Molecular and expression analysis of apolipoprotein E gene in the Chinese sturgeon, Acipenser sinensis.
Identifieur interne : 000352 ( Ncbi/Curation ); précédent : 000351; suivant : 000353Molecular and expression analysis of apolipoprotein E gene in the Chinese sturgeon, Acipenser sinensis.
Auteurs : Chuang-Ju Li [République populaire de Chine] ; Fang Gan ; Xi-Hua Chen ; Zhi-Gang Liu ; Luo-Xin Li ; Qi-Wei Wei ; Yong-Kai TangSource :
- Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology [ 1879-1107 ] ; 2011.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Apolipoproteins E (chemistry), Apolipoproteins E (genetics), Cloning, Molecular, Fishes (genetics), Gene Expression Profiling, Molecular Sequence Data, Phylogeny, Protein Conformation, RNA, Messenger (genetics), RNA, Messenger (metabolism), Reverse Transcriptase Polymerase Chain Reaction, Sequence Alignment, Species Specificity.
- MESH :
- chemical , chemistry : Apolipoproteins E.
- chemical , genetics : Apolipoproteins E, RNA, Messenger.
- genetics : Fishes.
- chemical , metabolism : RNA, Messenger.
- Amino Acid Sequence, Animals, Cloning, Molecular, Gene Expression Profiling, Molecular Sequence Data, Phylogeny, Protein Conformation, Reverse Transcriptase Polymerase Chain Reaction, Sequence Alignment, Species Specificity.
Abstract
Apolipoproteins are carrier proteins that bind to lipids to form lipoprotein particles and have been shown to play an important role in lipid metabolism. In this study, a full-length cDNA for apolipoprotein E, named AsapoE, was cloned from the Chinese sturgeon (Acipenser sinensis). This cDNA sequence is 1289 bp in length, and codes for a polypeptide of 274 amino acid residues, which is 45% and 42% identical to that of the rainbow trout and zebrafish, respectively, and 39%, 30%, and 29% identical to frog, mouse, and human respectively. The predicted AsApoE protein has a conserved amphipathic α-helix region with the potential to bind to lipids. RT-PCR analysis reveals that AsapoE is expressed in all tissues examined with a preferential expression in the kidney and liver. During the embryo development stage, AsapoE mRNA is low but still detectable at gastrula stage embryos; then AsapoE mRNAs reach a higher level in muscle contraction stage embryos, this relatively stable expression persists during the following embryogenic stages and declines 1 day after hatching. These results will serve as a basis for comparative studies on vertebrate apoE genes.
DOI: 10.1016/j.cbpb.2010.09.008
PubMed: 20868764
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Molecular and expression analysis of apolipoprotein E gene in the Chinese sturgeon, Acipenser sinensis.</title><author><name sortKey="Li, Chuang Ju" sort="Li, Chuang Ju" uniqKey="Li C" first="Chuang-Ju" last="Li">Chuang-Ju Li</name><affiliation wicri:level="1"><nlm:affiliation>Freshwater Fisheries Research Center, Chinese Academy of Fisheries Science, Wuxi 214081, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Freshwater Fisheries Research Center, Chinese Academy of Fisheries Science, Wuxi 214081</wicri:regionArea><wicri:noRegion>Wuxi 214081</wicri:noRegion></affiliation></author><author><name sortKey="Gan, Fang" sort="Gan, Fang" uniqKey="Gan F" first="Fang" last="Gan">Fang Gan</name></author><author><name sortKey="Chen, Xi Hua" sort="Chen, Xi Hua" uniqKey="Chen X" first="Xi-Hua" last="Chen">Xi-Hua Chen</name></author><author><name sortKey="Liu, Zhi Gang" sort="Liu, Zhi Gang" uniqKey="Liu Z" first="Zhi-Gang" last="Liu">Zhi-Gang Liu</name></author><author><name sortKey="Li, Luo Xin" sort="Li, Luo Xin" uniqKey="Li L" first="Luo-Xin" last="Li">Luo-Xin Li</name></author><author><name sortKey="Wei, Qi Wei" sort="Wei, Qi Wei" uniqKey="Wei Q" first="Qi-Wei" last="Wei">Qi-Wei Wei</name></author><author><name sortKey="Tang, Yong Kai" sort="Tang, Yong Kai" uniqKey="Tang Y" first="Yong-Kai" last="Tang">Yong-Kai Tang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:20868764</idno><idno type="pmid">20868764</idno><idno type="doi">10.1016/j.cbpb.2010.09.008</idno><idno type="wicri:Area/PubMed/Corpus">000367</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000367</idno><idno type="wicri:Area/PubMed/Curation">000367</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000367</idno><idno type="wicri:Area/PubMed/Checkpoint">000367</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000367</idno><idno type="wicri:Area/Ncbi/Merge">000352</idno><idno type="wicri:Area/Ncbi/Curation">000352</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular and expression analysis of apolipoprotein E gene in the Chinese sturgeon, Acipenser sinensis.</title><author><name sortKey="Li, Chuang Ju" sort="Li, Chuang Ju" uniqKey="Li C" first="Chuang-Ju" last="Li">Chuang-Ju Li</name><affiliation wicri:level="1"><nlm:affiliation>Freshwater Fisheries Research Center, Chinese Academy of Fisheries Science, Wuxi 214081, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Freshwater Fisheries Research Center, Chinese Academy of Fisheries Science, Wuxi 214081</wicri:regionArea><wicri:noRegion>Wuxi 214081</wicri:noRegion></affiliation></author><author><name sortKey="Gan, Fang" sort="Gan, Fang" uniqKey="Gan F" first="Fang" last="Gan">Fang Gan</name></author><author><name sortKey="Chen, Xi Hua" sort="Chen, Xi Hua" uniqKey="Chen X" first="Xi-Hua" last="Chen">Xi-Hua Chen</name></author><author><name sortKey="Liu, Zhi Gang" sort="Liu, Zhi Gang" uniqKey="Liu Z" first="Zhi-Gang" last="Liu">Zhi-Gang Liu</name></author><author><name sortKey="Li, Luo Xin" sort="Li, Luo Xin" uniqKey="Li L" first="Luo-Xin" last="Li">Luo-Xin Li</name></author><author><name sortKey="Wei, Qi Wei" sort="Wei, Qi Wei" uniqKey="Wei Q" first="Qi-Wei" last="Wei">Qi-Wei Wei</name></author><author><name sortKey="Tang, Yong Kai" sort="Tang, Yong Kai" uniqKey="Tang Y" first="Yong-Kai" last="Tang">Yong-Kai Tang</name></author></analytic><series><title level="j">Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology</title><idno type="eISSN">1879-1107</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Apolipoproteins E (chemistry)</term><term>Apolipoproteins E (genetics)</term><term>Cloning, Molecular</term><term>Fishes (genetics)</term><term>Gene Expression Profiling</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Protein Conformation</term><term>RNA, Messenger (genetics)</term><term>RNA, Messenger (metabolism)</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Sequence Alignment</term><term>Species Specificity</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Apolipoproteins E</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Apolipoproteins E</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>RNA, Messenger</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cloning, Molecular</term><term>Gene Expression Profiling</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Protein Conformation</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Sequence Alignment</term><term>Species Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Apolipoproteins are carrier proteins that bind to lipids to form lipoprotein particles and have been shown to play an important role in lipid metabolism. In this study, a full-length cDNA for apolipoprotein E, named AsapoE, was cloned from the Chinese sturgeon (Acipenser sinensis). This cDNA sequence is 1289 bp in length, and codes for a polypeptide of 274 amino acid residues, which is 45% and 42% identical to that of the rainbow trout and zebrafish, respectively, and 39%, 30%, and 29% identical to frog, mouse, and human respectively. The predicted AsApoE protein has a conserved amphipathic α-helix region with the potential to bind to lipids. RT-PCR analysis reveals that AsapoE is expressed in all tissues examined with a preferential expression in the kidney and liver. During the embryo development stage, AsapoE mRNA is low but still detectable at gastrula stage embryos; then AsapoE mRNAs reach a higher level in muscle contraction stage embryos, this relatively stable expression persists during the following embryogenic stages and declines 1 day after hatching. These results will serve as a basis for comparative studies on vertebrate apoE genes.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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