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      Natural product derived phytochemicals in managing acute lung injury by multiple mechanisms

      review-article
      a , 1 , c , 1 , a , 1 , a , a , b , a , b , * , a , b , *
      Pharmacological Research
      Elsevier Ltd.
      Luteolin (PubChem CID: 5280445), Baicalin (PubChem CID: 64982), Tanshinone IIA (PubChem CID: 164676), Quercetin (PubChem CID: 5280343), Kaempferol (PubChem CID: 5280863), Hydroxysafflor yellow A (PubChem CID: 6443665), Curcumin (PubChem CID: 969516), Resveratrol (PubChem CID: 445154), Emodin (PubChem CID: 3220), Osthole (PubChem CID: 10228), ALI, acute lung injury, ARDS, acute respiratory distress syndrome, TNF-α, tumor necrosis factor alpha, IL-1β, Interleukin-1 beta, IL-6, Interleukin-6, TGF-β, transforming growth factor-beta, MCP1, monocyte chemoattractant protein 1, SOD, superoxide dismutase, GSH, glutathione, MDA, malondialdehyde, ROS, reactive oxygen species, MPO, myeloperoxidase, ICAM-1, intercellular cell adhesion molecule-1, HMGB1, high mobility group protein, iNOS, inducible nitric oxide synthase, COX-2, cyclooxygenase-2, NF-κB, nuclear factor kappa-B, MAPK, mitogen-activated protein kinase, AMPK, AMP-activated protein kinase, TLRs, toll like receptor, PPAR-γ, peroxisome proliferator-activated receptor gamma, LPS, lipopolysaccharide, NO, nitric oxide, HO-1, heme oxygenase-1, NLRP3, nucleotide-binding oligomerization domain, leucine- rich repeat and pyrin domain-containing 3 , QP-1, aquaporin-1, HIF-1α, hypoxia-inducible factor-1α, ABCA1, ATP‑binding cassette transporter A1, LXRα, liver X receptorα, MMP9, matrix metallopeptidase 9, α7nAchR, α7-nicotinic acetylcholine receptor, MIF, macrophage migration inhibitory factor, ACE-2, angiotensin-converting enzyme 2, Ang‑(1‑7), angiotensin‑(1‑7), MIP-2, macrophage inhibitory protein 2, BMDMs, bone marrow-derived macrophages, IAV, Influenza A virus, Natural compounds, Acute lung injury, Acute respiratory distress syndrome, Chemical structures, Mechanisms

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          Highlights

          • This paper summarized 159 natural compounds against ALI.

          • The paper summed up the protective effects of all products on ALI in vivo and vitro.

          • This paper clarified the underlying mechanism of natural compounds against ALI.

          Abstract

          Acute lung injury (ALI) and its more severe form, acute respiratory distress syndrome (ARDS) as common life-threatening lung diseases with high mortality rates are mostly associated with acute and severe inflammation in lungs. With increasing in-depth studies of ALI/ARDS, significant breakthroughs have been made, however, there are still no effective pharmacological therapies for treatment of ALI/ARDS. Especially, the novel coronavirus pneumonia (COVID-19) is ravaging the globe, and causes severe respiratory distress syndrome. Therefore, developing new drugs for therapy of ALI/ARDS is in great demand, which might also be helpful for treatment of COVID-19. Natural compounds have always inspired drug development, and numerous natural products have shown potential therapeutic effects on ALI/ARDS. Therefore, this review focuses on the potential therapeutic effects of natural compounds on ALI and the underlying mechanisms. Overall, the review discusses 159 compounds and summarizes more than 400 references to present the protective effects of natural compounds against ALI and the underlying mechanism.

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          ROS Signaling in the Pathogenesis of Acute Lung Injury (ALI) and Acute Respiratory Distress Syndrome (ARDS)

          The generation of reactive oxygen species (ROS) plays an important role for the maintenance of cellular processes and functions in the body. However, the excessive generation of oxygen radicals under pathological conditions such as acute lung injury (ALI) and its most severe form acute respiratory distress syndrome (ARDS) leads to increased endothelial permeability. Within this hallmark of ALI and ARDS, vascular microvessels lose their junctional integrity and show increased myosin contractions that promote the migration of polymorphonuclear leukocytes (PMNs) and the transition of solutes and fluids in the alveolar lumen. These processes all have a redox component, and this chapter focuses on the role played by ROS during the development of ALI/ARDS. We discuss the origins of ROS within the cell, cellular defense mechanisms against oxidative damage, the role of ROS in the development of endothelial permeability, and potential therapies targeted at oxidative stress.
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            Nrf2–ARE signaling in cellular protection: Mechanism of action and the regulatory mechanisms

            Oxidative stress is the increase in cellular oxidant concentration in comparison to antioxidant titer. Toxic insults and many other diseased conditions are mediated through the formation of such condition. Once the redox equilibrium is disrupted, the cellular antioxidant system functions to bring back the cell to redox homeostasis state. The field players of the cytoprotective machinery are the xenobiotic-metabolizing enzymes that are transcriptionally controlled by upstream regulatory pathways like the Nrf2-ARE pathway and AhR-XRE pathway. The importance of Nrf2 lies in the fact that it is activated by a variety of compounds and has a wide range of inducers including metals, organic toxicants and so forth. The present review article aims to discuss the role of Nrf2 in cellular protection and also intends to illuminate the regulatory mechanisms that control Nrf2 itself. This can add to our knowledge of how the cell reacts and survives against such stressed conditions.
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              Is Open Access

              Role of Nrf2 and Its Activators in Respiratory Diseases

              Transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2) is a major regulator of antioxidant response element- (ARE-) driven cytoprotective protein expression. The activation of Nrf2 signaling plays an essential role in preventing cells and tissues from injury induced by oxidative stress. Under the unstressed conditions, natural inhibitor of Nrf2, Kelch-like ECH-associated protein 1 (Keap1), traps Nrf2 in the cytoplasm and promotes the degradation of Nrf2 by the 26S proteasome. Nevertheless, stresses including highly oxidative microenvironments, impair the ability of Keap1 to target Nrf2 for ubiquitination and degradation, and induce newly synthesized Nrf2 to translocate to the nucleus to bind with ARE. Due to constant exposure to external environments, including diverse pollutants and other oxidants, the redox balance maintained by Nrf2 is fairly important to the airways. To date, researchers have discovered that Nrf2 deletion results in high susceptibility and severity of insults in various models of respiratory diseases, including bronchopulmonary dysplasia (BPD), respiratory infections, acute respiratory distress syndrome (ARDS), chronic obstructive pulmonary disease (COPD), asthma, idiopathic pulmonary fibrosis (IPF), and lung cancer. Conversely, Nrf2 activation confers protective effects on these lung disorders. In the present review, we summarize Nrf2 involvement in the pathogenesis of the above respiratory diseases that have been identified by experimental models and human studies and describe the protective effects of Nrf2 inducers on these diseases.
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                Author and article information

                Journal
                Pharmacol Res
                Pharmacol. Res
                Pharmacological Research
                Elsevier Ltd.
                1043-6618
                1096-1186
                29 September 2020
                29 September 2020
                : 105224
                Affiliations
                [a ]Institute of Chinese Materia Madica, Shanghai University of Traditional Chinese Medicine, Shanghai 201203, China
                [b ]Department of Pharmacy, Changzheng Hospital, Second Military Medical University, Shanghai 200003, China
                [c ]Department of Pharmacy, Shanghai Tenth People’s Hospital, Tongji University School of Medicine, Shanghai 200072, China
                Author notes
                [* ]Corresponding authors at: Institute of Chinese Materia Madica, Shanghai University of Traditional Chinese Medicine, Shanghai 201203, China.
                [1]

                These authors contributed equally to this work.

                Article
                S1043-6618(20)31532-2 105224
                10.1016/j.phrs.2020.105224
                7522693
                33007416
                4d8fa5f2-a267-4ea0-8697-bfc44631d6dc
                © 2020 Elsevier Ltd. All rights reserved.

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

                History
                : 24 July 2020
                : 15 September 2020
                : 22 September 2020
                Categories
                Review

                Pharmacology & Pharmaceutical medicine
                luteolin (pubchem cid: 5280445),baicalin (pubchem cid: 64982),tanshinone iia (pubchem cid: 164676),quercetin (pubchem cid: 5280343),kaempferol (pubchem cid: 5280863),hydroxysafflor yellow a (pubchem cid: 6443665),curcumin (pubchem cid: 969516),resveratrol (pubchem cid: 445154),emodin (pubchem cid: 3220),osthole (pubchem cid: 10228),ali, acute lung injury,ards, acute respiratory distress syndrome,tnf-α, tumor necrosis factor alpha,il-1β, interleukin-1 beta,il-6, interleukin-6,tgf-β, transforming growth factor-beta,mcp1, monocyte chemoattractant protein 1,sod, superoxide dismutase,gsh, glutathione,mda, malondialdehyde,ros, reactive oxygen species,mpo, myeloperoxidase,icam-1, intercellular cell adhesion molecule-1,hmgb1, high mobility group protein,inos, inducible nitric oxide synthase,cox-2, cyclooxygenase-2,nf-κb, nuclear factor kappa-b,mapk, mitogen-activated protein kinase,ampk, amp-activated protein kinase,tlrs, toll like receptor,ppar-γ, peroxisome proliferator-activated receptor gamma,lps, lipopolysaccharide,no, nitric oxide,ho-1, heme oxygenase-1,nlrp3, nucleotide-binding oligomerization domain, leucine- rich repeat and pyrin domain-containing 3,qp-1, aquaporin-1,hif-1α, hypoxia-inducible factor-1α,abca1, atp‑binding cassette transporter a1,lxrα, liver x receptorα,mmp9, matrix metallopeptidase 9,α7nachr, α7-nicotinic acetylcholine receptor,mif, macrophage migration inhibitory factor,ace-2, angiotensin-converting enzyme 2,ang‑(1‑7), angiotensin‑(1‑7),mip-2, macrophage inhibitory protein 2,bmdms, bone marrow-derived macrophages,iav, influenza a virus,natural compounds,acute lung injury,acute respiratory distress syndrome,chemical structures,mechanisms
                Pharmacology & Pharmaceutical medicine
                luteolin (pubchem cid: 5280445), baicalin (pubchem cid: 64982), tanshinone iia (pubchem cid: 164676), quercetin (pubchem cid: 5280343), kaempferol (pubchem cid: 5280863), hydroxysafflor yellow a (pubchem cid: 6443665), curcumin (pubchem cid: 969516), resveratrol (pubchem cid: 445154), emodin (pubchem cid: 3220), osthole (pubchem cid: 10228), ali, acute lung injury, ards, acute respiratory distress syndrome, tnf-α, tumor necrosis factor alpha, il-1β, interleukin-1 beta, il-6, interleukin-6, tgf-β, transforming growth factor-beta, mcp1, monocyte chemoattractant protein 1, sod, superoxide dismutase, gsh, glutathione, mda, malondialdehyde, ros, reactive oxygen species, mpo, myeloperoxidase, icam-1, intercellular cell adhesion molecule-1, hmgb1, high mobility group protein, inos, inducible nitric oxide synthase, cox-2, cyclooxygenase-2, nf-κb, nuclear factor kappa-b, mapk, mitogen-activated protein kinase, ampk, amp-activated protein kinase, tlrs, toll like receptor, ppar-γ, peroxisome proliferator-activated receptor gamma, lps, lipopolysaccharide, no, nitric oxide, ho-1, heme oxygenase-1, nlrp3, nucleotide-binding oligomerization domain, leucine- rich repeat and pyrin domain-containing 3, qp-1, aquaporin-1, hif-1α, hypoxia-inducible factor-1α, abca1, atp‑binding cassette transporter a1, lxrα, liver x receptorα, mmp9, matrix metallopeptidase 9, α7nachr, α7-nicotinic acetylcholine receptor, mif, macrophage migration inhibitory factor, ace-2, angiotensin-converting enzyme 2, ang‑(1‑7), angiotensin‑(1‑7), mip-2, macrophage inhibitory protein 2, bmdms, bone marrow-derived macrophages, iav, influenza a virus, natural compounds, acute lung injury, acute respiratory distress syndrome, chemical structures, mechanisms

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