Biochemical and Biophysical Research Communications
Regular ArticleSilkworm Hemolymph Inhibits Baculovirus-Induced Insect Cell Apoptosis
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2023, International Journal of Biological MacromoleculesProtein-based direct reprogramming of fibroblasts to neuronal cells using 30Kc19 protein and transcription factor Ascl1
2020, International Journal of Biochemistry and Cell BiologyCitation Excerpt :30Kc19 protein is derived from hemolymph of silkworm, Bombyx mori, and it is a member of the 30K protein family (Kim et al., 2003). Previously, we have observed various effects of silkworm hemolymph (Ha et al., 1996; Ha and Park, 1997; Rhee et al., 1999; Rhee and Park, 2000; Choi et al., 2002; Rhee et al., 2002; Choi et al., 2005) and 30K protein (Kim and Park, 2003; Kim et al., 2004; Choi et al., 2006; Wang et al., 2011; Park et al., 2015) by gene expression or addition of recombinant proteins. Since then, cell-penetrating and enzyme-stabilizing effect of 30Kc19 protein have been demonstrated (Park et al., 2012a, b).
Enhanced single-cell viability using 30Kc6 for efficient expansion of human induced pluripotent stem cells
2019, Process BiochemistryCitation Excerpt :Similarly, we recently used the 30 Kc6 protein to increase single cell viability. The 30 Kc6 protein derived from Bombyx mori exhibits anti-apoptotic properties against insect cells [17–21] and mammalian cells [22–24]. The mechanism of apoptosis inhibition by 30 Kc6 was shown to be due to the prevention of Bax localization to mitochondria.
Enzyme delivery using protein-stabilizing and cell-penetrating 30Kc19α protein nanoparticles
2017, Process BiochemistryCitation Excerpt :It is a member of the 30K protein family originating from the hemolymph of the silkworm, Bombyx mori. We have previously described anti-apoptotic effects in various cells via 30K gene expression or addition of recombinant 30K protein produced from Escherichia coli [18–30]. The enzyme-stabilizing and cell-penetrating effects of 30Kc19 protein have also been demonstrated [14,31,32].
Anti-oxidative effects of silkworm storage protein 1 in HeLa cell
2017, Process BiochemistryLysine acetylation stabilizes SP2 protein in the silkworm Bombyx mori
2016, Journal of Insect PhysiologyCitation Excerpt :The hemolymph of B. mori contains many nutrient storage and immunity-related proteins, showing important functions in the growth and development of the silkworm (Li et al., 2012; Zhang et al., 2014a). Many experiments have shown that silkworm hemolymph can resist insect and mammalian cell apoptosis, demonstrating anti-apoptosis activity (Choi et al., 2002; Rhee et al., 2002; Rhee and Park, 2000), and apoptosis-inhibiting components from hemolymph have also been identified, such as storage protein (SP) and 30 K proteins (Kim et al., 2003, 2001; Rhee et al., 2007). SP2 is a member of the SP protein family that can inhibit apoptosis induced by many factors, such as staurosporine and BmNPV (Yu et al., 2013).
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