Naslov
Effects of inducible Hsp70 on staurosporine induced apoptosis

Autori
Matokanović, Mirela ; Novak, Ruđer ; Barišić, Karmela

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
The FEBS Journal 276, Supplement 1 (2009), Abstracts of the 34th FEBS Congress / - : Wiley-Blackwell, 2009, 212-212

Skup
34th FEBS Congress: "Life's Molecular Interactions"

Mjesto i datum
Prag, Češka Republika, 04.07.2009. - 09.07.2009

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
apoptosis; staurosporine; heat shock; Hsp70

Sažetak
Apoptosis, the process of programmed cell death, is characterized by a sequence of precisely regulated events that culminate in the self destruction of a cell. Expression of heat shock proteins (Hsp) is known to correlate with increased resistance to apoptosis induced by a range of diverse cytotoxic agents and has been implicated in chemotherapeutic resistance of tumors and carcinogenesis. Staurosporine, often used for apoptosis induction, is an alkaloid with ability to inhibit protein kinases through the prevention of ATP binding. Hsp70 is one of the major heat shock inducible proteins of the Hsp family. Jurkat cells (acute T cell leukemia), if exposed to heat stress (30 minutes, 44°C), express higher concentration of inducible Hsp70 (9-12.5 times elevation compared to the control cells), depending on the time left for the recovery in custom cell culture conditions. Induction of apoptosis with staurosporine was assessed at morphological level, by Flow Cytometry analysis, and at the level of terminal event of cell death, DNA fragmentation, by immune detection of single- and double-stranded DNA breaks. It is shown that increased concentration of inducible Hsp70 shifts the percentage of live cells from 37% to 55% (1, 5x), predicting the role of inducible Hsp70 in protection against staurosporine induced apoptosis with involvement of 36%.

Izvorni jezik
Engleski

Znanstvena područja
Temeljne medicinske znanosti

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