PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress
Abstract Cryopreservation of bull sperm, crucial for breeding and assisted reproduction, often reduces sperm quality due to oxidative stress. This study examines how oxidative stress during cryopreservation affects peroxiredoxin 5 (PRDX5) and peroxiredoxin 6 (PRDX6) proteins, leading to their transl...
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| Format: | Article |
| Language: | English |
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BMC
2025-01-01
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| Series: | Cell Communication and Signaling |
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| Online Access: | https://doi.org/10.1186/s12964-024-02015-9 |
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| author | Mostek-Majewska Agnieszka Bossowska-Nowicka Magdalena Słowińska Mariola Ciereszko Andrzej |
| author_facet | Mostek-Majewska Agnieszka Bossowska-Nowicka Magdalena Słowińska Mariola Ciereszko Andrzej |
| author_sort | Mostek-Majewska Agnieszka |
| collection | DOAJ |
| description | Abstract Cryopreservation of bull sperm, crucial for breeding and assisted reproduction, often reduces sperm quality due to oxidative stress. This study examines how oxidative stress during cryopreservation affects peroxiredoxin 5 (PRDX5) and peroxiredoxin 6 (PRDX6) proteins, leading to their translocation and oligomerization in bull sperm. Increased reactive oxygen species (ROS) and nitric oxide (NO) levels were linked to reduced mitochondrial potential, higher DNA fragmentation, and increased membrane fluidity, prompting PRDX5 to move intracellularly and PRDX6 to the cell membrane. Under cryopreservation, these proteins formed high molecular weight oligomers, that may shift from peroxidase to chaperone roles. Their interaction with Toll-like receptor 4 (TLR4) may be key to their intracellular transport. On the other hand, the presence of PRDX5 and PRDX6 in exosomal vesicles suggested a potential mechanism for their transport into sperm cells. Using Imaging Flow Cytometry and various PAGE techniques, the study detected PRDX5 and PRDX6 in different sperm locations and analyzed their oligomer formation. These findings highlight the adaptive roles of PRDX5 and PRDX6 in protecting sperm cells, offering insights that could improve cryopreservation protocols in animal breeding and human reproductive medicine, and advance our understanding of the oxidative stress response in sperm cells. |
| format | Article |
| id | doaj-art-e998b39e933e468096c7077364720b0f |
| institution | Kabale University |
| issn | 1478-811X |
| language | English |
| publishDate | 2025-01-01 |
| publisher | BMC |
| record_format | Article |
| series | Cell Communication and Signaling |
| spelling | doaj-art-e998b39e933e468096c7077364720b0f2025-01-12T12:32:55ZengBMCCell Communication and Signaling1478-811X2025-01-0123111610.1186/s12964-024-02015-9PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stressMostek-Majewska Agnieszka0Bossowska-Nowicka Magdalena1Słowińska Mariola2Ciereszko Andrzej3Institute of Animal Reproduction and Food ResearchInstitute of Animal Reproduction and Food ResearchInstitute of Animal Reproduction and Food ResearchInstitute of Animal Reproduction and Food ResearchAbstract Cryopreservation of bull sperm, crucial for breeding and assisted reproduction, often reduces sperm quality due to oxidative stress. This study examines how oxidative stress during cryopreservation affects peroxiredoxin 5 (PRDX5) and peroxiredoxin 6 (PRDX6) proteins, leading to their translocation and oligomerization in bull sperm. Increased reactive oxygen species (ROS) and nitric oxide (NO) levels were linked to reduced mitochondrial potential, higher DNA fragmentation, and increased membrane fluidity, prompting PRDX5 to move intracellularly and PRDX6 to the cell membrane. Under cryopreservation, these proteins formed high molecular weight oligomers, that may shift from peroxidase to chaperone roles. Their interaction with Toll-like receptor 4 (TLR4) may be key to their intracellular transport. On the other hand, the presence of PRDX5 and PRDX6 in exosomal vesicles suggested a potential mechanism for their transport into sperm cells. Using Imaging Flow Cytometry and various PAGE techniques, the study detected PRDX5 and PRDX6 in different sperm locations and analyzed their oligomer formation. These findings highlight the adaptive roles of PRDX5 and PRDX6 in protecting sperm cells, offering insights that could improve cryopreservation protocols in animal breeding and human reproductive medicine, and advance our understanding of the oxidative stress response in sperm cells.https://doi.org/10.1186/s12964-024-02015-9Bull spermPRDX5PRDX6Oxidative stressCryopreservation |
| spellingShingle | Mostek-Majewska Agnieszka Bossowska-Nowicka Magdalena Słowińska Mariola Ciereszko Andrzej PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress Cell Communication and Signaling Bull sperm PRDX5 PRDX6 Oxidative stress Cryopreservation |
| title | PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress |
| title_full | PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress |
| title_fullStr | PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress |
| title_full_unstemmed | PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress |
| title_short | PRDX5 and PRDX6 translocation and oligomerization in bull sperm: a response to cryopreservation-induced oxidative stress |
| title_sort | prdx5 and prdx6 translocation and oligomerization in bull sperm a response to cryopreservation induced oxidative stress |
| topic | Bull sperm PRDX5 PRDX6 Oxidative stress Cryopreservation |
| url | https://doi.org/10.1186/s12964-024-02015-9 |
| work_keys_str_mv | AT mostekmajewskaagnieszka prdx5andprdx6translocationandoligomerizationinbullspermaresponsetocryopreservationinducedoxidativestress AT bossowskanowickamagdalena prdx5andprdx6translocationandoligomerizationinbullspermaresponsetocryopreservationinducedoxidativestress AT słowinskamariola prdx5andprdx6translocationandoligomerizationinbullspermaresponsetocryopreservationinducedoxidativestress AT ciereszkoandrzej prdx5andprdx6translocationandoligomerizationinbullspermaresponsetocryopreservationinducedoxidativestress |