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Inhibition of Apoptosis by a Bombyx mori Gene
Author(s) -
Kim Eun Jeong,
Rhee Won Jong,
Park Tai Hyun
Publication year - 2008
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/bp034130y
Subject(s) - bombyx mori , hemolymph , apoptosis , transfection , intracellular , microbiology and biotechnology , gene , in vitro , biology , caspase , caspase 3 , homology (biology) , biochemistry , chemistry , programmed cell death
An apoptosis‐inhibiting component of silkworm hemolymph, isolated and characterized in our previous study, showed 95% N‐terminal amino acid sequence homology with one of the 30K proteins, a group of structurally related proteins. The 30K protein was expressed in mammalian HEK293 cells and CHOK1 cells by transfection with 30Kc6 . The expression of 30Kc6 inhibited apoptosis comparably to that of whole silkworm hemolymph, indicating that both intracellular expression and external supplementation inhibited apoptosis. The expression of 30Kc6 resulted in lower intracellular activity for caspase 3. However, the results of in vitro assay of caspase 3 show that the 30Kc6 protein does not inhibit caspase 3 activity. This indicates that the 30Kc6 protein inhibits the apoptosis by working in a further upstream event than caspase 3activation.