Cloning of Cytoplasmic Heat Shock Protein 90 (FcHSP90) from Fenneropenaeus chinensis and Its Expression Response to Heat Shock and Hypoxia
Heat shock protein 90 (HSP90) works as a multifunctional chaperone and is involved in the regulation of many essential cellular pathways. In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA...
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| Veröffentlicht in: | Cell stress & chaperones 2009-03, Vol.14 (2), p.161-172 |
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| creator | Li, Fuhua Luan, Wei Zhang, Chengsong Zhang, Jiquan Wang, Bing Xie, Yusu Li, Shihao Xiang, Jianhai |
| description | Heat shock protein 90 (HSP90) works as a multifunctional chaperone and is involved in the regulation of many essential cellular pathways. In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25°C to 35°C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocytes and gill, were induced at 2 h and depressed at 8 h during hypoxia stress. The assessment of FcHSP90 mRNA levels under heat shock and hypoxia stresses indicated that the transcription of FcHSP90 was very sensitive to heat shock and hypoxia, so we deduced that FcHSP90 might play very important roles for shrimp to cope with environmental stress. |
| doi_str_mv | 10.1007/s12192-008-0069-6 |
| format | Article |
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In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25°C to 35°C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocytes and gill, were induced at 2 h and depressed at 8 h during hypoxia stress. The assessment of FcHSP90 mRNA levels under heat shock and hypoxia stresses indicated that the transcription of FcHSP90 was very sensitive to heat shock and hypoxia, so we deduced that FcHSP90 might play very important roles for shrimp to cope with environmental stress.</description><identifier>ISSN: 1355-8145</identifier><identifier>EISSN: 1466-1268</identifier><identifier>DOI: 10.1007/s12192-008-0069-6</identifier><identifier>PMID: 18668349</identifier><language>eng</language><publisher>Dordrecht: Cell Stress Society International</publisher><subject>Amino Acid Sequence ; Amino acids ; Anaerobiosis ; Animals ; Base Sequence ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cancer Research ; Cell Biology ; Cloning, Molecular ; Complementary DNA ; Cytoplasm - metabolism ; DNA, Complementary - genetics ; Gene Expression Profiling ; Gene Expression Regulation ; Heat shock proteins ; Heat-Shock Response - genetics ; Hemocytes ; HSP90 Heat-Shock Proteins - chemistry ; HSP90 Heat-Shock Proteins - genetics ; HSP90 Heat-Shock Proteins - metabolism ; Hypoxia ; Immunology ; Messenger RNA ; Molecular Sequence Data ; Neurosciences ; Original Paper ; Oxygen - analysis ; Penaeidae - genetics ; Phylogeny ; Polymerase chain reaction ; Reverse transcriptase polymerase chain reaction ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Sea water ; Seawater ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; Shock heating</subject><ispartof>Cell stress & chaperones, 2009-03, Vol.14 (2), p.161-172</ispartof><rights>Copyright 2009 Cell Stress Society International</rights><rights>Cell Stress Society International 2008</rights><rights>Copyright Springer Science & Business Media Mar 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c555t-458664373855b8ab94c1a167b31b85da038b15553a4caf44ae16637887c61ae13</citedby><cites>FETCH-LOGICAL-c555t-458664373855b8ab94c1a167b31b85da038b15553a4caf44ae16637887c61ae13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/20456371$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/20456371$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,41464,42533,51294,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18668349$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Fuhua</creatorcontrib><creatorcontrib>Luan, Wei</creatorcontrib><creatorcontrib>Zhang, Chengsong</creatorcontrib><creatorcontrib>Zhang, Jiquan</creatorcontrib><creatorcontrib>Wang, Bing</creatorcontrib><creatorcontrib>Xie, Yusu</creatorcontrib><creatorcontrib>Li, Shihao</creatorcontrib><creatorcontrib>Xiang, Jianhai</creatorcontrib><title>Cloning of Cytoplasmic Heat Shock Protein 90 (FcHSP90) from Fenneropenaeus chinensis and Its Expression Response to Heat Shock and Hypoxia</title><title>Cell stress & chaperones</title><addtitle>Cell Stress and Chaperones</addtitle><addtitle>Cell Stress Chaperones</addtitle><description>Heat shock protein 90 (HSP90) works as a multifunctional chaperone and is involved in the regulation of many essential cellular pathways. In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25°C to 35°C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocytes and gill, were induced at 2 h and depressed at 8 h during hypoxia stress. The assessment of FcHSP90 mRNA levels under heat shock and hypoxia stresses indicated that the transcription of FcHSP90 was very sensitive to heat shock and hypoxia, so we deduced that FcHSP90 might play very important roles for shrimp to cope with environmental stress.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Anaerobiosis</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>Cytoplasm - metabolism</subject><subject>DNA, Complementary - genetics</subject><subject>Gene Expression Profiling</subject><subject>Gene Expression Regulation</subject><subject>Heat shock proteins</subject><subject>Heat-Shock Response - genetics</subject><subject>Hemocytes</subject><subject>HSP90 Heat-Shock Proteins - chemistry</subject><subject>HSP90 Heat-Shock Proteins - genetics</subject><subject>HSP90 Heat-Shock Proteins - metabolism</subject><subject>Hypoxia</subject><subject>Immunology</subject><subject>Messenger RNA</subject><subject>Molecular Sequence Data</subject><subject>Neurosciences</subject><subject>Original Paper</subject><subject>Oxygen - analysis</subject><subject>Penaeidae - genetics</subject><subject>Phylogeny</subject><subject>Polymerase chain reaction</subject><subject>Reverse transcriptase polymerase chain reaction</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Sea water</subject><subject>Seawater</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>Shock heating</subject><issn>1355-8145</issn><issn>1466-1268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kc1u1DAUhSMEoqXwACxAFgsEi4Ad_2aDhEYdplIlKgpry_E4Mx4SO_gmqPMKPDUeMmoLCxaWbd3vHN_rUxTPCX5HMJbvgVSkrkqMVV6iLsWD4pQwIUpSCfUwnynnpSKMnxRPAHY4a6Qkj4sTooRQlNWnxa9FF4MPGxRbtNiPcegM9N6ilTMjut5G-x1dpTg6H1CN0ZulXV1f1fgtalPs0dKF4FIcXDBuAmS3PrgAHpAJa3QxAjq_GZID8DGgLw6GGMChMd43P5Cr_RBvvHlaPGpNB-7ZcT8rvi3Pvy5W5eXnTxeLj5el5ZyPJeO5eUYlVZw3yjQ1s8QQIRtKGsXXBlPVkExSw6xpGTOOCEGlUtIKki_0rPgw-w5T07u1dWFMptND8r1Jex2N139Xgt_qTfypK1nJusbZ4PXRIMUfk4NR9x6s6zoTXJxAC1ETyYnK4Kt_wF2cUsjD6SoHmIP5A5EZsikCJNfedkKwPsSs55h1jlkfYtYia17eH-FOccw1A9UMQC6FjUt3L__P9cUs2sEY061phRnPH0job7cFvFQ</recordid><startdate>20090301</startdate><enddate>20090301</enddate><creator>Li, Fuhua</creator><creator>Luan, Wei</creator><creator>Zhang, Chengsong</creator><creator>Zhang, Jiquan</creator><creator>Wang, Bing</creator><creator>Xie, Yusu</creator><creator>Li, Shihao</creator><creator>Xiang, Jianhai</creator><general>Cell Stress Society International</general><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20090301</creationdate><title>Cloning of Cytoplasmic Heat Shock Protein 90 (FcHSP90) from Fenneropenaeus chinensis and Its Expression Response to Heat Shock and Hypoxia</title><author>Li, Fuhua ; Luan, Wei ; Zhang, Chengsong ; Zhang, Jiquan ; Wang, Bing ; Xie, Yusu ; Li, Shihao ; Xiang, Jianhai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c555t-458664373855b8ab94c1a167b31b85da038b15553a4caf44ae16637887c61ae13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Anaerobiosis</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cancer Research</topic><topic>Cell Biology</topic><topic>Cloning, Molecular</topic><topic>Complementary DNA</topic><topic>Cytoplasm - metabolism</topic><topic>DNA, Complementary - genetics</topic><topic>Gene Expression Profiling</topic><topic>Gene Expression Regulation</topic><topic>Heat shock proteins</topic><topic>Heat-Shock Response - genetics</topic><topic>Hemocytes</topic><topic>HSP90 Heat-Shock Proteins - chemistry</topic><topic>HSP90 Heat-Shock Proteins - genetics</topic><topic>HSP90 Heat-Shock Proteins - metabolism</topic><topic>Hypoxia</topic><topic>Immunology</topic><topic>Messenger RNA</topic><topic>Molecular Sequence Data</topic><topic>Neurosciences</topic><topic>Original Paper</topic><topic>Oxygen - analysis</topic><topic>Penaeidae - genetics</topic><topic>Phylogeny</topic><topic>Polymerase chain reaction</topic><topic>Reverse transcriptase polymerase chain reaction</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Sea water</topic><topic>Seawater</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>Shock heating</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, Fuhua</creatorcontrib><creatorcontrib>Luan, Wei</creatorcontrib><creatorcontrib>Zhang, Chengsong</creatorcontrib><creatorcontrib>Zhang, Jiquan</creatorcontrib><creatorcontrib>Wang, Bing</creatorcontrib><creatorcontrib>Xie, Yusu</creatorcontrib><creatorcontrib>Li, Shihao</creatorcontrib><creatorcontrib>Xiang, Jianhai</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell stress & chaperones</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, Fuhua</au><au>Luan, Wei</au><au>Zhang, Chengsong</au><au>Zhang, Jiquan</au><au>Wang, Bing</au><au>Xie, Yusu</au><au>Li, Shihao</au><au>Xiang, Jianhai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning of Cytoplasmic Heat Shock Protein 90 (FcHSP90) from Fenneropenaeus chinensis and Its Expression Response to Heat Shock and Hypoxia</atitle><jtitle>Cell stress & chaperones</jtitle><stitle>Cell Stress and Chaperones</stitle><addtitle>Cell Stress Chaperones</addtitle><date>2009-03-01</date><risdate>2009</risdate><volume>14</volume><issue>2</issue><spage>161</spage><epage>172</epage><pages>161-172</pages><issn>1355-8145</issn><eissn>1466-1268</eissn><abstract>Heat shock protein 90 (HSP90) works as a multifunctional chaperone and is involved in the regulation of many essential cellular pathways. In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25°C to 35°C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocytes and gill, were induced at 2 h and depressed at 8 h during hypoxia stress. The assessment of FcHSP90 mRNA levels under heat shock and hypoxia stresses indicated that the transcription of FcHSP90 was very sensitive to heat shock and hypoxia, so we deduced that FcHSP90 might play very important roles for shrimp to cope with environmental stress.</abstract><cop>Dordrecht</cop><pub>Cell Stress Society International</pub><pmid>18668349</pmid><doi>10.1007/s12192-008-0069-6</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell stress & chaperones, 2009-03, Vol.14 (2), p.161-172 |
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| source | Jstor Complete Legacy; MEDLINE; Springer Nature - Complete Springer Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Amino acids Anaerobiosis Animals Base Sequence Biochemistry Biomedical and Life Sciences Biomedicine Cancer Research Cell Biology Cloning, Molecular Complementary DNA Cytoplasm - metabolism DNA, Complementary - genetics Gene Expression Profiling Gene Expression Regulation Heat shock proteins Heat-Shock Response - genetics Hemocytes HSP90 Heat-Shock Proteins - chemistry HSP90 Heat-Shock Proteins - genetics HSP90 Heat-Shock Proteins - metabolism Hypoxia Immunology Messenger RNA Molecular Sequence Data Neurosciences Original Paper Oxygen - analysis Penaeidae - genetics Phylogeny Polymerase chain reaction Reverse transcriptase polymerase chain reaction RNA, Messenger - genetics RNA, Messenger - metabolism Sea water Seawater Sequence Analysis, DNA Sequence Homology, Amino Acid Shock heating |
| title | Cloning of Cytoplasmic Heat Shock Protein 90 (FcHSP90) from Fenneropenaeus chinensis and Its Expression Response to Heat Shock and Hypoxia |
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