Sperm Adhesion Molecule 1 (SPAM1) Distribution in Selected Human Sperm by Hyaluronic Acid Test
The failures of binding to the oocyte zona pellucida are commonly attributed to defects in the sperm recognition, adhesion, and fusion molecules. SPAM1 (sperm adhesion molecule 1) is a hyaluronidase implicated in the dispersion of the cumulus-oocyte matrix. Therefore, the aim of this study was to ch...
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MDPI AG
2022-10-01
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author | María José Gómez-Torres Paula Sáez-Espinosa Paula Manzano-Santiago Laura Robles-Gómez Natalia Huerta-Retamal Jon Aizpurua |
author_facet | María José Gómez-Torres Paula Sáez-Espinosa Paula Manzano-Santiago Laura Robles-Gómez Natalia Huerta-Retamal Jon Aizpurua |
author_sort | María José Gómez-Torres |
collection | DOAJ |
description | The failures of binding to the oocyte zona pellucida are commonly attributed to defects in the sperm recognition, adhesion, and fusion molecules. SPAM1 (sperm adhesion molecule 1) is a hyaluronidase implicated in the dispersion of the cumulus-oocyte matrix. Therefore, the aim of this study was to characterize the SPAM1 distribution in the different physiological conditions of human sperm. Specifically, we evaluated the location of the SPAM1 protein in human sperm before capacitation, at one and four hours of capacitation and after hyaluronic acid (HA) selection test by fluorescence microscopy. Sperm bound to HA were considered mature and those that crossed it immature. Our results detected three SPAM1 fluorescent patterns: label throughout the head (P1), equatorial segment with acrosomal faith label (P2), and postacrosomal label (P3). The data obtained after recovering the mature sperm by the HA selection significantly (<i>p</i> < 0.05) highlighted the P1 in both capacitation times, being 79.74 and 81.48% after one hour and four hours, respectively. Thus, the HA test identified that human sperm require the presence of SPAM1 throughout the sperm head (P1) to properly contact the cumulus-oocyte matrix. Overall, our results provide novel insights into the physiological basis of sperm capacitation and could contribute to the improvement of selection techniques. |
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spelling | doaj.art-88ac9be7691641d596f6e8fdc1cbd6ba2023-11-23T23:04:58ZengMDPI AGBiomedicines2227-90592022-10-011010255310.3390/biomedicines10102553Sperm Adhesion Molecule 1 (SPAM1) Distribution in Selected Human Sperm by Hyaluronic Acid TestMaría José Gómez-Torres0Paula Sáez-Espinosa1Paula Manzano-Santiago2Laura Robles-Gómez3Natalia Huerta-Retamal4Jon Aizpurua5Departamento de Biotecnología, Universidad de Alicante, 03690 Alicante, SpainDepartamento de Biotecnología, Universidad de Alicante, 03690 Alicante, SpainDepartamento de Biotecnología, Universidad de Alicante, 03690 Alicante, SpainDepartamento de Biotecnología, Universidad de Alicante, 03690 Alicante, SpainDepartamento de Biotecnología, Universidad de Alicante, 03690 Alicante, SpainIVF Spain, Reproductive Medicine, 03540 Alicante, SpainThe failures of binding to the oocyte zona pellucida are commonly attributed to defects in the sperm recognition, adhesion, and fusion molecules. SPAM1 (sperm adhesion molecule 1) is a hyaluronidase implicated in the dispersion of the cumulus-oocyte matrix. Therefore, the aim of this study was to characterize the SPAM1 distribution in the different physiological conditions of human sperm. Specifically, we evaluated the location of the SPAM1 protein in human sperm before capacitation, at one and four hours of capacitation and after hyaluronic acid (HA) selection test by fluorescence microscopy. Sperm bound to HA were considered mature and those that crossed it immature. Our results detected three SPAM1 fluorescent patterns: label throughout the head (P1), equatorial segment with acrosomal faith label (P2), and postacrosomal label (P3). The data obtained after recovering the mature sperm by the HA selection significantly (<i>p</i> < 0.05) highlighted the P1 in both capacitation times, being 79.74 and 81.48% after one hour and four hours, respectively. Thus, the HA test identified that human sperm require the presence of SPAM1 throughout the sperm head (P1) to properly contact the cumulus-oocyte matrix. Overall, our results provide novel insights into the physiological basis of sperm capacitation and could contribute to the improvement of selection techniques.https://www.mdpi.com/2227-9059/10/10/2553hyaluronic acidhyaluronidase PH-20male infertilityspermatozoasperm capacitation |
spellingShingle | María José Gómez-Torres Paula Sáez-Espinosa Paula Manzano-Santiago Laura Robles-Gómez Natalia Huerta-Retamal Jon Aizpurua Sperm Adhesion Molecule 1 (SPAM1) Distribution in Selected Human Sperm by Hyaluronic Acid Test Biomedicines hyaluronic acid hyaluronidase PH-20 male infertility spermatozoa sperm capacitation |
title | Sperm Adhesion Molecule 1 (SPAM1) Distribution in Selected Human Sperm by Hyaluronic Acid Test |
title_full | Sperm Adhesion Molecule 1 (SPAM1) Distribution in Selected Human Sperm by Hyaluronic Acid Test |
title_fullStr | Sperm Adhesion Molecule 1 (SPAM1) Distribution in Selected Human Sperm by Hyaluronic Acid Test |
title_full_unstemmed | Sperm Adhesion Molecule 1 (SPAM1) Distribution in Selected Human Sperm by Hyaluronic Acid Test |
title_short | Sperm Adhesion Molecule 1 (SPAM1) Distribution in Selected Human Sperm by Hyaluronic Acid Test |
title_sort | sperm adhesion molecule 1 spam1 distribution in selected human sperm by hyaluronic acid test |
topic | hyaluronic acid hyaluronidase PH-20 male infertility spermatozoa sperm capacitation |
url | https://www.mdpi.com/2227-9059/10/10/2553 |
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