title: Extrusion improved the anti-inflammatory effect of amaranth (Amaranthus hypochondriacus) hydrolysates in LPS-induced human THP-1 macrophage-like and mouse RAW 264.7 macrophages by preventing activation of NF-κB signaling.
abstract: METHODS
  The objective was to compare the anti-inflammatory potential of unprocessed and extruded amaranth pepsin/pancreatin hydrolysates in LPS-induced human THP-1 macrophages-like and mouse RAW 264.7 macrophages focusing on their anti-inflammatory mechanism of action related to NF-κB signaling pathway.
  
  
  RESULTS
  Amaranth hydrolysates were characterized by MS-MS and tested for anti-inflammatory effects on human and mouse macrophages. Peptides found in extruded amaranth hydrolysates displayed antioxidant capacity, angiotensin converting enzyme-inhibitor activity, and dipeptidyl peptidase-IV inhibitor activity. Gly-Pro-Arg peptide was present and reported as antithrombotic. Extruded amaranth hydrolysates (1 mg/mL) significantly reduced tumor necrosis factor alpha secretion in THP-1 and RAW 264.7 cells by 36.5 and 33.5%, respectively; with concomitant reduction in PGE2 (15.4 and 31.4%), and COX-2 (38.1 and 67.6%), respectively. Phosphorylation of IKK-α was significantly reduced by 52.5 and 88.2% leading to reduced phosphorylation of IκB-α (86.1 and 66.2%), respectively; resulting in a reduction in the expression of p65 NF-κB subunits in the nucleus by 64.2% for THP-1 and 70.7% for RAW 264.7 cells.
  
  
  CONCLUSIONS
  Amaranth hydrolysates inhibited LPS-induced inflammation in human and mouse macrophages by preventing activation of NF-κB signaling. Extrusion improved anti-inflammatory effect of amaranth hydrolysates in both cells, which might be attributed to the production of bioactive peptides during processing.
authors.affiliation: Programa Regional del Noroeste para el Doctorado en Biotecnología, FCQB-UAS, Ciudad Universitaria, Culiacán, Sinaloa, México; Food Science and Human Nutrition, University of Illinois at Urbana-Champaign, IL, USA.
authors.forename: Alvaro
authors.initials: A
authors.lastname: Montoya-Rodríguez
authors.forename: Elvira González
authors.initials: EG
authors.lastname: de Mejía
authors.forename: Vermont P
authors.initials: VP
authors.lastname: Dia
authors.forename: Cuauhtémoc
authors.initials: C
authors.lastname: Reyes-Moreno
authors.forename: Jorge
authors.initials: J
authors.lastname: Milán-Carrillo
mesh_terms: D027721:Amaranthus / Q000737:chemistry*; D000818:Animals; D000893:Anti-Inflammatory Agents / Q000494:pharmacology; D000975:Antioxidants / Q000494:pharmacology; D045744:Cell Line, Tumor; D051546:Cyclooxygenase 2 / Q000235:genetics / Q000378:metabolism; D006801:Humans; D051550:I-kappa B Kinase / Q000235:genetics / Q000378:metabolism; D020672:I-kappa B Proteins / Q000235:genetics / Q000378:metabolism; D007249:Inflammation / Q000188:drug therapy; D008070:Lipopolysaccharides; D008264:Macrophages / Q000166:cytology / Q000187:drug effects*; D051379:Mice; D000072000:NF-KappaB Inhibitor alpha; D016328:NF-kappa B / Q000235:genetics* / Q000378:metabolism; D009842:Oligopeptides / Q000494:pharmacology; D010766:Phosphorylation; D010936:Plant Extracts / Q000494:pharmacology*; D015398:Signal Transduction; D053719:Tandem Mass Spectrometry; D051996:Transcription Factor RelA / Q000235:genetics / Q000378:metabolism
chemical_list: D000893:Anti-Inflammatory Agents; D000975:Antioxidants; D020672:I-kappa B Proteins; D008070:Lipopolysaccharides; D016328:NF-kappa B; C000606204:NFKBIA protein, human; C000606205:Nfkbia protein, mouse; D009842:Oligopeptides; D010936:Plant Extracts; D051996:Transcription Factor RelA; D000072000:NF-KappaB Inhibitor alpha; C035024:glycyl-prolyl-arginine; C077623:Ptgs2 protein, mouse; D051546:Cyclooxygenase 2; C496540:PTGS2 protein, human; D051550:I-kappa B Kinase
keywords: Amaranthus hypochondriacus; Extrusion; Human THP-1 macrophages-like; Inflammation; Peptides