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Title 

Histone H3 is digested by granzyme A during compromised cell death in the Raji cells

Authors 

Phil Young LeeByoung Chul ParkSeung-Wook ChiKwang-Hee BaeSunhong KimS ChoJeong Hoon KimSung Goo Park

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

2015

Citation 

Journal of Microbiology and Biotechnology, vol. 25, no. 9, pp. 1578-1582

Keywords 

Caspase-independent cell deathGranzyme AHistone H3

Abstract 

Granzyme A (GzmA) was identified as a cytotoxic T lymphocyte protease protein expressed in the nucleus. A number of nuclear proteins are well known as GzmA substrates, and GzmA is related with caspase-independent apoptosis. Histones H1, H2B, and H3 were identified as GzmA substrates through in vitro experiment with purified nucleosome. Here, we demonstrated that histone H3 was cleaved by GzmA in vivo during staurosporine-induced cell death. Moreover, histone H3 cleavage was blocked by the GzmA inhibitor nafamostat mesylate and by GzmA knockdown using siRNA. Taken together, we verified that histone H3 is a real substrate for GzmA in vivo in the Raji cells treated by staurosporin.

ISSN 

1017-7825

Link 

http://dx.doi.org/10.4014/jmb.1503.03088

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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