EF-Hand-Binding Secreted Protein Hdh-SMP5 Regulates Shell Biomineralization and Responses to Stress in Pacific Abalone, <i>Haliotis discus hannai</i>
The development of a shell is a complex calcium metabolic process involving shell matrix proteins (SMPs). In this study, we describe the isolation, characterization, and expression of SMP5 and investigate its potential regulatory role in the shell biomineralization of Pacific abalone <i>Haliot...
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2023-12-01
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author | Md Abu Hanif Ji Do Han Soo Cheol Kim Shaharior Hossen Kang Hee Kho |
author_facet | Md Abu Hanif Ji Do Han Soo Cheol Kim Shaharior Hossen Kang Hee Kho |
author_sort | Md Abu Hanif |
collection | DOAJ |
description | The development of a shell is a complex calcium metabolic process involving shell matrix proteins (SMPs). In this study, we describe the isolation, characterization, and expression of SMP5 and investigate its potential regulatory role in the shell biomineralization of Pacific abalone <i>Haliotis discus hannai</i>. The full-length <i>Hdh-SMP5</i> cDNA contains 685 bp and encodes a polypeptide of 134 amino acids. Structurally, the Hdh-SMP5 protein belongs to the EF-hand-binding superfamily, which possesses three EF-hand Ca<sup>2+</sup>-binding regions and is rich in aspartic acid. The distinct clustering patterns in the phylogenetic tree indicate that the amino acid composition and structure of this protein may vary among different SMPs. During early development, significantly higher expression was observed in the trochophore and veliger stages. <i>Hdh-SMP5</i> was also upregulated during shell biomineralization in Pacific abalone. Long periods of starvation cause <i>Hdh-SMP5</i> expression to decrease. Furthermore, <i>Hdh-SMP5</i> expression was observed to be significantly higher under thermal stress at temperatures of 15, 30, and 25 °C for durations of 6 h, 12 h, and 48 h, respectively. Our study is the first to characterize Hdh-SMP5 comprehensively and analyze its expression to elucidate its dynamic roles in ontogenetic development, shell biomineralization, and the response to starvation and thermal stress. |
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spelling | doaj.art-0a956faf69ed4e3f88ff452539318ad72023-12-22T14:00:44ZengMDPI AGCurrent Issues in Molecular Biology1467-30371467-30452023-12-014512100791009610.3390/cimb45120629EF-Hand-Binding Secreted Protein Hdh-SMP5 Regulates Shell Biomineralization and Responses to Stress in Pacific Abalone, <i>Haliotis discus hannai</i>Md Abu Hanif0Ji Do Han1Soo Cheol Kim2Shaharior Hossen3Kang Hee Kho4Department of Fisheries Science, Chonnam National University, Yeosu 59626, Republic of KoreaSouth Sea Fisheries Research Institute, National Institute of Fisheries Science, Yeosu 59780, Republic of KoreaSouth Sea Fisheries Research Institute, National Institute of Fisheries Science, Yeosu 59780, Republic of KoreaDepartment of Fisheries Science, Chonnam National University, Yeosu 59626, Republic of KoreaDepartment of Fisheries Science, Chonnam National University, Yeosu 59626, Republic of KoreaThe development of a shell is a complex calcium metabolic process involving shell matrix proteins (SMPs). In this study, we describe the isolation, characterization, and expression of SMP5 and investigate its potential regulatory role in the shell biomineralization of Pacific abalone <i>Haliotis discus hannai</i>. The full-length <i>Hdh-SMP5</i> cDNA contains 685 bp and encodes a polypeptide of 134 amino acids. Structurally, the Hdh-SMP5 protein belongs to the EF-hand-binding superfamily, which possesses three EF-hand Ca<sup>2+</sup>-binding regions and is rich in aspartic acid. The distinct clustering patterns in the phylogenetic tree indicate that the amino acid composition and structure of this protein may vary among different SMPs. During early development, significantly higher expression was observed in the trochophore and veliger stages. <i>Hdh-SMP5</i> was also upregulated during shell biomineralization in Pacific abalone. Long periods of starvation cause <i>Hdh-SMP5</i> expression to decrease. Furthermore, <i>Hdh-SMP5</i> expression was observed to be significantly higher under thermal stress at temperatures of 15, 30, and 25 °C for durations of 6 h, 12 h, and 48 h, respectively. Our study is the first to characterize Hdh-SMP5 comprehensively and analyze its expression to elucidate its dynamic roles in ontogenetic development, shell biomineralization, and the response to starvation and thermal stress.https://www.mdpi.com/1467-3045/45/12/629Pacific abalonesecreted proteinEF handbiomineralizationstarvationthermal stress |
spellingShingle | Md Abu Hanif Ji Do Han Soo Cheol Kim Shaharior Hossen Kang Hee Kho EF-Hand-Binding Secreted Protein Hdh-SMP5 Regulates Shell Biomineralization and Responses to Stress in Pacific Abalone, <i>Haliotis discus hannai</i> Current Issues in Molecular Biology Pacific abalone secreted protein EF hand biomineralization starvation thermal stress |
title | EF-Hand-Binding Secreted Protein Hdh-SMP5 Regulates Shell Biomineralization and Responses to Stress in Pacific Abalone, <i>Haliotis discus hannai</i> |
title_full | EF-Hand-Binding Secreted Protein Hdh-SMP5 Regulates Shell Biomineralization and Responses to Stress in Pacific Abalone, <i>Haliotis discus hannai</i> |
title_fullStr | EF-Hand-Binding Secreted Protein Hdh-SMP5 Regulates Shell Biomineralization and Responses to Stress in Pacific Abalone, <i>Haliotis discus hannai</i> |
title_full_unstemmed | EF-Hand-Binding Secreted Protein Hdh-SMP5 Regulates Shell Biomineralization and Responses to Stress in Pacific Abalone, <i>Haliotis discus hannai</i> |
title_short | EF-Hand-Binding Secreted Protein Hdh-SMP5 Regulates Shell Biomineralization and Responses to Stress in Pacific Abalone, <i>Haliotis discus hannai</i> |
title_sort | ef hand binding secreted protein hdh smp5 regulates shell biomineralization and responses to stress in pacific abalone i haliotis discus hannai i |
topic | Pacific abalone secreted protein EF hand biomineralization starvation thermal stress |
url | https://www.mdpi.com/1467-3045/45/12/629 |
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