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PtP38 May Increase the Immune Ability of Portunus trituberculatus Stimulated by LPS Imitating a Gram-Negative Bacterial Infection
The P38 mitogen-activated protein kinase (MAPK) signal transduction pathway is widespread in organisms and plays important roles in immune activities. The infection mechanism of environmental gram-negative bacteria on crustaceans is an important scientific problem. In this study, the cDNA full-lengt...
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creator | Lu, Cheng-Peng Wei, Chao-Guang Zhu, Jun-Quan Tang, Dao-Jun Wang, Chun-Lin Hou, Cong-Cong |
description | The P38 mitogen-activated protein kinase (MAPK) signal transduction pathway is widespread in organisms and plays important roles in immune activities. The infection mechanism of environmental gram-negative bacteria on crustaceans is an important scientific problem. In this study, the cDNA full-length sequence of
Portunus trituberculatus
P38 (PtP38) was cloned and its structure was analyzed by bioinformatics methods. To study the function of the PtP38 gene after a Gram-negative bacterial infection, we injected
P. trituberculatus
with LPS to activate the immune response instead of directly infecting with Gram-negative bacteria. With LPS stimulation, the expression of the PtP38 gene in different tissues increased significantly. At the same time, the expression of immune-related genes (ALF and crustin) in the hepatopancreas, activities of antioxidant enzymes [superoxide dismutase (SOD), catalase (CAT), and inducible nitric oxide synthase (iNOS) enzymes], and expression of apoptosis-related genes (caspase2 and caspase3) were increased significantly. To further conform the function of PtP38 in the immune response, we injected
P. trituberculatus
with P38 inhibitor and subsequently injected with LPS. The results showed that the expression of immune-related genes was inhibited, the activity of antioxidant enzymes was decreased, and the expression of apoptosis-related genes were inhibited. Thus, we speculated that PtP38 may increase the immune ability by improving the expression of antimicrobial peptides, increasing the activity of oxidative stress-related enzymes, and promoting cell apoptosis in infected
P. trituberculatus
. This study also laid the foundation for further study of the P38 MAPK signaling pathway and immune mechanism of
P. trituberculatus
. |
doi_str_mv | 10.3389/fmars.2021.658733 |
format | article |
fullrecord | <record><control><sourceid>proquest_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_3984e22db0444e7db8772b6f7a160232</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_3984e22db0444e7db8772b6f7a160232</doaj_id><sourcerecordid>2521261779</sourcerecordid><originalsourceid>FETCH-LOGICAL-c334t-e3427b3c3feb277d697a74b5cf4c9cf02ca9938cd67c796ab00ff860ffd32ec3</originalsourceid><addsrcrecordid>eNpNUcFu1DAQjRBIVKUfwM0S5yyO7djxsVRQVlpgpfZujZ3x4lUSF9tB2iN_Xm8XIS4z80Yz743mNc37jm44H_RHP0PKG0ZZt5H9oDh_1VwxpmWrlOhf_1e_bW5yPlJKOy5oL_RV82df9nwg3-BEtotLCBlJ-YlkO8_rguTWhimUE4me7GMq67JmUlIoq8Xk1glKxQ8lzOcSR2JPZLd_qMuhQAnLgQC5TzC33_FQ8W8kn8AVTAGmqubRlRCXd80bD1PGm7_5unn88vnx7mu7-3G_vbvdtY5zUVrkginLHfdomVKj1AqUsL3zwmnnKXOgNR_cKJVTWoKl1PtB1jByho5fN9sL7RjhaJ5SqD87mQjBvDRiOhhIJbgJDdeDQMZGS4UQqEY7KMWs9Ao6SRlnlevDhespxV8r5mKOcU1Lvd6wnnVMdkrpOtVdplyKOSf0_1Q7as6-mRffzNk3c_GNPwPc9I0B</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2521261779</pqid></control><display><type>article</type><title>PtP38 May Increase the Immune Ability of Portunus trituberculatus Stimulated by LPS Imitating a Gram-Negative Bacterial Infection</title><source>Publicly Available Content Database</source><creator>Lu, Cheng-Peng ; Wei, Chao-Guang ; Zhu, Jun-Quan ; Tang, Dao-Jun ; Wang, Chun-Lin ; Hou, Cong-Cong</creator><creatorcontrib>Lu, Cheng-Peng ; Wei, Chao-Guang ; Zhu, Jun-Quan ; Tang, Dao-Jun ; Wang, Chun-Lin ; Hou, Cong-Cong</creatorcontrib><description>The P38 mitogen-activated protein kinase (MAPK) signal transduction pathway is widespread in organisms and plays important roles in immune activities. The infection mechanism of environmental gram-negative bacteria on crustaceans is an important scientific problem. In this study, the cDNA full-length sequence of
Portunus trituberculatus
P38 (PtP38) was cloned and its structure was analyzed by bioinformatics methods. To study the function of the PtP38 gene after a Gram-negative bacterial infection, we injected
P. trituberculatus
with LPS to activate the immune response instead of directly infecting with Gram-negative bacteria. With LPS stimulation, the expression of the PtP38 gene in different tissues increased significantly. At the same time, the expression of immune-related genes (ALF and crustin) in the hepatopancreas, activities of antioxidant enzymes [superoxide dismutase (SOD), catalase (CAT), and inducible nitric oxide synthase (iNOS) enzymes], and expression of apoptosis-related genes (caspase2 and caspase3) were increased significantly. To further conform the function of PtP38 in the immune response, we injected
P. trituberculatus
with P38 inhibitor and subsequently injected with LPS. The results showed that the expression of immune-related genes was inhibited, the activity of antioxidant enzymes was decreased, and the expression of apoptosis-related genes were inhibited. Thus, we speculated that PtP38 may increase the immune ability by improving the expression of antimicrobial peptides, increasing the activity of oxidative stress-related enzymes, and promoting cell apoptosis in infected
P. trituberculatus
. This study also laid the foundation for further study of the P38 MAPK signaling pathway and immune mechanism of
P. trituberculatus
.</description><identifier>ISSN: 2296-7745</identifier><identifier>EISSN: 2296-7745</identifier><identifier>DOI: 10.3389/fmars.2021.658733</identifier><language>eng</language><publisher>Lausanne: Frontiers Research Foundation</publisher><subject>Antimicrobial peptides ; Antioxidants ; Apoptosis ; Aquatic crustaceans ; Bacteria ; Bacterial diseases ; Bacterial infections ; Bioinformatics ; Catalase ; Cell cycle ; Cloning ; Crustaceans ; Cytokines ; Defence mechanisms ; E coli ; Enzymes ; Gene expression ; Gram-negative bacteria ; Hepatopancreas ; Immune response ; Immunity ; Insects ; Invertebrates ; Kinases ; Laboratory animals ; Lipopolysaccharides ; LPS ; MAP kinase ; MAPK ; Nitric oxide ; Nitric-oxide synthase ; Oxidative stress ; P38 ; Peptides ; Phosphorylation ; Portunus trituberculatus ; Protein kinase ; Proteins ; Signal transduction ; Superoxide dismutase ; Websites</subject><ispartof>Frontiers in Marine Science, 2021-05, Vol.8</ispartof><rights>2021. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c334t-e3427b3c3feb277d697a74b5cf4c9cf02ca9938cd67c796ab00ff860ffd32ec3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2521261779/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2521261779?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,25753,27924,27925,37012,44590,75126</link.rule.ids></links><search><creatorcontrib>Lu, Cheng-Peng</creatorcontrib><creatorcontrib>Wei, Chao-Guang</creatorcontrib><creatorcontrib>Zhu, Jun-Quan</creatorcontrib><creatorcontrib>Tang, Dao-Jun</creatorcontrib><creatorcontrib>Wang, Chun-Lin</creatorcontrib><creatorcontrib>Hou, Cong-Cong</creatorcontrib><title>PtP38 May Increase the Immune Ability of Portunus trituberculatus Stimulated by LPS Imitating a Gram-Negative Bacterial Infection</title><title>Frontiers in Marine Science</title><description>The P38 mitogen-activated protein kinase (MAPK) signal transduction pathway is widespread in organisms and plays important roles in immune activities. The infection mechanism of environmental gram-negative bacteria on crustaceans is an important scientific problem. In this study, the cDNA full-length sequence of
Portunus trituberculatus
P38 (PtP38) was cloned and its structure was analyzed by bioinformatics methods. To study the function of the PtP38 gene after a Gram-negative bacterial infection, we injected
P. trituberculatus
with LPS to activate the immune response instead of directly infecting with Gram-negative bacteria. With LPS stimulation, the expression of the PtP38 gene in different tissues increased significantly. At the same time, the expression of immune-related genes (ALF and crustin) in the hepatopancreas, activities of antioxidant enzymes [superoxide dismutase (SOD), catalase (CAT), and inducible nitric oxide synthase (iNOS) enzymes], and expression of apoptosis-related genes (caspase2 and caspase3) were increased significantly. To further conform the function of PtP38 in the immune response, we injected
P. trituberculatus
with P38 inhibitor and subsequently injected with LPS. The results showed that the expression of immune-related genes was inhibited, the activity of antioxidant enzymes was decreased, and the expression of apoptosis-related genes were inhibited. Thus, we speculated that PtP38 may increase the immune ability by improving the expression of antimicrobial peptides, increasing the activity of oxidative stress-related enzymes, and promoting cell apoptosis in infected
P. trituberculatus
. This study also laid the foundation for further study of the P38 MAPK signaling pathway and immune mechanism of
P. trituberculatus
.</description><subject>Antimicrobial peptides</subject><subject>Antioxidants</subject><subject>Apoptosis</subject><subject>Aquatic crustaceans</subject><subject>Bacteria</subject><subject>Bacterial diseases</subject><subject>Bacterial infections</subject><subject>Bioinformatics</subject><subject>Catalase</subject><subject>Cell cycle</subject><subject>Cloning</subject><subject>Crustaceans</subject><subject>Cytokines</subject><subject>Defence mechanisms</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Gene expression</subject><subject>Gram-negative bacteria</subject><subject>Hepatopancreas</subject><subject>Immune response</subject><subject>Immunity</subject><subject>Insects</subject><subject>Invertebrates</subject><subject>Kinases</subject><subject>Laboratory animals</subject><subject>Lipopolysaccharides</subject><subject>LPS</subject><subject>MAP kinase</subject><subject>MAPK</subject><subject>Nitric oxide</subject><subject>Nitric-oxide synthase</subject><subject>Oxidative stress</subject><subject>P38</subject><subject>Peptides</subject><subject>Phosphorylation</subject><subject>Portunus trituberculatus</subject><subject>Protein kinase</subject><subject>Proteins</subject><subject>Signal transduction</subject><subject>Superoxide dismutase</subject><subject>Websites</subject><issn>2296-7745</issn><issn>2296-7745</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpNUcFu1DAQjRBIVKUfwM0S5yyO7djxsVRQVlpgpfZujZ3x4lUSF9tB2iN_Xm8XIS4z80Yz743mNc37jm44H_RHP0PKG0ZZt5H9oDh_1VwxpmWrlOhf_1e_bW5yPlJKOy5oL_RV82df9nwg3-BEtotLCBlJ-YlkO8_rguTWhimUE4me7GMq67JmUlIoq8Xk1glKxQ8lzOcSR2JPZLd_qMuhQAnLgQC5TzC33_FQ8W8kn8AVTAGmqubRlRCXd80bD1PGm7_5unn88vnx7mu7-3G_vbvdtY5zUVrkginLHfdomVKj1AqUsL3zwmnnKXOgNR_cKJVTWoKl1PtB1jByho5fN9sL7RjhaJ5SqD87mQjBvDRiOhhIJbgJDdeDQMZGS4UQqEY7KMWs9Ao6SRlnlevDhespxV8r5mKOcU1Lvd6wnnVMdkrpOtVdplyKOSf0_1Q7as6-mRffzNk3c_GNPwPc9I0B</recordid><startdate>20210503</startdate><enddate>20210503</enddate><creator>Lu, Cheng-Peng</creator><creator>Wei, Chao-Guang</creator><creator>Zhu, Jun-Quan</creator><creator>Tang, Dao-Jun</creator><creator>Wang, Chun-Lin</creator><creator>Hou, Cong-Cong</creator><general>Frontiers Research Foundation</general><general>Frontiers Media S.A</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7TN</scope><scope>7XB</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M2P</scope><scope>M7P</scope><scope>PCBAR</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>DOA</scope></search><sort><creationdate>20210503</creationdate><title>PtP38 May Increase the Immune Ability of Portunus trituberculatus Stimulated by LPS Imitating a Gram-Negative Bacterial Infection</title><author>Lu, Cheng-Peng ; Wei, Chao-Guang ; Zhu, Jun-Quan ; Tang, Dao-Jun ; Wang, Chun-Lin ; Hou, Cong-Cong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c334t-e3427b3c3feb277d697a74b5cf4c9cf02ca9938cd67c796ab00ff860ffd32ec3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Antimicrobial peptides</topic><topic>Antioxidants</topic><topic>Apoptosis</topic><topic>Aquatic crustaceans</topic><topic>Bacteria</topic><topic>Bacterial diseases</topic><topic>Bacterial infections</topic><topic>Bioinformatics</topic><topic>Catalase</topic><topic>Cell cycle</topic><topic>Cloning</topic><topic>Crustaceans</topic><topic>Cytokines</topic><topic>Defence mechanisms</topic><topic>E coli</topic><topic>Enzymes</topic><topic>Gene expression</topic><topic>Gram-negative bacteria</topic><topic>Hepatopancreas</topic><topic>Immune response</topic><topic>Immunity</topic><topic>Insects</topic><topic>Invertebrates</topic><topic>Kinases</topic><topic>Laboratory animals</topic><topic>Lipopolysaccharides</topic><topic>LPS</topic><topic>MAP kinase</topic><topic>MAPK</topic><topic>Nitric oxide</topic><topic>Nitric-oxide synthase</topic><topic>Oxidative stress</topic><topic>P38</topic><topic>Peptides</topic><topic>Phosphorylation</topic><topic>Portunus trituberculatus</topic><topic>Protein kinase</topic><topic>Proteins</topic><topic>Signal transduction</topic><topic>Superoxide dismutase</topic><topic>Websites</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lu, Cheng-Peng</creatorcontrib><creatorcontrib>Wei, Chao-Guang</creatorcontrib><creatorcontrib>Zhu, Jun-Quan</creatorcontrib><creatorcontrib>Tang, Dao-Jun</creatorcontrib><creatorcontrib>Wang, Chun-Lin</creatorcontrib><creatorcontrib>Hou, Cong-Cong</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Oceanic Abstracts</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>ProQuest Science Journals</collection><collection>ProQuest Biological Science Journals</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Frontiers in Marine Science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lu, Cheng-Peng</au><au>Wei, Chao-Guang</au><au>Zhu, Jun-Quan</au><au>Tang, Dao-Jun</au><au>Wang, Chun-Lin</au><au>Hou, Cong-Cong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PtP38 May Increase the Immune Ability of Portunus trituberculatus Stimulated by LPS Imitating a Gram-Negative Bacterial Infection</atitle><jtitle>Frontiers in Marine Science</jtitle><date>2021-05-03</date><risdate>2021</risdate><volume>8</volume><issn>2296-7745</issn><eissn>2296-7745</eissn><abstract>The P38 mitogen-activated protein kinase (MAPK) signal transduction pathway is widespread in organisms and plays important roles in immune activities. The infection mechanism of environmental gram-negative bacteria on crustaceans is an important scientific problem. In this study, the cDNA full-length sequence of
Portunus trituberculatus
P38 (PtP38) was cloned and its structure was analyzed by bioinformatics methods. To study the function of the PtP38 gene after a Gram-negative bacterial infection, we injected
P. trituberculatus
with LPS to activate the immune response instead of directly infecting with Gram-negative bacteria. With LPS stimulation, the expression of the PtP38 gene in different tissues increased significantly. At the same time, the expression of immune-related genes (ALF and crustin) in the hepatopancreas, activities of antioxidant enzymes [superoxide dismutase (SOD), catalase (CAT), and inducible nitric oxide synthase (iNOS) enzymes], and expression of apoptosis-related genes (caspase2 and caspase3) were increased significantly. To further conform the function of PtP38 in the immune response, we injected
P. trituberculatus
with P38 inhibitor and subsequently injected with LPS. The results showed that the expression of immune-related genes was inhibited, the activity of antioxidant enzymes was decreased, and the expression of apoptosis-related genes were inhibited. Thus, we speculated that PtP38 may increase the immune ability by improving the expression of antimicrobial peptides, increasing the activity of oxidative stress-related enzymes, and promoting cell apoptosis in infected
P. trituberculatus
. This study also laid the foundation for further study of the P38 MAPK signaling pathway and immune mechanism of
P. trituberculatus
.</abstract><cop>Lausanne</cop><pub>Frontiers Research Foundation</pub><doi>10.3389/fmars.2021.658733</doi><oa>free_for_read</oa></addata></record> |
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subjects | Antimicrobial peptides Antioxidants Apoptosis Aquatic crustaceans Bacteria Bacterial diseases Bacterial infections Bioinformatics Catalase Cell cycle Cloning Crustaceans Cytokines Defence mechanisms E coli Enzymes Gene expression Gram-negative bacteria Hepatopancreas Immune response Immunity Insects Invertebrates Kinases Laboratory animals Lipopolysaccharides LPS MAP kinase MAPK Nitric oxide Nitric-oxide synthase Oxidative stress P38 Peptides Phosphorylation Portunus trituberculatus Protein kinase Proteins Signal transduction Superoxide dismutase Websites |
title | PtP38 May Increase the Immune Ability of Portunus trituberculatus Stimulated by LPS Imitating a Gram-Negative Bacterial Infection |
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