Lunasin and lunasin-like peptides inhibit inflammation through suppression of NF-kappaB pathway in the macrophage.
Inflammation is part of the host defense mechanism against harmful matters and injury; however, aberrant inflammation is associated to the development of chronic diseases such as cancer. Lunasin is a novel peptide that demonstrates potential anticancer activity against mammalian cancer cell lines and may play a role in inflammation. The objective of this study was to determine the mechanism of action by which lunasin and lunasin-like peptides exert their anti-inflammatory properties using RAW 264.7 macrophage cell line as an in vitro model. We purified three peptides (5, 8, and 14 kDa) from defatted soybean flour with a positive immunoreactivity towards lunasin mouse monoclonal antibody. Treatment with these peptides (10-50 microM) resulted in the inhibition of pro-inflammatory markers in lipopolysaccharide (LPS)-induced RAW 264.7 macrophages. The 5 kDa peptide inhibited most potently pro-inflammatory markers including interleukin-6 production (IC(50)=2 microM), interleukin-1beta production (IC(50)=13 microM), nuclear factor-kappa B (NF-kappaB) transactivation (IC(50)=21 microM), cyclooxygenase-2 expression (IC(50)=25 microM), nitric oxide production (IC(50)=28 microM), inducible nitric oxide synthase expression (IC(50)=37 microM), prostaglandin E(2) production (IC(50)=41 microM), p65 nuclear translocation (IC(50)=48 microM) and p50 nuclear translocation (IC(50)=77 microM). In conclusion, lunasin and lunasin-like peptides purified from defatted soybean flour inhibited inflammation in LPS-induced RAW 264.7 macrophage by suppressing NF-kappaB pathway.
de Mejia
Elvira Gonzalez
EG
Department of Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, 228 ERML, MC-051, 1201 W Gregory Dr, Urbana, IL 61801, United States. edemejia@illinois.edu
Dia
Vermont P
VP
D000818:Animals; D000893:Anti-Inflammatory Agents / Q000494:pharmacology*; D015153:Blotting, Western; D045744:Cell Line, Tumor; D051545:Cyclooxygenase 1 / Q000378:metabolism; D051546:Cyclooxygenase 2 / Q000378:metabolism; D015232:Dinoprostone / Q000378:metabolism; D007249:Inflammation / Q000139:chemically induced; D015850:Interleukin-6 / Q000378:metabolism; D008070:Lipopolysaccharides / Q000494:pharmacology; D008264:Macrophages / Q000187:drug effects* / Q000276:immunology*; D008565:Membrane Proteins / Q000378:metabolism; D051379:Mice; D016328:NF-kappa B / Q000378:metabolism*; D052247:Nitric Oxide Synthase Type II / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology*; D015398:Signal Transduction / Q000187:drug effects*; D030262:Soybean Proteins / Q000494:pharmacology*
D000893:Anti-Inflammatory Agents; C120514:GM2S-1 protein, soybean; D015850:Interleukin-6; D008070:Lipopolysaccharides; D008565:Membrane Proteins; D016328:NF-kappa B; D010455:Peptides; D030262:Soybean Proteins; D052247:Nitric Oxide Synthase Type II; C077623:Ptgs2 protein, mouse; D051545:Cyclooxygenase 1; D051546:Cyclooxygenase 2; C496512:Ptgs1 protein, mouse; D015232:Dinoprostone