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http://dx.doi.org/10.5483/BMBRep.2016.49.10.105

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

Lee, Phil Young (Disease Target Structure Research Center)
Park, Byoung Chul (Disease Target Structure Research Center)
Chi, Seung Wook (Disease Target Structure Research Center)
Bae, Kwang-Hee (Metabolic Regulation Research Center)
Kim, Sunhong (Disease Target Structure Research Center)
Cho, Sayeon (College of Pharmacy, Chung-Ang University)
Kang, Seongman (Division of Life Sciences, Korea University)
Kim, Jeong-Hoon (Personalized Genomic Medicine Research Center, Korea Research Institute of Bioscience & Biotechnology (KRIBB))
Park, Sung Goo (Disease Target Structure Research Center)
Publication Information
BMB Reports / v.49, no.10, 2016 , pp. 560-565 More about this Journal
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.
Keywords
Caspase-independent cell death; Granzyme A; Histone H4; Raji cell;
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Times Cited By KSCI : 2  (Citation Analysis)
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