Insect Peptide CopA3 Mitigates the Effects of Heat Stress on Porcine Muscle Satellite Cells
Heat stress inhibits cell proliferation as well as animal production. Here, we aimed to demonstrate that 9-mer disulfide dimer peptide (CopA3) supplementation stabilizes porcine muscle satellite cell (PMSC) proliferation and heat shock protein (HSP) expression at different temperatures. Therefore, w...
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| Format: | Article |
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MDPI AG
2023-10-01
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| Series: | Animals |
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| Online Access: | https://www.mdpi.com/2076-2615/13/20/3209 |
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| author | Jeongeun Lee Shah Ahmed Belal Xi Lin Jinryong Park Kwanseob Shim |
| author_facet | Jeongeun Lee Shah Ahmed Belal Xi Lin Jinryong Park Kwanseob Shim |
| author_sort | Jeongeun Lee |
| collection | DOAJ |
| description | Heat stress inhibits cell proliferation as well as animal production. Here, we aimed to demonstrate that 9-mer disulfide dimer peptide (CopA3) supplementation stabilizes porcine muscle satellite cell (PMSC) proliferation and heat shock protein (HSP) expression at different temperatures. Therefore, we investigated the beneficial effects of CopA3 on PMSCs at three different temperatures (37, 39, and 41 °C). Based on temperature and CopA3 treatment, PMSCs were divided into six different groups including treatment and control groups for each temperature. Cell viability was highest with 10 µg/mL CopA3 and decreased as the concentration increased in a dose-dependent manner. CopA3 significantly increased the cell viability at all temperatures at 24 and 48 h. It significantly decreased apoptosis compared to that in the untreated groups. In addition, it decreased the apoptosis-related protein, Bcl-2-associated X (BAX), expression at 41 °C. Notably, temperature and CopA3 had no effects on the apoptosis-related protein, caspase 3. Expression levels of HSP40, HSP70, and HSP90 were significantly upregulated, whereas those of HSP47 and HSP60 were not affected by temperature changes. Except HSP90, CopA3 did not cause temperature-dependent changes in protein expression. Therefore, CopA3 promotes cell proliferation, inhibits apoptosis, and maintains stable HSP expression, thereby enhancing the heat-stress-tolerance capacity of PMSCs. |
| first_indexed | 2024-03-10T21:30:50Z |
| format | Article |
| id | doaj.art-eafa403dff884fa3bc02060d15111533 |
| institution | Directory Open Access Journal |
| issn | 2076-2615 |
| language | English |
| last_indexed | 2024-03-10T21:30:50Z |
| publishDate | 2023-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Animals |
| spelling | doaj.art-eafa403dff884fa3bc02060d151115332023-11-19T15:24:40ZengMDPI AGAnimals2076-26152023-10-011320320910.3390/ani13203209Insect Peptide CopA3 Mitigates the Effects of Heat Stress on Porcine Muscle Satellite CellsJeongeun Lee0Shah Ahmed Belal1Xi Lin2Jinryong Park3Kwanseob Shim4Department of Agricultural Convergence Technology, Jeonbuk National University, Jeonju 54896, Republic of KoreaDepartment of Animal Biotechnology, Jeonbuk National University, Jeonju 54896, Republic of KoreaDepartment of Animal Science, North Carolina State University, Raleigh, NC 27695, USADepartment of Stem Cell and Regenerative Biotechnology, Konkuk University, Seoul 05029, Republic of KoreaDepartment of Agricultural Convergence Technology, Jeonbuk National University, Jeonju 54896, Republic of KoreaHeat stress inhibits cell proliferation as well as animal production. Here, we aimed to demonstrate that 9-mer disulfide dimer peptide (CopA3) supplementation stabilizes porcine muscle satellite cell (PMSC) proliferation and heat shock protein (HSP) expression at different temperatures. Therefore, we investigated the beneficial effects of CopA3 on PMSCs at three different temperatures (37, 39, and 41 °C). Based on temperature and CopA3 treatment, PMSCs were divided into six different groups including treatment and control groups for each temperature. Cell viability was highest with 10 µg/mL CopA3 and decreased as the concentration increased in a dose-dependent manner. CopA3 significantly increased the cell viability at all temperatures at 24 and 48 h. It significantly decreased apoptosis compared to that in the untreated groups. In addition, it decreased the apoptosis-related protein, Bcl-2-associated X (BAX), expression at 41 °C. Notably, temperature and CopA3 had no effects on the apoptosis-related protein, caspase 3. Expression levels of HSP40, HSP70, and HSP90 were significantly upregulated, whereas those of HSP47 and HSP60 were not affected by temperature changes. Except HSP90, CopA3 did not cause temperature-dependent changes in protein expression. Therefore, CopA3 promotes cell proliferation, inhibits apoptosis, and maintains stable HSP expression, thereby enhancing the heat-stress-tolerance capacity of PMSCs.https://www.mdpi.com/2076-2615/13/20/3209porcine satellite cellCopA3cell viabilityheat shock proteinheat stress |
| spellingShingle | Jeongeun Lee Shah Ahmed Belal Xi Lin Jinryong Park Kwanseob Shim Insect Peptide CopA3 Mitigates the Effects of Heat Stress on Porcine Muscle Satellite Cells Animals porcine satellite cell CopA3 cell viability heat shock protein heat stress |
| title | Insect Peptide CopA3 Mitigates the Effects of Heat Stress on Porcine Muscle Satellite Cells |
| title_full | Insect Peptide CopA3 Mitigates the Effects of Heat Stress on Porcine Muscle Satellite Cells |
| title_fullStr | Insect Peptide CopA3 Mitigates the Effects of Heat Stress on Porcine Muscle Satellite Cells |
| title_full_unstemmed | Insect Peptide CopA3 Mitigates the Effects of Heat Stress on Porcine Muscle Satellite Cells |
| title_short | Insect Peptide CopA3 Mitigates the Effects of Heat Stress on Porcine Muscle Satellite Cells |
| title_sort | insect peptide copa3 mitigates the effects of heat stress on porcine muscle satellite cells |
| topic | porcine satellite cell CopA3 cell viability heat shock protein heat stress |
| url | https://www.mdpi.com/2076-2615/13/20/3209 |
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