Histone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells

Cited 11 time in scopus
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Title
Histone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells
Author(s)
Phil Young Lee; Byoung Chul ParkSeung-Wook ChiKwang-Hee Bae; Sunhong Kim; S Cho; S Kang; Jeong Hoon KimSung Goo Park
Bibliographic Citation
BMB Reports, vol. 49, no. 10, pp. 560-565
Publication Year
2016
Abstract
Granzyme A (GzmA) was first identified as a cytotoxic T lymphocyte protease protein with limited tissue expression. A number of cellular proteins are known to be cleaved by GzmA, and its function is to induce apoptosis. Histones H1, H2B, and H3 were identified as GzmA substrates during apoptotic cell death. Here, we demonstrated that histone H4 was cleaved by GzmA during staurosporine-induced cell death; however, in the presence of caspase inhibitors, staurosporine-treated Raji cells underwent necroptosis instead of apoptosis. Furthermore, histone H4 cleavage was blocked by the GzmA inhibitor nafamostat mesylate and by GzmA knockdown using siRNA. These results suggest that histone H4 is a novel substrate for GzmA in staurosporine-induced cells.
Keyword
Caspase-independent cell deathGranzyme AHistone H4Raji cell
ISSN
1225-8687
Publisher
South Korea
DOI
http://dx.doi.org/10.5483/BMBRep.2016.49.10.105
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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