The Role of Polyamination in Apoptosis
Date Issued
2012
Date
2012
Author(s)
Lee, Yueh-Ling
Abstract
Apoptosis is an autonomous cell-death phenomenon, whose underlying mecha-nisms remain to be investigated. The involvement of transglutaminse II, polyamine and polyamination in apoptosis, and identities of polyamine-modified proteins have been vigorously studied in recent years.
In this study, we have generated an anti-spermine antiserum and confirm that pol-yamination is regulated by the transamidation activity of transglutaminse II and poly-amine in staurosporine-induced apoptosis in HeLa cells. The increase in polyamination in HeLa cells induced by staurosporine is dose-dependent. Treatment with cystamine, an inhibitor of transglutaminse II, decreased the transamidation activity, polyamination and cell death of HeLa cells. This suggests the transamidation activity of transglutaminse II is pro-apoptosis in HeLa cells. Depletion of spermine level in HeLa cells accelerates apoptosis; this suggests the role of polyamine in HeLa cells is pro-cell survival. The identification of two major polyamine-modified proteins, molecular weight of about 14 and 20 kDa, in apoptosis are in progress.
We have previously identified HtrA2/Omi, an important pro-apoptosis protein, as a spermine-binding protein. In this study, we confirm HtrA2/Omi is a polyamine-modified protein in HeLa cells, but the physiological function of polyamination of this protein requires further investigation.
Subjects
apoptosis
transglutaminse II
polyamine
polyamination
Type
thesis
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