Naslov
Cytotoxicity mechanism of human amylin involves phosphorylation of stress-activated protein kinases and caspase-3 activation

Autori
Rumora, Lada ; Hadžija, Mirko ; Barišić, Karmela ; Maysinger, Dusica ; Žanić Grubišić, Tihana

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

Izvornik
Kongres hrvatskih biokemičara i molekularnih biologa uz međunarodno sudjelovanje HB2000 Program i kniga sažetaka / Floegel, Mirna - Zagreb : Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 2000

Skup
Kongres hrvatskih biokemičara i molekularnih biologa uz međunarodno sudjelovanje HB2000

Mjesto i datum
Zagreb, Hrvatska, 13.10.2000. - 15.10.2000

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
Human amylin; Apoptosis; Mitogen-activated protein kinase; Caspase; RINm5F cells

Sažetak
Nanomolar concentrations of human amylin promote death of RINm5F cells in a time- and in a dose-dependent manner. Morphological changes of membrane and chromatin integrity suggest that cells are predominantly undergoing apoptosis, although necrotic cell death is also observed with higher (100nM and 1ěM) amylin concentrations. Activation of caspase-3 and mitogen-activated protein kinases (MAPKs) was detected by Western blot analysis. Human amylin induces significant activation of caspase-3 and strong and sustained phosphorylation of stress-activated protein kinases, JNK and p38. Caspase-3 activation precedes MAPKs activation. Our data suggest that activation of caspase-3 and stress-activated protein kinases has a role in human amylin-induced cytotoxicity of RINm5F cells.

Izvorni jezik
Engleski

Znanstvena područja
Temeljne medicinske znanosti

POVEZANOST RADA