Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility
HSP70s constitute a family of chaperones, some isoforms of which appear to play a role in sperm function. Notably, global proteomic studies analyzing proteins deregulated in asthenozoospermia, a main cause of male infertility characterized by low sperm motility, showed the dysregulation of some HSP7...
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| Format: | Article |
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MDPI AG
2022-06-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/12/6497 |
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| author | Sarah Grassi Marie Bisconti Baptiste Martinet Vanessa Arcolia Jean-François Simon Ruddy Wattiez Baptiste Leroy Elise Hennebert |
| author_facet | Sarah Grassi Marie Bisconti Baptiste Martinet Vanessa Arcolia Jean-François Simon Ruddy Wattiez Baptiste Leroy Elise Hennebert |
| author_sort | Sarah Grassi |
| collection | DOAJ |
| description | HSP70s constitute a family of chaperones, some isoforms of which appear to play a role in sperm function. Notably, global proteomic studies analyzing proteins deregulated in asthenozoospermia, a main cause of male infertility characterized by low sperm motility, showed the dysregulation of some HSP70 isoforms. However, to date, no clear trend has been established since the variations in the abundance of HSP70 isoforms differed between studies. The HSPA2 isoform has been reported to play a key role in fertilization, but its dysregulation and possible relocation during capacitation, a maturation process making the spermatozoon capable of fertilizing an oocyte, is debated in the literature. The aim of the present study was to investigate the fate of all sperm HSP70 isoforms during capacitation and in relation to sperm motility. Using Multiple-Reaction Monitoring (MRM) mass spectrometry, we showed that the relative abundance of all detected isoforms was stable between non-capacitated and capacitated spermatozoa. Immunofluorescence using two different antibodies also demonstrated the stability of HSP70 isoform localization during capacitation. We also investigated spermatozoa purified from 20 sperm samples displaying various levels of total and progressive sperm motility. We showed that the abundance of HSP70 isoforms is not correlated to sperm total or progressive motility. |
| first_indexed | 2024-03-09T23:34:54Z |
| format | Article |
| id | doaj.art-370d7709371847a8b7c7ad51812b032c |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-09T23:34:54Z |
| publishDate | 2022-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-370d7709371847a8b7c7ad51812b032c2023-11-23T17:01:44ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-06-012312649710.3390/ijms23126497Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and MotilitySarah Grassi0Marie Bisconti1Baptiste Martinet2Vanessa Arcolia3Jean-François Simon4Ruddy Wattiez5Baptiste Leroy6Elise Hennebert7Laboratory of Cell Biology, Research Institute for Biosciences, Research Institute for Health Sciences and Technology, University of Mons, Place du Parc 23, 7000 Mons, BelgiumLaboratory of Cell Biology, Research Institute for Biosciences, Research Institute for Health Sciences and Technology, University of Mons, Place du Parc 23, 7000 Mons, BelgiumEvolutionary Biology & Ecology, Université Libre de Bruxelles, Avenue Paul Héger-CP 160/12, 1000 Brussels, BelgiumClinique de Fertilité Régionale de Mons, CHU Ambroise Paré Hospital, Boulevard Kennedy 2, 7000 Mons, BelgiumClinique de Fertilité Régionale de Mons, CHU Ambroise Paré Hospital, Boulevard Kennedy 2, 7000 Mons, BelgiumLaboratory of Proteomics and Microbiology, CISMa, Research Institute for Biosciences, University of Mons, Place du Parc 23, 7000 Mons, BelgiumLaboratory of Proteomics and Microbiology, CISMa, Research Institute for Biosciences, University of Mons, Place du Parc 23, 7000 Mons, BelgiumLaboratory of Cell Biology, Research Institute for Biosciences, Research Institute for Health Sciences and Technology, University of Mons, Place du Parc 23, 7000 Mons, BelgiumHSP70s constitute a family of chaperones, some isoforms of which appear to play a role in sperm function. Notably, global proteomic studies analyzing proteins deregulated in asthenozoospermia, a main cause of male infertility characterized by low sperm motility, showed the dysregulation of some HSP70 isoforms. However, to date, no clear trend has been established since the variations in the abundance of HSP70 isoforms differed between studies. The HSPA2 isoform has been reported to play a key role in fertilization, but its dysregulation and possible relocation during capacitation, a maturation process making the spermatozoon capable of fertilizing an oocyte, is debated in the literature. The aim of the present study was to investigate the fate of all sperm HSP70 isoforms during capacitation and in relation to sperm motility. Using Multiple-Reaction Monitoring (MRM) mass spectrometry, we showed that the relative abundance of all detected isoforms was stable between non-capacitated and capacitated spermatozoa. Immunofluorescence using two different antibodies also demonstrated the stability of HSP70 isoform localization during capacitation. We also investigated spermatozoa purified from 20 sperm samples displaying various levels of total and progressive sperm motility. We showed that the abundance of HSP70 isoforms is not correlated to sperm total or progressive motility.https://www.mdpi.com/1422-0067/23/12/6497spermatozoaHSP70 isoformsLC–MRM mass spectrometrycapacitationsperm motility |
| spellingShingle | Sarah Grassi Marie Bisconti Baptiste Martinet Vanessa Arcolia Jean-François Simon Ruddy Wattiez Baptiste Leroy Elise Hennebert Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility International Journal of Molecular Sciences spermatozoa HSP70 isoforms LC–MRM mass spectrometry capacitation sperm motility |
| title | Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility |
| title_full | Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility |
| title_fullStr | Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility |
| title_full_unstemmed | Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility |
| title_short | Targeted Analysis of HSP70 Isoforms in Human Spermatozoa in the Context of Capacitation and Motility |
| title_sort | targeted analysis of hsp70 isoforms in human spermatozoa in the context of capacitation and motility |
| topic | spermatozoa HSP70 isoforms LC–MRM mass spectrometry capacitation sperm motility |
| url | https://www.mdpi.com/1422-0067/23/12/6497 |
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