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This galley proof is being listed electronically before publishing the final manuscript (It's not final version).

 
Histone H4 is cleaved by granzyme A during staurosporine-induced cell death in B-lymphoid Raji cells
Phil Young Lee1,4, Byoung Chul Park1, Seung Wook Chi1, Kwang Hee Bae2, Sunhong Kim1, Sayeon Cho3, Seongman Kang4, Jeong-Hoon Kim5, Sung Goo Park1,*
1Disease Target Structure Research Center and 2Metabolic Regulation Research Center, KRIBB,
3College of Pharmacy, Chung-Ang University,
4Division of Life Sciences, Korea University,
5Personalized Genomic Medicine Research Center, KRIBB
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.
Abstract, Accepted Manuscript(in press) [Submitted on June 27, 2016, Accepted on July 20, 2016]
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