Two HSPs gene from juvenile Amur sturgeon (Acipenser schrenckii): cloning, characterization and expression pattern to crowding and hypoxia stress.
Identifieur interne : 000157 ( PubMed/Corpus ); précédent : 000156; suivant : 000158Two HSPs gene from juvenile Amur sturgeon (Acipenser schrenckii): cloning, characterization and expression pattern to crowding and hypoxia stress.
Auteurs : Meng Ni ; Haishen Wen ; Jifang Li ; Meili Chi ; Yuanyuan Ren ; Zhifei Song ; Houmeng DingSource :
- Fish physiology and biochemistry [ 1573-5168 ] ; 2014.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animal Husbandry, Animals, Base Sequence, Cloning, Molecular, Fishes (growth & development), Fishes (metabolism), Gene Expression Regulation, Developmental (physiology), HSP70 Heat-Shock Proteins (genetics), HSP70 Heat-Shock Proteins (metabolism), HSP90 Heat-Shock Proteins (genetics), HSP90 Heat-Shock Proteins (metabolism), Hypoxia (metabolism), Molecular Sequence Data, RNA (genetics), RNA (metabolism), Species Specificity, Stress, Physiological (physiology).
- MESH :
- chemical , genetics : HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, RNA.
- growth & development : Fishes.
- metabolism : Fishes, HSP70 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Hypoxia, RNA.
- physiology : Gene Expression Regulation, Developmental, Stress, Physiological.
- Amino Acid Sequence, Animal Husbandry, Animals, Base Sequence, Cloning, Molecular, Molecular Sequence Data, Species Specificity.
Abstract
In this study, the cDNA sequences of HSP70 and HSP90 were isolated from the special chondr-ganoid scale, Amur sturgeon, for the first time. Homology analysis indicated that amino acid sequences of HSP70 and HSP90 shared high identity with other species (82.68-99.07 and 90.19-98.07%, respectively). The tissue expression analysis showed that the asHSP70 and asHSP90 mRNA were ubiquitously expressed in all the examined tissues under unstressed condition. The expression pattern of HSP70 and HSP90 under chronic (crowding) and acute (hypoxia) stress was examined by q-PCR in liver, spleen and kidney. Results showed that stocking density could significantly influence the expression of HSP70 at day 20 and/or day 40. In contrast to stocking density, levels of HSP70 transcripts indicated a remarkable increase in all examined tissues after hypoxia stress. HSP90 levels in liver and spleen increased significantly in high stocking density. By comparison, significant increase of asHSP90 in kidney was only found in high stocking density at day 40. Similar to HSP70, the levels of HSP90 transcripts showed significant increases after hypoxia stress except the transcript of liver in H2 group 6 h after hypoxia. The assessment of asHSP70 and asHSP90 mRNA levels under crowding and hypoxia stresses indicated that asHSP70 and asHSP90 gene might be good indicators of stressful situations for Amur sturgeon. Taking serum globulin and electrolytes account, we suggest that crowding and hypoxia stress can result in considerable stress for Amur sturgeon.
DOI: 10.1007/s10695-014-9969-9
PubMed: 25117508
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pubmed:25117508Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Two HSPs gene from juvenile Amur sturgeon (Acipenser schrenckii): cloning, characterization and expression pattern to crowding and hypoxia stress.</title><author><name sortKey="Ni, Meng" sort="Ni, Meng" uniqKey="Ni M" first="Meng" last="Ni">Meng Ni</name><affiliation><nlm:affiliation>Fisheries College, Ocean University of China, 5 Yushan Road, Qingdao, Shandong, 266003, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Wen, Haishen" sort="Wen, Haishen" uniqKey="Wen H" first="Haishen" last="Wen">Haishen Wen</name></author><author><name sortKey="Li, Jifang" sort="Li, Jifang" uniqKey="Li J" first="Jifang" last="Li">Jifang Li</name></author><author><name sortKey="Chi, Meili" sort="Chi, Meili" uniqKey="Chi M" first="Meili" last="Chi">Meili Chi</name></author><author><name sortKey="Ren, Yuanyuan" sort="Ren, Yuanyuan" uniqKey="Ren Y" first="Yuanyuan" last="Ren">Yuanyuan Ren</name></author><author><name sortKey="Song, Zhifei" sort="Song, Zhifei" uniqKey="Song Z" first="Zhifei" last="Song">Zhifei Song</name></author><author><name sortKey="Ding, Houmeng" sort="Ding, Houmeng" uniqKey="Ding H" first="Houmeng" last="Ding">Houmeng Ding</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25117508</idno><idno type="pmid">25117508</idno><idno type="doi">10.1007/s10695-014-9969-9</idno><idno type="wicri:Area/PubMed/Corpus">000157</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000157</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Two HSPs gene from juvenile Amur sturgeon (Acipenser schrenckii): cloning, characterization and expression pattern to crowding and hypoxia stress.</title><author><name sortKey="Ni, Meng" sort="Ni, Meng" uniqKey="Ni M" first="Meng" last="Ni">Meng Ni</name><affiliation><nlm:affiliation>Fisheries College, Ocean University of China, 5 Yushan Road, Qingdao, Shandong, 266003, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Wen, Haishen" sort="Wen, Haishen" uniqKey="Wen H" first="Haishen" last="Wen">Haishen Wen</name></author><author><name sortKey="Li, Jifang" sort="Li, Jifang" uniqKey="Li J" first="Jifang" last="Li">Jifang Li</name></author><author><name sortKey="Chi, Meili" sort="Chi, Meili" uniqKey="Chi M" first="Meili" last="Chi">Meili Chi</name></author><author><name sortKey="Ren, Yuanyuan" sort="Ren, Yuanyuan" uniqKey="Ren Y" first="Yuanyuan" last="Ren">Yuanyuan Ren</name></author><author><name sortKey="Song, Zhifei" sort="Song, Zhifei" uniqKey="Song Z" first="Zhifei" last="Song">Zhifei Song</name></author><author><name sortKey="Ding, Houmeng" sort="Ding, Houmeng" uniqKey="Ding H" first="Houmeng" last="Ding">Houmeng Ding</name></author></analytic><series><title level="j">Fish physiology and biochemistry</title><idno type="eISSN">1573-5168</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animal Husbandry</term><term>Animals</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Fishes (growth & development)</term><term>Fishes (metabolism)</term><term>Gene Expression Regulation, Developmental (physiology)</term><term>HSP70 Heat-Shock Proteins (genetics)</term><term>HSP70 Heat-Shock Proteins (metabolism)</term><term>HSP90 Heat-Shock Proteins (genetics)</term><term>HSP90 Heat-Shock Proteins (metabolism)</term><term>Hypoxia (metabolism)</term><term>Molecular Sequence Data</term><term>RNA (genetics)</term><term>RNA (metabolism)</term><term>Species Specificity</term><term>Stress, Physiological (physiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>HSP70 Heat-Shock Proteins</term><term>HSP90 Heat-Shock Proteins</term><term>RNA</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fishes</term><term>HSP70 Heat-Shock Proteins</term><term>HSP90 Heat-Shock Proteins</term><term>Hypoxia</term><term>RNA</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Gene Expression Regulation, Developmental</term><term>Stress, Physiological</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animal Husbandry</term><term>Animals</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Molecular Sequence Data</term><term>Species Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In this study, the cDNA sequences of HSP70 and HSP90 were isolated from the special chondr-ganoid scale, Amur sturgeon, for the first time. Homology analysis indicated that amino acid sequences of HSP70 and HSP90 shared high identity with other species (82.68-99.07 and 90.19-98.07%, respectively). The tissue expression analysis showed that the asHSP70 and asHSP90 mRNA were ubiquitously expressed in all the examined tissues under unstressed condition. The expression pattern of HSP70 and HSP90 under chronic (crowding) and acute (hypoxia) stress was examined by q-PCR in liver, spleen and kidney. Results showed that stocking density could significantly influence the expression of HSP70 at day 20 and/or day 40. In contrast to stocking density, levels of HSP70 transcripts indicated a remarkable increase in all examined tissues after hypoxia stress. HSP90 levels in liver and spleen increased significantly in high stocking density. By comparison, significant increase of asHSP90 in kidney was only found in high stocking density at day 40. Similar to HSP70, the levels of HSP90 transcripts showed significant increases after hypoxia stress except the transcript of liver in H2 group 6 h after hypoxia. The assessment of asHSP70 and asHSP90 mRNA levels under crowding and hypoxia stresses indicated that asHSP70 and asHSP90 gene might be good indicators of stressful situations for Amur sturgeon. Taking serum globulin and electrolytes account, we suggest that crowding and hypoxia stress can result in considerable stress for Amur sturgeon.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25117508</PMID><DateCreated><Year>2014</Year><Month>11</Month><Day>10</Day></DateCreated><DateCompleted><Year>2015</Year><Month>07</Month><Day>13</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-5168</ISSN><JournalIssue CitedMedium="Internet"><Volume>40</Volume><Issue>6</Issue><PubDate><Year>2014</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Fish physiology and biochemistry</Title><ISOAbbreviation>Fish Physiol. Biochem.</ISOAbbreviation></Journal><ArticleTitle>Two HSPs gene from juvenile Amur sturgeon (Acipenser schrenckii): cloning, characterization and expression pattern to crowding and hypoxia stress.</ArticleTitle><Pagination><MedlinePgn>1801-16</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s10695-014-9969-9</ELocationID><Abstract><AbstractText>In this study, the cDNA sequences of HSP70 and HSP90 were isolated from the special chondr-ganoid scale, Amur sturgeon, for the first time. Homology analysis indicated that amino acid sequences of HSP70 and HSP90 shared high identity with other species (82.68-99.07 and 90.19-98.07%, respectively). The tissue expression analysis showed that the asHSP70 and asHSP90 mRNA were ubiquitously expressed in all the examined tissues under unstressed condition. The expression pattern of HSP70 and HSP90 under chronic (crowding) and acute (hypoxia) stress was examined by q-PCR in liver, spleen and kidney. Results showed that stocking density could significantly influence the expression of HSP70 at day 20 and/or day 40. In contrast to stocking density, levels of HSP70 transcripts indicated a remarkable increase in all examined tissues after hypoxia stress. HSP90 levels in liver and spleen increased significantly in high stocking density. By comparison, significant increase of asHSP90 in kidney was only found in high stocking density at day 40. Similar to HSP70, the levels of HSP90 transcripts showed significant increases after hypoxia stress except the transcript of liver in H2 group 6 h after hypoxia. The assessment of asHSP70 and asHSP90 mRNA levels under crowding and hypoxia stresses indicated that asHSP70 and asHSP90 gene might be good indicators of stressful situations for Amur sturgeon. Taking serum globulin and electrolytes account, we suggest that crowding and hypoxia stress can result in considerable stress for Amur sturgeon.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ni</LastName><ForeName>Meng</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Fisheries College, Ocean University of China, 5 Yushan Road, Qingdao, Shandong, 266003, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wen</LastName><ForeName>Haishen</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Jifang</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Chi</LastName><ForeName>Meili</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ren</LastName><ForeName>Yuanyuan</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Zhifei</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Ding</LastName><ForeName>Houmeng</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>08</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Fish Physiol Biochem</MedlineTA><NlmUniqueID>100955049</NlmUniqueID><ISSNLinking>0920-1742</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018840">HSP70 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018841">HSP90 Heat-Shock Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance 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Developmental</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018840" MajorTopicYN="N">HSP70 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018841" MajorTopicYN="N">HSP90 Heat-Shock Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000860" MajorTopicYN="N">Hypoxia</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName 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PubStatus="medline"><Year>2015</Year><Month>7</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25117508</ArticleId><ArticleId IdType="doi">10.1007/s10695-014-9969-9</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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