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Inhibition of HeLa Cell Apoptosis by Storage‐Protein 2
Author(s) -
Rhee Won Jong,
Lee Eun Hee,
Park Ju Hyun,
Lee Ji Eun,
Park Tai Hyun
Publication year - 2007
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp0702065
Subject(s) - hemolymph , hela , apoptosis , dna fragmentation , microbiology and biotechnology , inhibitor of apoptosis , staurosporine , biology , programmed cell death , cell , biochemistry , signal transduction , protein kinase c
Apoptosis is a barrier to maintaining high viable cell densities in animal cell culture. Silkworm hemolymph and its 30K protein have been reported to exhibit anti‐apoptotic activity in various mammalian and insect cell systems. The 30K protein is thermally unstable at temperatures higher than 60 °C; however, the silkworm hemolymph heat‐treated at 70–80 °C still exhibited anti‐apoptotic activity. This indicates that silkworm hemolymph contains another anti‐apoptotic compound other than 30K protein. In this article, the anti‐apoptotic molecule other than 30K protein was found from the silkworm hemolymph and identified. This molecule was storage‐protein 2 (SP2), which has no homology with any known anti‐apoptotic protein. This molecule was heat‐stable up to 80 °C, while 30K protein lost its activity at temperatures higher than 60 °C. When apoptosis was induced by staurosporine in HeLa cells, SP2 protein suppressed nuclear fragmentation and apoptotic body formation. Moreover, the generation of reactive oxygen species after apoptosis induction was inhibited, which means the inhibition occurred in an early step of the apoptotic process. Inhibition of apoptosis by the SP2 protein would lead to the minimization of cell death during commercial mammalian cell culture.