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Jae Ho Park,Jin Boo Jeong,Jeong Rak Lee,Ben O,de Lumen2,Hyung Jin Jeong 한국자원식물학회 2009 한국자원식물학회지 Vol.22 No.3
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.
The Anticancer Properties of Lunasin Peptide from Aged Callus Induced by the Soybean Tissue Culture
Park, Jae-Ho,Jeong, Jin-Boo,De Lumen, Ben O.,Jeong, Hyung-Jin The Plant Resources Society of Korea 2007 한국자원식물학회지 Vol.20 No.6
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.
Lunasin is prevalent in barley and is bioavailable and bioactive in in vivo and in vitro studies.
Jeong, Hyung Jin,Jeong, Jin Boo,Hsieh, Chia Chien,Hernandez-Ledesma, Blanca,de Lumen, Ben O Lawrence Erlbaum Associates, Publishers [etc.] 2010 Nutrition and cancer Vol.62 No.8
<P>Lunasin, a unique 43-amino acid peptide found in a number of seeds, has been shown to be chemopreventive in mammalian cells and in a skin cancer mouse model. To elucidate the role of cereals in cancer prevention, we report here the prevalence, bioavailability, and bioactivity of lunasin from barley. Lunasin is present in all cultivars of barley analyzed. The liver and kidney of rats fed with lunasin-enriched barley (LEB) show the presence of lunasin in Western blot. Lunasin extracted from the kidney and liver inhibits the activities of HATs (histone acetyl transferases), yGCN5 by 20% and 18% at 100 nM, and PCAF activity by 25% and 24% at 100 nM, confirming that the peptide is intact and bioactive. Purified barley lunasin localizes in the nuclei of NIH 3T3 cells. Barley lunasin added to NIH 3T3 cells in the presence of the chemical carcinogen MCA activates the expression of tumor suppressors p21 and p15 by 45% and 47%, decreases cyclin D1 by 98%, and inhibits Rb hyperphosphorylation by 45% compared with the MCA treatment alone. We conclude that lunasin is prevalent in barley, bioavailable, and bioactive and that consumption of barley could play an important role of cancer prevention in barley-consuming populations.</P>
Identification and Bioavailability of a Chromatin-Binding Peptide(Lunasin) from Korean Soybean
Park, Jae Ho,Kim, Soon Young,Ben O. de Lumen,Lee, Kon Joo,Jeong, Hyung Jin 한국식물학회 2002 Journal of Plant Biology Vol.45 No.2
Lunasin is a novel peptide with great potential as a nontoxic chemopreventive drug. This compound might account for part of the anticancer effects reported from studies with soybean (Glycine max). We studied its isolation, purification and biological assay, and observed that both its band from soybean and one from synthetic lunasin were <5 kD in their molecular weights. Among all the crop varieties tested, only the soybean produced a lunasin band on our western blot. Levels of this peptide ranged from 0.045㎎ per gram of seed for the Hanbatkong cultivar to 0.156㎎ per gram seed for 'Poolunkong'. The effect on colony formation by lunasin from different soybean extracts was significantly higher than for either the positive control or the synthetic lunasin. When lunasin was present in those natural extracts, histone acetylation decreased 100% compared with cells that were treated with Na-butyrate.