Effects of Hsp90 inhibition on galectin3 expression in human monocytic cell line THP1 (CROSBI ID 631318)
Prilog sa skupa u časopisu | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Dumić, Jerka ; Dabelić, Sanja ; Zorbaz, Tamara ; Šupraha Goreta, Sandra ; Petrik, Jozsef ; Čulić, Ognjen ; Barišić, Karmela
engleski
Effects of Hsp90 inhibition on galectin3 expression in human monocytic cell line THP1
Inhibition of Hsp90 is a promising therapeutic approach with clinical relevance for treatment of specific tumour types since both Hsp90 homologous (Hsp90α and Hsp90β) account for maturation and functional stability of a plethora of polypeptides (Hsp90 client proteins), including many proteins involved in tumorigenesis (e.g. antiapoptotic and signaltransduction proteins, transcription factors, Tyrkinase receptors, etc.). Galectin3, a βgalactoside lectin is a multifunctional protein, ubiquitously expressed in both intracellular and extracellular environments as well as on the surface of different cell types. Intracellular galectin3, recognised as a strong antiapoptotic molecule, is well known for its roles being correlated with the development and malignancy of cancers and cancer drug resistance. We studied the effects of antibiotic geldanamycin, 17DMAG [17( dimethylaminoethyl amino)17demethoxygeldanamycin], an orally bioavailable derivative of ansamycin and siRNA directed to Hsp90α mRNA (Hsp90αsiRNA) on the expression of galectin3, different heat shock protein family members and Hsp90 client proteins involved in cell cycle regulation in human monocytic cell line THP1. Although slight transient increase of galectin3 expression was observed after 24 hours of both treatments, with 17DMAG, and with Hsp90αsiRNA, inhibition of Hsp90 had no significant effect on galectin3 expression. 17DMAG slightly induced the expression of both Hsp90α and Hsp90β, while Hsp90αsiRNA treatment resulted in inhibition of Hsp90α expression, but did not affect Hsp90β expression. While 17DMAG tremendously upregulated expression of HSP70, cdk1, p(Tyr)cdk1, and cdk2, and did not affect Hsp27 expression, Hsp90αsiRNA did not affected any of aforementioned proteins. These results encourage for further studies focused on elucidation of galectin3 in apoptosis and tumorigenesis.
Hsp90 ; THP-1 ; galectin-3 ; 17-DMAG
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Podaci o prilogu
156-156.
2015.
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objavljeno
10.1111/febs.13339
Podaci o matičnoj publikaciji
The FEBS journal
Berlin: Federation of European Biochemical Societies (FEBS)
1742-464X
1742-4658
Podaci o skupu
40th Congress of The Federation of the European Biochemical Societies 'The Biochemical Basis of Life'
poster
04.07.2015-09.07.2015
Berlin, Njemačka