin; HSF1; HSP70; HSP90; K562 erythroleukemic cells;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Kang, HS Pusan Natl Univ, Dept Mol Biol, Coll Nat Sci, Pusan 609735, SouthKorea Pusan Natl Univ Pusan South Korea 609735 an 609735, South Korea
Citazione:
H.R. Kim et al., "Geldanamycin induces heat shock protein expression through activation of HSF1 in K562 erythroleukemic cells", IUBMB LIFE, 48(4), 1999, pp. 429-433

Abstract

HSP90 is one of the most abundant heat shock proteins (HSPs) in eukaryoticcells and is found in complex with several regulatory proteins such as kinases and transcription factors. Geldanamycin (GA), a benzoquinone ansamycin, specifically binds to HSP90 and disrupts the interaction of HSP90 and target proteins. Thus, GA has been used as a specific inhibitor of HSP90. In this study, we examined whether GA could affect protein synthesis and gene expression in the human erythroleukemic cell line K562. Treatment with GA, but not herbimycin A (another benzoquinone ansamycin), highly induced a 70-kDa protein, which was revealed to be HSP70 by immunoblotting and immunoprecipitation with anti-HSP70 antibody The expression of HSP28 was also enhanced by GA. Furthermore, GA induced the activation of heat shock factor 1 (HSF1), but not HSF2, as determined by electromobility shift and electromobility supershift assay. In addition, similar to heat shock treatment, GA inducted the phosphorylation of HSF1. Heat shock element-binding activity and phosphorylation of HSF1 were attenuated 3 h after GA treatment, These results indicate that the functional inactivation of HSP90 by GA potentially stimulates the expression of heat shock proteins through activation of HSF1.

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Documento generato il 03/04/20 alle ore 08:05:46