Glycosylation modification of human prion protein provokes apoptosis in HeLa cells in vitro.

Abstract:

:We investigate the correlation between the glycosylation modified prion proteins and apoptosis. The wild-type PRNP gene and four PRNP gene glycosylated mutants were transiently expressed in HeLa cells. The effect of apoptosis induced by PrP mutants was confirmed by MTT assay, Hochest staining, Annexin-V staining and PI staining. ROS test detected ROS generation within the cells. The mitochondrial membrane potential was analyzed by the flow cytometry. The expression levels of Bcl-xL, Bax, cleaved Caspase-9 proteins were analyzed by Western Blot. The results indicated that the expressed non-glycosylated PrP in HeLa cells obviously induced apoptosis, inhibited the growth of cells and reduced the mitochondrial membrane potential, and more ROS generation and low levels of the apoptosis-related proteins Bcl-xL, the activated the cleaved Caspase-9 proteins were found. The apoptosis induced by non-glycosylated PrP demonstrates that its underlying mechanism correlates with the mitochondria-mediated signal transduction pathway.

journal_name

BMB Rep

journal_title

BMB reports

authors

Yang Y,Chen L,Pan HZ,Kou Y,Xu CM

doi

10.5483/bmbrep.2009.42.6.331

subject

Has Abstract

pub_date

2009-06-30 00:00:00

pages

331-7

issue

6

eissn

1976-6696

issn

1976-670X

journal_volume

42

pub_type

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