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      Nitric Oxide Synthesis Inhibition and Anti-Inflammatory Effect
of Polypeptide Isolated from Chicken Feather Meal
in Lipopolysaccharide-Stimulated RAW 264.7 Macrophages

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          SUMMARY

          Nitric oxide (NO) plays a key role in the pathogenesis of inflammation and has been implicated in endotoxin-induced tissue injury. Chicken feather meal is a rich source of amino acids that may serve as a peptide hydrolysate to inhibit NO activity. Anti-inflammatory hydrolysates of chicken feather meal were prepared and fractionated into five samples based on molecular mass. The smallest fraction (<0.65 kDa) exhibited the highest NO inhibitory activity without cytotoxicity towards macrophage RAW 264.7 cells. Further subfractions were sufficient to obtain amino acid sequences by Q-TOF LC-MS/MS ESI analysis. Of these, the SNPSVAGVR (885.97 Da) peptide and its corresponding pure synthetic peptide have inhibitory activity against NO production by RAW 264.7 cells (IC 50=(55.2±0.2) mM) without cytotoxicity. Reverse transcriptase polymerase chain reaction (RT-PCR) and quantitative real-time RT-PCR results revealed that the peptide of the obtained fraction reduced transcript expression levels of the pro-inflammatory cytokines iNOS, TNF-α, COX-2 and IL-6 in lipopolysaccharide-stimulated RAW 264.7 cells. These results suggest that the peptides derived from the chicken feather meal protein could potentially be used as a promising ingredient in functional foods or nutraceuticals against inflammatory diseases.

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          Most cited references36

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          The Role of Inflammatory and Anti-Inflammatory Cytokines in the Pathogenesis of Osteoarthritis

          Osteoarthritis (OA) is the most common chronic disease of human joints. The basis of pathologic changes involves all the tissues forming the joint; already, at an early stage, it has the nature of inflammation with varying degrees of severity. An analysis of the complex relationships indicates that the processes taking place inside the joint are not merely a set that (seemingly) only includes catabolic effects. Apart from them, anti-inflammatory anabolic processes also occur continually. These phenomena are driven by various mediators, of which the key role is attributed to the interactions within the cytokine network. The most important group controlling the disease seems to be inflammatory cytokines, including IL-1 β , TNF α , IL-6, IL-15, IL-17, and IL-18. The second group with antagonistic effect is formed by cytokines known as anti-inflammatory cytokines such as IL-4, IL-10, and IL-13. The role of inflammatory and anti-inflammatory cytokines in the pathogenesis of OA with respect to inter- and intracellular signaling pathways is still under investigation. This paper summarizes the current state of knowledge. The cytokine network in OA is put in the context of cells involved in this degenerative joint disease. The possibilities for further implementation of new therapeutic strategies in OA are also pointed.
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            Oxidative stress and redox regulation of lung inflammation in COPD.

            Reactive oxygen species, either directly or via the formation of lipid peroxidation products, may play a role in enhancing inflammation through the activation of stress kinases (c-Jun activated kinase, extracellular signal-regulated kinase, p38) and redox-sensitive transcription factors, such as nuclear factor (NF)-kappaB and activator protein-1. This results in increased expression of a battery of distinct pro-inflammatory mediators. Oxidative stress activates NF-kappaB-mediated transcription of pro-inflammatory mediators either through activation of its activating inhibitor of kappaB-alpha kinase or the enhanced recruitment and activation of transcriptional co-activators. Enhanced NF-kappaB-co-activator complex formation results in targeted increases in histone modifications, such as acetylation leading to inflammatory gene expression. Emerging evidence suggests the glutathione redox couple may entail dynamic regulation of protein function by reversible disulphide bond formation on kinases, phosphatases and transcription factors. Oxidative stress also inhibits histone deacetylase activity and in doing so further enhances inflammatory gene expression and may attenuate glucocorticoid sensitivity. The antioxidant/anti-inflammatory effects of thiol molecules (glutathione, N-acetyl-L-cysteine and N-acystelyn, erdosteine), dietary polyphenols (curcumin-diferuloylmethane, cathechins/quercetin and reserveratol), specific spin traps, such as alpha-phenyl-N-tert-butyl nitrone, a catalytic antioxidant (extracellular superoxide dismutase (SOD) mimetic, SOD mimetic M40419 and SOD, and catalase manganic salen compound, eukarion-8), porphyrins (AEOL 10150 and AEOL 10113) and theophylline have all been shown to play a role in either controlling NF-kappaB activation or affecting histone modifications with subsequent effects on inflammatory gene expression in lung epithelial cells. Thus, oxidative stress regulates both key signal transduction pathways and histone modifications involved in lung inflammation. Various approaches to enhance lung antioxidant capacity and clinical trials of antioxidant compounds in chronic obstructive pulmonary disease are also discussed.
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              Purification and identification of novel antioxidant peptides from enzymatic hydrolysates of sardinelle (Sardinella aurita) by-products proteins

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                Author and article information

                Journal
                Food Technol Biotechnol
                Food Technol. Biotechnol
                FTB
                Food Technology and Biotechnology
                University of Zagreb Faculty of Food Technology and Biotechnology
                1330-9862
                1334-2606
                June 2019
                June 2019
                : 57
                : 2
                : 200-212
                Affiliations
                [1 ]Technopreneurship and Innovation Management Program, Graduate School, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok 10330, Thailand
                [2 ]Program in Biotechnology, Faculty of Science, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok 10330, Thailand
                [3 ]Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University, 420/6 Ratchawithi Road, Ratchathewi, Bangkok 10400, Thailand
                [4 ]Department of Medicine, Faculty of Medicine, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok 10330, Thailand
                [5 ]Department of Marketing, Faculty of Commerce and Accountancy, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok 10330, Thailand
                [6 ]Research Unit in Bioconversion/Bioseparation for Value-Added Chemical Production, Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok 10330, Thailand
                Author notes
                [* ]Corresponding author: Phone: +6622188078, Fax: +6622188069, E-mail: Aphichart.K@ 123456chula.ac.th
                Author information
                https://orcid.org/0000-0002-8178-3419
                https://orcid.org/0000-0002-4649-7433
                https://orcid.org/0000-0002-1154-6485
                https://orcid.org/0000-0002-2628-0894
                https://orcid.org/0000-0003-1361-5859
                https://orcid.org/0000-0001-5315-8264
                https://orcid.org/0000-0002-6085-1144
                https://orcid.org/0000-0002-6598-013X
                Article
                FTB-57-200
                10.17113/ftb.57.02.19.5964
                6718961
                d830a3d2-e305-4c7f-8d0b-4dcacd35f27d
                Copyright @ 2019

                This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial (CC BY-NC) 4.0 License.

                History
                : 02 August 2018
                : 26 March 2019
                Categories
                Original Scientific Papers

                nitric oxide,anti-inflammatory activity,chicken feather meal,protein hydrolysate,polypeptide,macrophage raw 264.7

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