Molecular Characterization and Response of Prolyl Hydroxylase Domain (PHD) Genes to Hypoxia Stress in <i>Hypophthalmichthys molitrix</i>
As an economically and ecologically important freshwater fish, silver carp (<i>Hypophthalmichthys molitrix</i>) is sensitive to low oxygen tension. Prolyl hydroxylase domain (PHD) proteins are critical regulators of adaptive responses to hypoxia for their function of regulating the hypox...
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MDPI AG
2022-01-01
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| author | Xiaohui Li Meidong Zhang Chen Ling Hang Sha Guiwei Zou Hongwei Liang |
| author_facet | Xiaohui Li Meidong Zhang Chen Ling Hang Sha Guiwei Zou Hongwei Liang |
| author_sort | Xiaohui Li |
| collection | DOAJ |
| description | As an economically and ecologically important freshwater fish, silver carp (<i>Hypophthalmichthys molitrix</i>) is sensitive to low oxygen tension. Prolyl hydroxylase domain (PHD) proteins are critical regulators of adaptive responses to hypoxia for their function of regulating the hypoxia inducible factor-1 alpha subunit (HIF-1α) stability via hydroxylation reaction. In the present study, three PHD genes were cloned from <i>H</i><i>. molitrix</i> by rapid amplification of cDNA ends (RACE). The total length of <i>HmPHD1</i>, <i>HmPHD2</i>, and <i>HmPHD3</i> were 2981, 1954, and 1847 base pair (bp), and contained 1449, 1080, and 738 bp open reading frames (ORFs) that encoded 482, 359, and 245 amino acids (aa), respectively. Amino acid sequence analysis showed that HmPHD1, HmPHD2, and HmPHD3 had the conserved prolyl 4-hydroxylase alpha subunit homolog domains at their C-termini. Meanwhile, the evaluation of phylogeny revealed PHD2 and PHD3 of <i>H. molitrix</i> were more closely related as they belonged to sister clades, whereas the clade of PHD1 was relatively distant from these two. The transcripts of PHD genes are ubiquitously distributed in <i>H. molitrix</i> tissues, with the highest expressional level of <i>HmPHD1</i> and <i>HmPHD</i><i>3</i> in liver, and <i>HmPHD2</i> in muscle. After acute hypoxic treatment for 0.5 h, PHD genes of <i>H. molitrix</i> were induced mainly in liver and brain, and different from <i>HmPHD1</i> and <i>HmPHD2</i>, the expression of <i>HmPHD3</i> showed no overt tissue specificity. Furthermore, under continued hypoxic condition, PHD genes exhibited an obviously rapid but gradually attenuated response from 3 h to 24 h, and upon reoxygenation, the transcriptional expression of PHD genes showed a decreasing trend in most of the tissues. These results indicate that the PHD genes of <i>H. molitrix</i> are involved in the early response to hypoxic stress, and they show tissue-specific transcript expression when performing physiological regulation functions. This study is of great relevance for advancing our understanding of how PHD genes are regulated when addressing the hypoxic challenge and provides a reference for the subsequent research of the molecular mechanisms underlying hypoxia adaptation in silver carp. |
| first_indexed | 2024-03-10T03:03:48Z |
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| spelling | doaj.art-86d298cdd10647dcbfb4bd98e63084d32023-11-23T12:40:56ZengMDPI AGAnimals2076-26152022-01-0112213110.3390/ani12020131Molecular Characterization and Response of Prolyl Hydroxylase Domain (PHD) Genes to Hypoxia Stress in <i>Hypophthalmichthys molitrix</i>Xiaohui Li0Meidong Zhang1Chen Ling2Hang Sha3Guiwei Zou4Hongwei Liang5Yangtze River Fisheries Research Institute, Chinese Academy of Fishery Sciences, Wuhan 430223, ChinaYangtze River Fisheries Research Institute, Chinese Academy of Fishery Sciences, Wuhan 430223, ChinaYangtze River Fisheries Research Institute, Chinese Academy of Fishery Sciences, Wuhan 430223, ChinaYangtze River Fisheries Research Institute, Chinese Academy of Fishery Sciences, Wuhan 430223, ChinaYangtze River Fisheries Research Institute, Chinese Academy of Fishery Sciences, Wuhan 430223, ChinaYangtze River Fisheries Research Institute, Chinese Academy of Fishery Sciences, Wuhan 430223, ChinaAs an economically and ecologically important freshwater fish, silver carp (<i>Hypophthalmichthys molitrix</i>) is sensitive to low oxygen tension. Prolyl hydroxylase domain (PHD) proteins are critical regulators of adaptive responses to hypoxia for their function of regulating the hypoxia inducible factor-1 alpha subunit (HIF-1α) stability via hydroxylation reaction. In the present study, three PHD genes were cloned from <i>H</i><i>. molitrix</i> by rapid amplification of cDNA ends (RACE). The total length of <i>HmPHD1</i>, <i>HmPHD2</i>, and <i>HmPHD3</i> were 2981, 1954, and 1847 base pair (bp), and contained 1449, 1080, and 738 bp open reading frames (ORFs) that encoded 482, 359, and 245 amino acids (aa), respectively. Amino acid sequence analysis showed that HmPHD1, HmPHD2, and HmPHD3 had the conserved prolyl 4-hydroxylase alpha subunit homolog domains at their C-termini. Meanwhile, the evaluation of phylogeny revealed PHD2 and PHD3 of <i>H. molitrix</i> were more closely related as they belonged to sister clades, whereas the clade of PHD1 was relatively distant from these two. The transcripts of PHD genes are ubiquitously distributed in <i>H. molitrix</i> tissues, with the highest expressional level of <i>HmPHD1</i> and <i>HmPHD</i><i>3</i> in liver, and <i>HmPHD2</i> in muscle. After acute hypoxic treatment for 0.5 h, PHD genes of <i>H. molitrix</i> were induced mainly in liver and brain, and different from <i>HmPHD1</i> and <i>HmPHD2</i>, the expression of <i>HmPHD3</i> showed no overt tissue specificity. Furthermore, under continued hypoxic condition, PHD genes exhibited an obviously rapid but gradually attenuated response from 3 h to 24 h, and upon reoxygenation, the transcriptional expression of PHD genes showed a decreasing trend in most of the tissues. These results indicate that the PHD genes of <i>H. molitrix</i> are involved in the early response to hypoxic stress, and they show tissue-specific transcript expression when performing physiological regulation functions. This study is of great relevance for advancing our understanding of how PHD genes are regulated when addressing the hypoxic challenge and provides a reference for the subsequent research of the molecular mechanisms underlying hypoxia adaptation in silver carp.https://www.mdpi.com/2076-2615/12/2/131PHD<i>hypophthalmichthys molitrix</i>RACEhypoxic stressgene expression |
| spellingShingle | Xiaohui Li Meidong Zhang Chen Ling Hang Sha Guiwei Zou Hongwei Liang Molecular Characterization and Response of Prolyl Hydroxylase Domain (PHD) Genes to Hypoxia Stress in <i>Hypophthalmichthys molitrix</i> Animals PHD <i>hypophthalmichthys molitrix</i> RACE hypoxic stress gene expression |
| title | Molecular Characterization and Response of Prolyl Hydroxylase Domain (PHD) Genes to Hypoxia Stress in <i>Hypophthalmichthys molitrix</i> |
| title_full | Molecular Characterization and Response of Prolyl Hydroxylase Domain (PHD) Genes to Hypoxia Stress in <i>Hypophthalmichthys molitrix</i> |
| title_fullStr | Molecular Characterization and Response of Prolyl Hydroxylase Domain (PHD) Genes to Hypoxia Stress in <i>Hypophthalmichthys molitrix</i> |
| title_full_unstemmed | Molecular Characterization and Response of Prolyl Hydroxylase Domain (PHD) Genes to Hypoxia Stress in <i>Hypophthalmichthys molitrix</i> |
| title_short | Molecular Characterization and Response of Prolyl Hydroxylase Domain (PHD) Genes to Hypoxia Stress in <i>Hypophthalmichthys molitrix</i> |
| title_sort | molecular characterization and response of prolyl hydroxylase domain phd genes to hypoxia stress in i hypophthalmichthys molitrix i |
| topic | PHD <i>hypophthalmichthys molitrix</i> RACE hypoxic stress gene expression |
| url | https://www.mdpi.com/2076-2615/12/2/131 |
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