Characterization of type I and II procollagen α1 chain in Amur sturgeon (Acipenser schrenckii) and comparison of their gene expression.
Identifieur interne : 000095 ( Main/Curation ); précédent : 000094; suivant : 000096Characterization of type I and II procollagen α1 chain in Amur sturgeon (Acipenser schrenckii) and comparison of their gene expression.
Auteurs : Xi Zhang [Japon] ; Noriko Azuma [Japon] ; Seishi Hagihara [Japon] ; Shinji Adachi [Japon] ; Kazuhiro Ura [Japon] ; Yasuaki Takagi [Japon]Source :
- Gene [ 1879-0038 ] ; 2016.
English descriptors
- KwdEn :
- Animals, Cloning, Molecular, Collagen Type I (chemistry), Collagen Type I (genetics), Collagen Type II (chemistry), Collagen Type II (genetics), Fish Proteins (chemistry), Fish Proteins (genetics), Fishes (genetics), Fishes (metabolism), Phylogeny, Protein Denaturation, Protein Stability, Protein Structure, Secondary, Protein Structure, Tertiary, Temperature.
- MESH :
- chemical , chemistry : Collagen Type I, Collagen Type II, Fish Proteins.
- chemical , genetics : Collagen Type I, Collagen Type II, Fish Proteins.
- genetics : Fishes.
- metabolism : Fishes.
- Animals, Cloning, Molecular, Phylogeny, Protein Denaturation, Protein Stability, Protein Structure, Secondary, Protein Structure, Tertiary, Temperature.
Abstract
To characterize type I and II collagen in the Amur sturgeon at the molecular level, mRNAs encoding the proα chain of both types of collagen were cloned and sequenced. Full sequences of both were obtained, and the molecular phylogeny based on the deduced amino acid sequence indicated that the correct sequences of the target genes were obtained. Analyses of primary structure of the proα chains revealed that type I and II collagen share the basic structure of the proα chain of fibril collagen, but have different characteristics, especially in residues related to thermal stability. In the triple helical domain, Gly-Pro-Pro sequence stabilizing the tripeptide unit was more frequent in type II than in type I, and Gly-Gly, which likely decline in thermal stability, was more frequent in type I than in type II. These results suggested that the denaturation temperature of type II would be remarkably higher than type I. The spatial pattern of gene expression was analyzed by quantitative real-time PCR, which showed that relatively ubiquitous type I gene and strongly skewed distribution of type II gene, which highly expressed only in vertebra, snout cartilage, and notochord. This pattern was similar to the distribution pattern of each collagen protein detected by previous biochemical analyses using Amur and Bester sturgeons. The present study is the first report of the cloning of the full-length cDNAs for both of type I and type II collagen in the Amur sturgeon, and is the first comparative analysis of type I and II collagens in a sturgeon species at the molecular level. The results provide basic and general information on collagens in sturgeons.
DOI: 10.1016/j.gene.2015.12.038
PubMed: 26768575
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Electronic address: norikoazuma@gmail.com.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate</wicri:regionArea><wicri:noRegion>Hakodate</wicri:noRegion></affiliation></author><author><name sortKey="Hagihara, Seishi" sort="Hagihara, Seishi" uniqKey="Hagihara S" first="Seishi" last="Hagihara">Seishi Hagihara</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate</wicri:regionArea><wicri:noRegion>Hakodate</wicri:noRegion></affiliation></author><author><name sortKey="Adachi, Shinji" sort="Adachi, Shinji" uniqKey="Adachi S" first="Shinji" last="Adachi">Shinji Adachi</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate</wicri:regionArea><wicri:noRegion>Hakodate</wicri:noRegion></affiliation></author><author><name sortKey="Ura, Kazuhiro" sort="Ura, Kazuhiro" uniqKey="Ura K" first="Kazuhiro" last="Ura">Kazuhiro Ura</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate</wicri:regionArea><wicri:noRegion>Hakodate</wicri:noRegion></affiliation></author><author><name sortKey="Takagi, Yasuaki" sort="Takagi, Yasuaki" uniqKey="Takagi Y" first="Yasuaki" last="Takagi">Yasuaki Takagi</name><affiliation wicri:level="1"><nlm:affiliation>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Graduate School of Fisheries Sciences, Hokkaido University, Hakodate</wicri:regionArea><wicri:noRegion>Hakodate</wicri:noRegion></affiliation></author></analytic><series><title level="j">Gene</title><idno type="eISSN">1879-0038</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cloning, Molecular</term><term>Collagen Type I (chemistry)</term><term>Collagen Type I (genetics)</term><term>Collagen Type II (chemistry)</term><term>Collagen Type II (genetics)</term><term>Fish Proteins (chemistry)</term><term>Fish Proteins (genetics)</term><term>Fishes (genetics)</term><term>Fishes (metabolism)</term><term>Phylogeny</term><term>Protein Denaturation</term><term>Protein Stability</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Temperature</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Collagen Type I</term><term>Collagen Type II</term><term>Fish Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Collagen Type I</term><term>Collagen Type II</term><term>Fish Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cloning, Molecular</term><term>Phylogeny</term><term>Protein Denaturation</term><term>Protein Stability</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To characterize type I and II collagen in the Amur sturgeon at the molecular level, mRNAs encoding the proα chain of both types of collagen were cloned and sequenced. Full sequences of both were obtained, and the molecular phylogeny based on the deduced amino acid sequence indicated that the correct sequences of the target genes were obtained. Analyses of primary structure of the proα chains revealed that type I and II collagen share the basic structure of the proα chain of fibril collagen, but have different characteristics, especially in residues related to thermal stability. In the triple helical domain, Gly-Pro-Pro sequence stabilizing the tripeptide unit was more frequent in type II than in type I, and Gly-Gly, which likely decline in thermal stability, was more frequent in type I than in type II. These results suggested that the denaturation temperature of type II would be remarkably higher than type I. The spatial pattern of gene expression was analyzed by quantitative real-time PCR, which showed that relatively ubiquitous type I gene and strongly skewed distribution of type II gene, which highly expressed only in vertebra, snout cartilage, and notochord. This pattern was similar to the distribution pattern of each collagen protein detected by previous biochemical analyses using Amur and Bester sturgeons. The present study is the first report of the cloning of the full-length cDNAs for both of type I and type II collagen in the Amur sturgeon, and is the first comparative analysis of type I and II collagens in a sturgeon species at the molecular level. The results provide basic and general information on collagens in sturgeons.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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