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      Stress-Induced Mucus Secretion and Its Composition by a Combination of Proteomics and Metabolomics of the Jellyfish Aurelia coerulea

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          Abstract

          Background: Jellyfish respond quickly to external stress that stimulates mucus secretion as a defense. Neither the composition of secreted mucus nor the process of secretion are well understood. Methods: Aurelia coerulea jellyfish were stimulated by removing them from environmental seawater. Secreted mucus and tissue samples were then collected within 60 min, and analyzed by a combination of proteomics and metabolomics using liquid chromatography coupled with tandem mass spectrometry (LC-MS/MS) and ultra-performance liquid chromatography/quadrupole time-of-flight mass spectrometry (UPLC-QTOF-MS/MS), respectively. Results: Two phases of sample collection displayed a quick decrease in volume, followed by a gradual increase. A total of 2421 and 1208 proteins were identified in tissue homogenate and secreted mucus, respectively. Gene Ontology (GO) analysis showed that the mucus-enriched proteins are mainly located in extracellular or membrane-associated regions, while the tissue-enriched proteins are distributed throughout intracellular compartments. Tryptamine, among 16 different metabolites, increased with the largest-fold change value of 7.8 in mucus, which is consistent with its involvement in the Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway ‘tryptophan metabolism’. We identified 11 metalloproteinases, four serpins, three superoxide dismutases and three complements, and their presence was speculated to be related to self-protective defense. Conclusions: Our results provide a composition profile of proteins and metabolites in stress-induced mucus and tissue homogenate of A. coerulea. This provides insight for the ongoing endeavors to discover novel bioactive compounds. The large increase of tryptamine in mucus may indicate a strong stress response when jellyfish were taken out of seawater and the active self-protective components such as enzymes, serpins and complements potentially play a key role in innate immunity of jellyfish.

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          Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling

          Wang et al. review the dual role of superoxide dismutases in controlling reactive oxygen species (ROS) damage and regulating ROS signaling across model systems as well as their involvement in human diseases.
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            Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression.

            Superoxide dismutases are an ubiquitous family of enzymes that function to efficiently catalyze the dismutation of superoxide anions. Three unique and highly compartmentalized mammalian superoxide dismutases have been biochemically and molecularly characterized to date. SOD1, or CuZn-SOD (EC 1.15.1.1), was the first enzyme to be characterized and is a copper and zinc-containing homodimer that is found almost exclusively in intracellular cytoplasmic spaces. SOD2, or Mn-SOD (EC 1.15.1.1), exists as a tetramer and is initially synthesized containing a leader peptide, which targets this manganese-containing enzyme exclusively to the mitochondrial spaces. SOD3, or EC-SOD (EC 1.15.1.1), is the most recently characterized SOD, exists as a copper and zinc-containing tetramer, and is synthesized containing a signal peptide that directs this enzyme exclusively to extracellular spaces. What role(s) these SODs play in both normal and disease states is only slowly beginning to be understood. A molecular understanding of each of these genes has proven useful toward the deciphering of their biological roles. For example, a variety of single amino acid mutations in SOD1 have been linked to familial amyotrophic lateral sclerosis. Knocking out the SOD2 gene in mice results in a lethal cardiomyopathy. A single amino acid mutation in human SOD3 is associated with 10 to 30-fold increases in serum SOD3 levels. As more information is obtained, further insights will be gained.
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              Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation.

              The action of matrix metalloproteinases (MMPs) was originally believed to be restricted to degradation of the extracellular matrix; however, in recent years, it has become evident that these proteases can modify many nonmatrix substrates, such as cytokines and chemokines. The use of MMP-deficient animals has revealed that these proteases can indeed influence the progression of various inflammatory processes. This review aims to provide the reader with a concise overview of these novel MMP functions in relation to leukocyte migration.
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                Author and article information

                Journal
                Mar Drugs
                Mar Drugs
                marinedrugs
                Marine Drugs
                MDPI
                1660-3397
                18 September 2018
                September 2018
                : 16
                : 9
                : 341
                Affiliations
                [1 ]College of Traditional Chinese Medicine, Jilin Agricultural University, Changchun 130118, China; lww0325@ 123456hotmail.com (W.L.); lianghongyu0819@ 123456hotmail.com (H.L.)
                [2 ]Department of Marine Biotechnology, Faculty of Naval Medicine, Second Military Medical University, Shanghai 200433, China; maria940501@ 123456outlook.com (C.M.); zhanglulu2822@ 123456outlook.com (L.Z.)
                [3 ]Department of Ship Hygiene, Faculty of Navy Medicine, Second Military Medical University, Shanghai 200433, China; fengfengmo@ 123456hotmail.com
                [4 ]Clinical Medicine, Grade 2015, Second Military Medical University, Shanghai 200433, China; jiangdaxian@ 123456hotmail.com
                [5 ]School of Marine Sciences, Ningbo University, Ningbo 315211, China; 18317128586@ 123456163.com
                [6 ]Department of Traditional Chinese Medicine Identification, School of Pharmacy, Second Military Medical University, Shanghai 200433, China; xlyiverson@ 123456126.com
                [7 ]Department of Earth, Environment and Life Sciences (DISTAV), University of Genova, Viale Benedetto XV 5, I-16132 Genova, Italy; Gian.Luigi.Mariottini@ 123456unige.it
                Author notes
                [* ]Correspondence: zhjing0701@ 123456163.com (J.Z.); hormat830713@ 123456hotmail.com (L.X.); Tel.: +86-13353144693 (J.Z.); +86-15921431590 (L.X.)
                [†]

                These authors contributed equally to this work.

                Article
                marinedrugs-16-00341
                10.3390/md16090341
                6165293
                30231483
                314c3559-c1ce-4309-b9b3-a3c84b592a31
                © 2018 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 24 August 2018
                : 09 September 2018
                Categories
                Article

                Pharmacology & Pharmaceutical medicine
                jellyfish,aurelia coerulea,mucus,proteomics,metabolomics
                Pharmacology & Pharmaceutical medicine
                jellyfish, aurelia coerulea, mucus, proteomics, metabolomics

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