Molecular cloning, characterization, and expression of two 5-HTRs from the pearl oyster Pinctada fucata martensii
The receptors of serotonin, also known as 5-hydroxytryptamine receptor (5-HTR) can mediate regulatory metamorphosis processes in a variety of mollusks. Studying the mechanisms of metamorphosis of the pearl oyster is significant to elucidate breeding, resource recovery and marine pearl production. In...
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Online Access: | http://dx.doi.org/10.3389/fmars.2022.1011420 https://www.frontiersin.org/articles/10.3389/fmars.2022.1011420/full |
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crfrontiers:10.3389/fmars.2022.1011420 2024-02-11T10:03:13+01:00 Molecular cloning, characterization, and expression of two 5-HTRs from the pearl oyster Pinctada fucata martensii Zhu, Shaojie He, Yubo Xu, Qiongyu Zhang, Jiabin Yang, Chuangye Hao, Ruijuan Li, Junhui Deng, Yuewen National Natural Science Foundation of China 2022 http://dx.doi.org/10.3389/fmars.2022.1011420 https://www.frontiersin.org/articles/10.3389/fmars.2022.1011420/full unknown Frontiers Media SA https://creativecommons.org/licenses/by/4.0/ Frontiers in Marine Science volume 9 ISSN 2296-7745 Ocean Engineering Water Science and Technology Aquatic Science Global and Planetary Change Oceanography journal-article 2022 crfrontiers https://doi.org/10.3389/fmars.2022.1011420 2024-01-26T10:07:35Z The receptors of serotonin, also known as 5-hydroxytryptamine receptor (5-HTR) can mediate regulatory metamorphosis processes in a variety of mollusks. Studying the mechanisms of metamorphosis of the pearl oyster is significant to elucidate breeding, resource recovery and marine pearl production. In this study, two 5-HTR genes from Pinctada fucata martensii ( Pm5-HTR2 and Pm5-HTR4 ) were cloned. A total of 1623 bp open reading frame was identified in Pm5-HTR2 , and a 1185 bp open reading frame was detected in Pm5-HTR4 these open reading frames encoded a 540-residue polypeptide and a 394-residue polypeptide, respectively. We also conducted a domain analysis, which indicated that Pm5-HTR2 and Pm5-HTR4 contained a seven-transmembrane domain and revealed that the receptors had high similarity to Crassostrea gigas 5-HTR2 (54.62%) and 5-HTR4 (66.23%). Sequence analysis demonstrated conserved advanced structure and motifs (the DRY/ERY and NPXXY motifs). The expression pattern analysis revealed high expression levels of Pm5-HTR2 and Pm5-HTR4 during the developmental stages. ISH analysis showed that Pm5-HTR2 was primarily expressed in the FE, B, T, EU, and EL stages and Pm5-HTR4 was mainly expressed in the FE, B, T, D, EU, and EL stages. These results suggest that 5-HTRs may play key roles in P. f. martensii larval metamorphosis. Article in Journal/Newspaper Crassostrea gigas Frontiers (Publisher) Frontiers in Marine Science 9 |
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Frontiers (Publisher) |
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unknown |
topic |
Ocean Engineering Water Science and Technology Aquatic Science Global and Planetary Change Oceanography |
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Ocean Engineering Water Science and Technology Aquatic Science Global and Planetary Change Oceanography Zhu, Shaojie He, Yubo Xu, Qiongyu Zhang, Jiabin Yang, Chuangye Hao, Ruijuan Li, Junhui Deng, Yuewen Molecular cloning, characterization, and expression of two 5-HTRs from the pearl oyster Pinctada fucata martensii |
topic_facet |
Ocean Engineering Water Science and Technology Aquatic Science Global and Planetary Change Oceanography |
description |
The receptors of serotonin, also known as 5-hydroxytryptamine receptor (5-HTR) can mediate regulatory metamorphosis processes in a variety of mollusks. Studying the mechanisms of metamorphosis of the pearl oyster is significant to elucidate breeding, resource recovery and marine pearl production. In this study, two 5-HTR genes from Pinctada fucata martensii ( Pm5-HTR2 and Pm5-HTR4 ) were cloned. A total of 1623 bp open reading frame was identified in Pm5-HTR2 , and a 1185 bp open reading frame was detected in Pm5-HTR4 these open reading frames encoded a 540-residue polypeptide and a 394-residue polypeptide, respectively. We also conducted a domain analysis, which indicated that Pm5-HTR2 and Pm5-HTR4 contained a seven-transmembrane domain and revealed that the receptors had high similarity to Crassostrea gigas 5-HTR2 (54.62%) and 5-HTR4 (66.23%). Sequence analysis demonstrated conserved advanced structure and motifs (the DRY/ERY and NPXXY motifs). The expression pattern analysis revealed high expression levels of Pm5-HTR2 and Pm5-HTR4 during the developmental stages. ISH analysis showed that Pm5-HTR2 was primarily expressed in the FE, B, T, EU, and EL stages and Pm5-HTR4 was mainly expressed in the FE, B, T, D, EU, and EL stages. These results suggest that 5-HTRs may play key roles in P. f. martensii larval metamorphosis. |
author2 |
National Natural Science Foundation of China |
format |
Article in Journal/Newspaper |
author |
Zhu, Shaojie He, Yubo Xu, Qiongyu Zhang, Jiabin Yang, Chuangye Hao, Ruijuan Li, Junhui Deng, Yuewen |
author_facet |
Zhu, Shaojie He, Yubo Xu, Qiongyu Zhang, Jiabin Yang, Chuangye Hao, Ruijuan Li, Junhui Deng, Yuewen |
author_sort |
Zhu, Shaojie |
title |
Molecular cloning, characterization, and expression of two 5-HTRs from the pearl oyster Pinctada fucata martensii |
title_short |
Molecular cloning, characterization, and expression of two 5-HTRs from the pearl oyster Pinctada fucata martensii |
title_full |
Molecular cloning, characterization, and expression of two 5-HTRs from the pearl oyster Pinctada fucata martensii |
title_fullStr |
Molecular cloning, characterization, and expression of two 5-HTRs from the pearl oyster Pinctada fucata martensii |
title_full_unstemmed |
Molecular cloning, characterization, and expression of two 5-HTRs from the pearl oyster Pinctada fucata martensii |
title_sort |
molecular cloning, characterization, and expression of two 5-htrs from the pearl oyster pinctada fucata martensii |
publisher |
Frontiers Media SA |
publishDate |
2022 |
url |
http://dx.doi.org/10.3389/fmars.2022.1011420 https://www.frontiersin.org/articles/10.3389/fmars.2022.1011420/full |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_source |
Frontiers in Marine Science volume 9 ISSN 2296-7745 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3389/fmars.2022.1011420 |
container_title |
Frontiers in Marine Science |
container_volume |
9 |
_version_ |
1790599408478322688 |