Cytotoxicity mechanism of human amylin involves phosphorylation of stress-activated protein kinases and caspase-3 activation (CROSBI ID 478978)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | domaća recenzija
Podaci o odgovornosti
Rumora, Lada ; Hadžija, Mirko ; Barišić, Karmela ; Maysinger, Dusica ; Žanić Grubišić, Tihana
engleski
Cytotoxicity mechanism of human amylin involves phosphorylation of stress-activated protein kinases and caspase-3 activation
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.
Human amylin; Apoptosis; Mitogen-activated protein kinase; Caspase; RINm5F cells
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Podaci o prilogu
110-x.
2000.
objavljeno
Podaci o matičnoj publikaciji
Kongres hrvatskih biokemičara i molekularnih biologa uz međunarodno sudjelovanje HB2000 Program i kniga sažetaka
Floegel, Mirna
Zagreb: Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu
Podaci o skupu
Kongres Hrvatskih Biokemičara i Molekularnih Biologa uz međunarodno sudjelovanje HB2000
poster
13.10.2000-15.10.2000
Zagreb, Hrvatska