• Korean Journal of Plant Resources
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• v.30 no.1
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• pp.1-7
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• 2017

In this study, we produced the recombinant lunasin peptide using E. coli and P. pastoris, and evaluated biological activity of the recombinant lunasin peptide. Lunasin peptide was produced from E. coli transfected with pPGEX-lunasin expression vector and P. pastoris GS115 transfected with pPIC-lunasin expression vector. These recombinant lunasin peptides were similar to the synthetic lunasin peptide in the identification by LC-ESI-MS. In addition, the recombinant lunasin peptide from E. coli and P. pastoris was bound in the chromatin, and inhibited histone acetylation and the activity of histone acetyltransferase. These findings suggest that the production of the lunasin peptide using E. coli and P. pastoris will be useful for industrial utilization of lunasin peptide.

• Korean Journal of Plant Resources
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• v.20 no.6
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• pp.518-523
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• 2007

Lunasin is small subunit peptide of coded from Gm2S-1 gene in soybean. It has been previously demonstrated that lunasin is a novel and promising cancer preventive peptide. Lunasin peptide is found only in the seed and not other tissues. And lunasin peptide starts to appear at 5 weeks after flowering and remains in the mature seed. We report here firstly lunasin peptide identified from soybean callus induced by the tissue culture and demonstrate its anticancer properties. The lunasin was identified and purified from soybean callus aged for 6 months. The callus lunasin($1{\mu}M$) inhibited the acetylation of histone H3 and H4 by 58.8% and 56.5%, respectively. And it fully inhibited foci formation compared to the values of the positive control(no lunasin) and negative control(no MCA). Purified lunasin was able to internalize into the cell and localized in the nucleus.

• Korean Journal of Plant Resources
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• v.22 no.3
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• pp.203-208
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• 2009

Lunasin is a unique 43-amino acid peptide which has shown a chemopreventive in mammalian cells and in a skin cancer mouse model. In search for new sources of lunasin and the role of cereals in cancer prevention, we report here the properties of lunasin purified from millet. Stability of millet lunasin was measured by in vitro digestibility assay using pepsin and pancreatin. Inhibition of HAT (histone acetyltransferase) and nuclear localization in mammalian cells were used to measure lunasin bioactivity as the cancer chemopreventive agent. Lunasin present in millet crude protein was stable to pepsin and pancreatin in in vitro digestion and inhibited the activities of HATs. When added exogenously, lunasin purified from millet internalized in the nuclei of mouse fibroblast cells. On the base of this result, we conclude that lunasin in millet is bioactive and consumption of millet may play an important role on cancer prevention in millet-consuming populations.

• Journal of Life Science
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• v.15 no.4 s.71
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• pp.528-535
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• 2005

The non-enzymatic anti-oxidants and lunasin peptide from the extracts of the pepper were examined in order to utilize the discovery in natural products as cancer chemopreventive agents. The DPPH (1,1-diphenyl-2-picryl-hydrazyl) free radical scavenging activity on the fruit parts of the pepper was higher than that of the seed, but the difference was low. The Inhibition activity of xanthine/ xanthine oxidase in extracts of the seed was higher than that of the fruit and that of the seed on 20 days after flowering was the highest at the growing period. These were identified as fatty acids and phenolic compounds such as 1-eicosanol, palmitic acid, linoleic acid, linolenic acid and benzonitrile. The contents of fatty acids and phenolic compounds increased according to the time passing at the growing period. Peroxidase (POD) activity of the fruit at middle stage was high than that of other growing stages and that of the seed was the highest at later growing period. Though superoxide dismutase (SOD) activities in fruit were hish by passage of Slowing stage, the activity in seed was low. Lunasin was searched from seeds of the peppers by coomassie blue staining and western blot among them and we just found lunasin peptide from extracted protein of the pepper by western blot. In addition, we observed the contents of lunasin after flowering and confirmed to appear the lunasin at 35 days after flowering. We confirmed that lunasin is complex protein of maturing seeds. 100nM lunasin peptide in pepper showed inhibition effect on colony formation in $2\~12$ cells.

• Proceedings of the Plant Resources Society of Korea Conference
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• 2003.04a
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• pp.146-147
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• 2003

• Proceedings of the Korean Society of Crop Science Conference
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• 2001.09a
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• pp.210-211
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• 2001

• Proceedings of the Plant Resources Society of Korea Conference
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• 2002.04a
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• pp.37-37
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• 2002

• Proceedings of the Korean Society of Crop Science Conference
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• 2004.04a
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• pp.120-121
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• 2004

• Journal of Life Science
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• v.21 no.5
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• pp.713-719
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• 2011

In this study, we evaluated whether Lunasin Enriched Soybean (LES) suppressed 1-chloro-2,4-dinitrochlorobenzene (DNCB) induced allergic contact dermatitis in vivo. In the group treated with DNCB alone, erythema and hemorrhage in the skin were observed, while the application of LES after DNCB treatment modulated erythema and hemorrhage similar to the untreated group. In histopathological analysis of the skin, DNCB-treated groups showed increased skin thickness compared to the untreated groups, while the treatment of LES dose-dependently modulated skin thickness. Also, hypertrophy and hyperkeratosis of the epidermis, intracellular edema and infiltration of inflammatory cells were observed in the group treated with DNCB alone, while treatment of LES inhibited these inflammatory changes. DNCB also induced a significant up-regulation of iNOS and COX-2 expression, as compared to the untreated groups. However, the treatment of LES significantly decreased the down-regulation of iNOS and COX-2 expression, as compared to DNCB-treated groups. Also, LES reduced the IgE level in DNCB-stimulated groups. And lunasin from LES translocated the nucleus of the cells in the skin of Sprague-Dawley rats. Taken together, it is thought that LES has the potential to be used as an alternative treatment for allergic contact dermatitis.

• Proceedings of the Korean Society of Food Science and Nutrition Conference
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• 2004.11a
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• pp.80-84
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• 2004