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Histone H3 is Digested by Granzyme A During Compromised Cell Death in the Raji Cells
- Authors
- Lee, Phil Young; Park, Byoung Chul; Chi, Seung Wook; Bae, Kwang-Hee; Kim, Sunhong; Cho, Sayeon; Kim, Jeong-Hoon; Park, Sung Goo
- Issue Date
- Sep-2015
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Caspase-independent cell death; histone H3; granzyme A
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.25, no.9, pp 1578 - 1582
- Pages
- 5
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 25
- Number
- 9
- Start Page
- 1578
- End Page
- 1582
- ISSN
- 1017-7825
1738-8872
- 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.
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