ADAM20 Participates Modestly to Fertilization as Its Absence Leads to In Vitro Hypofertility in Mouse.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: ADAM20 Participates Modestly to Fertilization as Its Absence Leads to In Vitro Hypofertility in Mouse.
Συγγραφείς: Girault MS; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France., Dupuis S; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France., Pierre R; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France., Gourier C; Laboratoire de Physique de l'Ecole Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université Paris Cité, Paris, France., Lee JE; Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada., Barbaux S; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France., Ziyyat A; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France.; Service d'Histologie, d'Embryologie, Biologie de la Reproduction, AP-HP, Hôpital Cochin, Paris, France.
Πηγή: Cell biochemistry and function [Cell Biochem Funct] 2026 Jul; Vol. 44 (7), pp. e70265.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Wiley-Blackwell Country of Publication: England NLM ID: 8305874 Publication Model: Print Cited Medium: Internet ISSN: 1099-0844 (Electronic) Linking ISSN: 02636484 NLM ISO Abbreviation: Cell Biochem Funct Subsets: MEDLINE
Imprint Name(s): Publication: Oxford, England : Wiley-Blackwell
Original Publication: Guildford, Surrey : Butterworth Scientific Ltd., c1983-
Ιατρικοί όροι (MeSH): ADAM Proteins*/genetics , ADAM Proteins*/metabolism , ADAM Proteins*/deficiency , Infertility, Male*/genetics , Infertility, Male*/metabolism , Fertilization* , Fertility*, Spermatozoa/metabolism ; Animals ; Male ; Mice ; Mice, Knockout ; Female ; Fertilization in Vitro
Περίληψη: A mutation of the ADAM20 gene was described in an infertile patient whose spermatozoa were observed accumulating in the perivitelline space of oocytes. To decipher its role in the fertilization process, we produced a mouse model knock-out (KO) for the Adam20 gene. Surprisingly, Adam20-KO males showed an in vivo fertility similar to their wild-type littermates and had normal sperm counts and morphology. However, they presented a reduced fertility in in vitro fertilization assays. To explore the hypothesis that the two flanking genes Adam25 and Adam39 could compensate the lack of Adam20 given their very high homology, we produced a triple KO deleting these three neighbor genes simultaneously. The phenotype was strictly identical to that of the single gene deletion. Therefore, ADAM20, ADAM25, and ADAM39 are not essential proteins for fertilization in mice but they seem to participate modestly to the process. Adam20-KO males are fertile in vivo but have a reduced fertility in vitro. Males deleted for three neighbor and very homologous genes (Adam20, Adam25, and Adam39) have the same phenotype as the simple Adam20-KO. These genes are dispensable for normal fertility but contribute modestly to fertilization.
(© 2026 John Wiley & Sons Ltd.)
References: M. Chalbi, V. Barraud‐Lange, B. Ravaux, et al., “Binding of Sperm Protein Izumo1 and Its Egg Receptor Juno Drives Cd9 Accumulation in the Intercellular Contact Area Prior to Fusion During Mammalian Fertilization,” Development 141 (2014): 3732–3739, https://doi.org/10.1242/dev.111534.
A. Jégou, A. Ziyyat, V. Barraud‐Lange, et al., “CD9 Tetraspanin Generates Fusion Competent Sites on the Egg Membrane for Mammalian Fertilization,” Proceedings of the National Academy of Sciences 108 (2011): 10946–10951, https://doi.org/10.1073/pnas.1017400108.
F. Le Naour, E. Rubinstein, C. Jasmin, M. Prenant, and C. Boucheix, “Severely Reduced Female Fertility in CD9‐Deficient Mice,” Science 287 (2000): 319–321, https://doi.org/10.1126/science.287.5451.319.
K. Miyado, G. Yamada, S. Yamada, et al., “Requirement of CD9 on the Egg Plasma Membrane for Fertilization,” Science 287 (2000): 321–324.
K. Kaji, S. Oda, T. Shikano, et al., “The Gamete Fusion Process Is Defective in Eggs of Cd9‐Deficient Mice,” Nature Genetics 24 (2000): 279–282, https://doi.org/10.1038/73502.
E. Bianchi, B. Doe, D. Goulding, and G. J. Wright, “Juno Is the Egg Izumo Receptor and Is Essential for Mammalian Fertilization,” Nature 508 (2014): 483–487, https://doi.org/10.1038/nature13203.
N. Inoue, M. Ikawa, A. Isotani, and M. Okabe, “The Immunoglobulin Superfamily Protein Izumo Is Required for Sperm to Fuse With Eggs,” Nature 434 (2005): 234–238, https://doi.org/10.1038/nature03362.
B. Ravaux, S. Favier, E. Perez, and C. Gourier, “Egg CD9 Protein Tides Correlated With Sperm Oscillations Tune the Gamete Fusion Ability in Mammal,” Journal of Molecular Cell Biology 10 (2018): 494–502, https://doi.org/10.1093/jmcb/mjy005.
N. Inoue, D. Hamada, H. Kamikubo, et al., “Molecular Dissection of IZUMO1, a Sperm Protein Essential for Sperm‐Egg Fusion,” Development 140 (2013): 3221–3229, https://doi.org/10.1242/dev.094854.
S. Barbaux, C. Ialy‐Radio, M. Chalbi, et al., “Sperm SPACA6 Protein Is Required for Mammalian Sperm‐Egg Adhesion/Fusion,” Scientific Reports 10 (2020): 5335, https://doi.org/10.1038/s41598-020-62091-y.
Y. Fujihara, Y. Lu, T. Noda, et al., “Spermatozoa Lacking Fertilization Influencing Membrane Protein (FIMP) Fail to Fuse With Oocytes in Mice,” Proceedings of the National Academy of Sciences 117 (2020): 9393–9400, https://doi.org/10.1073/pnas.1917060117.
M. Hernandez‐Falco, P. Saez‐Espinosa, A. Lopez‐Botella, J. Aizpurua, and M. J. Gomez‐Torres, “The Role of Sperm Proteins IZUMO1 and TMEM95 in Mammalian Fertilization: A Systematic Review,” International Journal of Molecular Sciences 23 (2022): 3929, https://doi.org/10.3390/ijms23073929.
N. Inoue, Y. Hagihara, and I. Wada, “Evolutionarily Conserved Sperm Factors, DCST1 and DCST2, Are Required for Gamete Fusion,” eLife 10 (2021): e66313, https://doi.org/10.7554/eLife.66313.
I. Lamas‐Toranzo, J. G. Hamze, E. Bianchi, et al., “TMEM95 Is a Sperm Membrane Protein Essential for Mammalian Fertilization,” eLife 9 (2020): e53913, https://doi.org/10.7554/eLife.53913.
T. Noda, A. Blaha, Y. Fujihara, et al., “Sperm Membrane Proteins DCST1 and DCST2 Are Required for Sperm‐Egg Interaction in Mice and Fish,” Communications Biology 5 (2022): 332, https://doi.org/10.1038/s42003-022-03289-w.
T. Noda, Y. Lu, Y. Fujihara, et al., “Sperm Proteins SOF1, TMEM95, and SPACA6 Are Required for Sperm‐Oocyte Fusion in Mice,” Proceedings of the National Academy of Sciences 117 (2020): 11493–11502, https://doi.org/10.1073/pnas.1922650117.
S. Tang, Y. Lu, W. M. Skinner, et al., “Human Sperm TMEM95 Binds Eggs and Facilitates Membrane Fusion,” Proceedings of the National Academy of Sciences of the United States of America 119 (2022): e2207805119, https://doi.org/10.1073/pnas.2207805119.
V. E. Deneke, A. Blaha, Y. Lu, et al., “A Conserved Fertilization Complex Bridges Sperm and Egg in Vertebrates,” Cell 187 (2024): 7066–7078.e22, https://doi.org/10.1016/j.cell.2024.09.035.
D. Lorenzetti, C. Poirier, M. Zhao, P. A. Overbeek, W. Harrison, and C. E. Bishop, “A Transgenic Insertion on Mouse Chromosome 17 Inactivates a Novel Immunoglobulin Superfamily Gene Potentially Involved in Sperm‐Egg Fusion,” Mammalian Genome 25 (2014): 141–148, https://doi.org/10.1007/s00335-013-9491-x.
C. Jean, F. Haghighirad, Y. Zhu, et al., “JUNO, the Receptor of Sperm IZUMO1, Is Expressed by the Human Oocyte and Is Essential for Human Fertilisation,” Human Reproduction 34 (2019): 118–126, https://doi.org/10.1093/humrep/dey340.
A. Ziyyat, E. Rubinstein, F. Monier‐Gavelle, et al., “CD9 Controls the Formation of Clusters That Contain Tetraspanins and the Integrin α6β1, Which Are Involved in Human and Mouse Gamete Fusion,” Journal of Cell Science 119 (2006): 416–424, https://doi.org/10.1242/jcs.02730.
Y. W. Sha, X. Xu, Z. Y. Ji, et al., “Sperm‐Egg Fusion Disorder in a Chinese Male Patient Was Associated With a Rare ADAM20 Variant,” Oncotarget 9 (2018): 2086–2091, https://doi.org/10.18632/oncotarget.23331.
M. Aghababaei, K. Hogg, S. Perdu, W. P. Robinson, and A. G. Beristain, “ADAM12‐Directed Ectodomain Shedding of E‐Cadherin Potentiates Trophoblast Fusion,” Cell Death & Differentiation 22 (2015): 1970–1984, https://doi.org/10.1038/cdd.2015.44.
H. Nishimura, E. Kim, T. Nakanishi, and T. Baba, “Possible Function of the ADAM1a/ADAM2 Fertilin Complex in the Appearance of ADAM3 on the Sperm Surface,” Journal of Biological Chemistry 279 (2004): 34957–34962, https://doi.org/10.1074/jbc.M314249200.
T. Yagami‐Hiromasa, T. Sato, T. Kurisaki, K. Kamijo, Y. Nabeshima, and A. Fujisawa‐Sehara, “A Metalloprotease‐Disintegrin Participating in Myoblast Fusion,” Nature 377 (1995): 652–656, https://doi.org/10.1038/377652a0.
I. Choi, J. Oh, B. N. Cho, et al., “Characterization and Comparative Genomic Analysis of Intronless Adams With Testicular Gene Expression,” Genomics 83 (2004): 636–646, https://doi.org/10.1016/j.ygeno.2003.10.001.
A. Kelso, “The Enigma of Cytokine Redundancy,” Immunology & Cell Biology 72 (1994): 97–101, https://doi.org/10.1038/icb.1994.14.
A. Satyanarayana and P. Kaldis, “Mammalian Cell‐Cycle Regulation: Several Cdks, Numerous Cyclins and Diverse Compensatory Mechanisms,” Oncogene 28 (2009): 2925–2939, https://doi.org/10.1038/onc.2009.170.
G. Z. Zhu, Y. Lin, D. G. Myles, and P. Primakoff, “Identification of Four Novel ADAMs With Potential Roles in Spermatogenesis and Fertilization,” Gene 234 (1999): 227–237, https://doi.org/10.1016/s0378-1119(99)00208-5.
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C. Han, E. Choi, I. Park, et al., “Comprehensive Analysis of Reproductive ADAMs: Relationship of ADAM4 and ADAM6 With an ADAM Complex Required for Fertilization in Mice,” Biology of Reproduction 80 (2009): 1001–1008, https://doi.org/10.1095/biolreprod.108.073700.
T. T. T. Nguyen, K. Tokuhiro, K. Shimada, et al., “Gene‐Deficient Mouse Model Established by CRISPR/Cas9 System Reveals 15 Reproductive Organ‐Enriched Genes Dispensable for Male Fertility,” Frontiers in Cell and Developmental Biology 12 (2024): 1411162, https://doi.org/10.3389/fcell.2024.1411162.
S. Dupuis, M. S. Girault, M. Le Beulze, et al., “The Lack of Tex44 Causes Severe Subfertility With Flagellar Abnormalities in Male Mice,” Cellular & Molecular Biology Letters 29 (2024): 74, https://doi.org/10.1186/s11658-024-00587-5.
M. S. Girault, S. Dupuis, C. Ialy‐Radio, et al., “Deletion of the Spata3 Gene Induces Sperm Alterations and In Vitro Hypofertility in Mice,” International Journal of Molecular Sciences 22 (2021): 1959, https://doi.org/10.3390/ijms22041959.
H. Choi, C. Han, S. Jin, et al., “Reduced Fertility and Altered Epididymal and Sperm Integrity in Mice Lacking ADAM7,” Biology of Reproduction 93 (2015): 70, https://doi.org/10.1095/biolreprod.115.130252.
C. Han, J. T. Kwon, I. Park, et al., “Impaired Sperm Aggregation in Adam2 and Adam3 Null Mice,” Fertility and Sterility 93 (2010): 2754–2756, https://doi.org/10.1016/j.fertnstert.2010.03.013.
D. Mashiko, S. Tonai, and M. Ikawa, “ADAM5 Is Required for Sperm‐Zona Pellucida Binding and Sperm Oviduct Migration,” Biology of Reproduction 114 (2025): 1091–1100, https://doi.org/10.1093/biolre/ioaf254.
V. A. Voronina, F. M. Harris, J. Schmahl, et al., “Deletion of Adam6 in Mus Musculus Leads to Male Subfertility and Deficits in Sperm Ascent Into the Oviduct,” Biology of Reproduction 100 (2019): 686–696, https://doi.org/10.1093/biolre/ioy210.
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Grant Information: Institut National de la Santé et de la Recherche Médicale; Centre National de la Recherche Scientifique; Université Paris Cité; ANR-21-CE13-0032-01 Agence Nationale de la Recherche; CIHR; PJT-203841 Canada CAPMC CIHR; NFRFE-2019-00230 New frontiers in research fund
Contributed Indexing: Keywords: fertility; fertilization; infertility; knock‐out; male; mouse; sperm; testis
Substance Nomenclature: EC 3.4.24.- (ADAM Proteins)
Entry Date(s): Date Created: 20260715 Date Completed: 20260715 Latest Revision: 20260726
Update Code: 20260726
PubMed Central ID: PMC13370512
DOI: 10.1002/cbf.70265
PMID: 42454366
Βάση Δεδομένων: MEDLINE
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  Data: ADAM20 Participates Modestly to Fertilization as Its Absence Leads to In Vitro Hypofertility in Mouse.
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  Data: <searchLink fieldCode="AU" term="%22Girault+MS%22">Girault MS</searchLink>; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France.<br /><searchLink fieldCode="AU" term="%22Dupuis+S%22">Dupuis S</searchLink>; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France.<br /><searchLink fieldCode="AU" term="%22Pierre+R%22">Pierre R</searchLink>; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France.<br /><searchLink fieldCode="AU" term="%22Gourier+C%22">Gourier C</searchLink>; Laboratoire de Physique de l'Ecole Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université Paris Cité, Paris, France.<br /><searchLink fieldCode="AU" term="%22Lee+JE%22">Lee JE</searchLink>; Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.<br /><searchLink fieldCode="AU" term="%22Barbaux+S%22">Barbaux S</searchLink>; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France.<br /><searchLink fieldCode="AU" term="%22Ziyyat+A%22">Ziyyat A</searchLink>; Institut Cochin, INSERM, CNRS, Université Paris Cité, Paris, France.; Service d'Histologie, d'Embryologie, Biologie de la Reproduction, AP-HP, Hôpital Cochin, Paris, France.
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  Data: <searchLink fieldCode="JN" term="%228305874%22">Cell biochemistry and function</searchLink> [Cell Biochem Funct] 2026 Jul; Vol. 44 (7), pp. e70265.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Wiley-Blackwell%22">Wiley-Blackwell </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>8305874 <i>Publication Model: </i>Print <i>Cited Medium: </i>Internet <i>ISSN: </i>1099-0844 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2202636484%22">02636484 </searchLink><i>NLM ISO Abbreviation: </i>Cell Biochem Funct <i>Subsets: </i>MEDLINE
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  Data: <i>Publication</i>: Oxford, England : Wiley-Blackwell<br /><i>Original Publication</i>: Guildford, Surrey : Butterworth Scientific Ltd., c1983-
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  Data: <searchLink fieldCode="MM" term="%22ADAM+Proteins%22">ADAM Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22ADAM+Proteins+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22ADAM+Proteins%22">ADAM Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22ADAM+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22ADAM+Proteins%22">ADAM Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22ADAM+Proteins+deficiency%22">deficiency</searchLink> <br /><searchLink fieldCode="MM" term="%22Infertility%2C+Male%22">Infertility, Male*</searchLink>/<searchLink fieldCode="MM" term="%22Infertility%2C+Male+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Infertility%2C+Male%22">Infertility, Male*</searchLink>/<searchLink fieldCode="MM" term="%22Infertility%2C+Male+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Fertilization%22">Fertilization*</searchLink> <br /><searchLink fieldCode="MM" term="%22Fertility%22">Fertility*</searchLink><br /><searchLink fieldCode="MH" term="%22Spermatozoa%22">Spermatozoa</searchLink>/<searchLink fieldCode="MH" term="%22Spermatozoa+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Animals%22">Animals</searchLink> ; <searchLink fieldCode="MH" term="%22Male%22">Male</searchLink> ; <searchLink fieldCode="MH" term="%22Mice%22">Mice</searchLink> ; <searchLink fieldCode="MH" term="%22Mice%2C+Knockout%22">Mice, Knockout</searchLink> ; <searchLink fieldCode="MH" term="%22Female%22">Female</searchLink> ; <searchLink fieldCode="MH" term="%22Fertilization+in+Vitro%22">Fertilization in Vitro</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: A mutation of the ADAM20 gene was described in an infertile patient whose spermatozoa were observed accumulating in the perivitelline space of oocytes. To decipher its role in the fertilization process, we produced a mouse model knock-out (KO) for the Adam20 gene. Surprisingly, Adam20-KO males showed an in vivo fertility similar to their wild-type littermates and had normal sperm counts and morphology. However, they presented a reduced fertility in in vitro fertilization assays. To explore the hypothesis that the two flanking genes Adam25 and Adam39 could compensate the lack of Adam20 given their very high homology, we produced a triple KO deleting these three neighbor genes simultaneously. The phenotype was strictly identical to that of the single gene deletion. Therefore, ADAM20, ADAM25, and ADAM39 are not essential proteins for fertilization in mice but they seem to participate modestly to the process. Adam20-KO males are fertile in vivo but have a reduced fertility in vitro. Males deleted for three neighbor and very homologous genes (Adam20, Adam25, and Adam39) have the same phenotype as the simple Adam20-KO. These genes are dispensable for normal fertility but contribute modestly to fertilization.<br /> (© 2026 John Wiley & Sons Ltd.)
– Name: Ref
  Label: References
  Group: RefInfo
  Data: M. Chalbi, V. Barraud‐Lange, B. Ravaux, et al., “Binding of Sperm Protein Izumo1 and Its Egg Receptor Juno Drives Cd9 Accumulation in the Intercellular Contact Area Prior to Fusion During Mammalian Fertilization,” Development 141 (2014): 3732–3739, https://doi.org/10.1242/dev.111534.<br />A. Jégou, A. Ziyyat, V. Barraud‐Lange, et al., “CD9 Tetraspanin Generates Fusion Competent Sites on the Egg Membrane for Mammalian Fertilization,” Proceedings of the National Academy of Sciences 108 (2011): 10946–10951, https://doi.org/10.1073/pnas.1017400108.<br />F. Le Naour, E. Rubinstein, C. Jasmin, M. Prenant, and C. Boucheix, “Severely Reduced Female Fertility in CD9‐Deficient Mice,” Science 287 (2000): 319–321, https://doi.org/10.1126/science.287.5451.319.<br />K. Miyado, G. Yamada, S. Yamada, et al., “Requirement of CD9 on the Egg Plasma Membrane for Fertilization,” Science 287 (2000): 321–324.<br />K. Kaji, S. Oda, T. Shikano, et al., “The Gamete Fusion Process Is Defective in Eggs of Cd9‐Deficient Mice,” Nature Genetics 24 (2000): 279–282, https://doi.org/10.1038/73502.<br />E. Bianchi, B. Doe, D. Goulding, and G. J. Wright, “Juno Is the Egg Izumo Receptor and Is Essential for Mammalian Fertilization,” Nature 508 (2014): 483–487, https://doi.org/10.1038/nature13203.<br />N. Inoue, M. Ikawa, A. Isotani, and M. Okabe, “The Immunoglobulin Superfamily Protein Izumo Is Required for Sperm to Fuse With Eggs,” Nature 434 (2005): 234–238, https://doi.org/10.1038/nature03362.<br />B. Ravaux, S. Favier, E. Perez, and C. Gourier, “Egg CD9 Protein Tides Correlated With Sperm Oscillations Tune the Gamete Fusion Ability in Mammal,” Journal of Molecular Cell Biology 10 (2018): 494–502, https://doi.org/10.1093/jmcb/mjy005.<br />N. Inoue, D. Hamada, H. Kamikubo, et al., “Molecular Dissection of IZUMO1, a Sperm Protein Essential for Sperm‐Egg Fusion,” Development 140 (2013): 3221–3229, https://doi.org/10.1242/dev.094854.<br />S. Barbaux, C. Ialy‐Radio, M. Chalbi, et al., “Sperm SPACA6 Protein Is Required for Mammalian Sperm‐Egg Adhesion/Fusion,” Scientific Reports 10 (2020): 5335, https://doi.org/10.1038/s41598-020-62091-y.<br />Y. Fujihara, Y. Lu, T. Noda, et al., “Spermatozoa Lacking Fertilization Influencing Membrane Protein (FIMP) Fail to Fuse With Oocytes in Mice,” Proceedings of the National Academy of Sciences 117 (2020): 9393–9400, https://doi.org/10.1073/pnas.1917060117.<br />M. Hernandez‐Falco, P. Saez‐Espinosa, A. Lopez‐Botella, J. Aizpurua, and M. J. Gomez‐Torres, “The Role of Sperm Proteins IZUMO1 and TMEM95 in Mammalian Fertilization: A Systematic Review,” International Journal of Molecular Sciences 23 (2022): 3929, https://doi.org/10.3390/ijms23073929.<br />N. Inoue, Y. Hagihara, and I. Wada, “Evolutionarily Conserved Sperm Factors, DCST1 and DCST2, Are Required for Gamete Fusion,” eLife 10 (2021): e66313, https://doi.org/10.7554/eLife.66313.<br />I. Lamas‐Toranzo, J. G. Hamze, E. Bianchi, et al., “TMEM95 Is a Sperm Membrane Protein Essential for Mammalian Fertilization,” eLife 9 (2020): e53913, https://doi.org/10.7554/eLife.53913.<br />T. Noda, A. Blaha, Y. Fujihara, et al., “Sperm Membrane Proteins DCST1 and DCST2 Are Required for Sperm‐Egg Interaction in Mice and Fish,” Communications Biology 5 (2022): 332, https://doi.org/10.1038/s42003-022-03289-w.<br />T. Noda, Y. Lu, Y. Fujihara, et al., “Sperm Proteins SOF1, TMEM95, and SPACA6 Are Required for Sperm‐Oocyte Fusion in Mice,” Proceedings of the National Academy of Sciences 117 (2020): 11493–11502, https://doi.org/10.1073/pnas.1922650117.<br />S. Tang, Y. Lu, W. M. Skinner, et al., “Human Sperm TMEM95 Binds Eggs and Facilitates Membrane Fusion,” Proceedings of the National Academy of Sciences of the United States of America 119 (2022): e2207805119, https://doi.org/10.1073/pnas.2207805119.<br />V. E. Deneke, A. Blaha, Y. Lu, et al., “A Conserved Fertilization Complex Bridges Sperm and Egg in Vertebrates,” Cell 187 (2024): 7066–7078.e22, https://doi.org/10.1016/j.cell.2024.09.035.<br />D. Lorenzetti, C. Poirier, M. Zhao, P. A. Overbeek, W. Harrison, and C. E. Bishop, “A Transgenic Insertion on Mouse Chromosome 17 Inactivates a Novel Immunoglobulin Superfamily Gene Potentially Involved in Sperm‐Egg Fusion,” Mammalian Genome 25 (2014): 141–148, https://doi.org/10.1007/s00335-013-9491-x.<br />C. Jean, F. Haghighirad, Y. Zhu, et al., “JUNO, the Receptor of Sperm IZUMO1, Is Expressed by the Human Oocyte and Is Essential for Human Fertilisation,” Human Reproduction 34 (2019): 118–126, https://doi.org/10.1093/humrep/dey340.<br />A. Ziyyat, E. 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  Data: Institut National de la Santé et de la Recherche Médicale; Centre National de la Recherche Scientifique; Université Paris Cité; ANR-21-CE13-0032-01 Agence Nationale de la Recherche; CIHR; PJT-203841 Canada CAPMC CIHR; NFRFE-2019-00230 New frontiers in research fund
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  Data: <i>Keywords: </i>fertility; fertilization; infertility; knock‐out; male; mouse; sperm; testis
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  Data: EC 3.4.24.- (ADAM Proteins)
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  Data: <i>Date Created: </i>20260715 <i>Date Completed: </i>20260715 <i>Latest Revision: </i>20260726
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        Value: 10.1002/cbf.70265
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        Text: English
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        StartPage: e70265
    Subjects:
      – SubjectFull: Spermatozoa metabolism
        Type: general
      – SubjectFull: Animals
        Type: general
      – SubjectFull: Male
        Type: general
      – SubjectFull: Mice
        Type: general
      – SubjectFull: Mice, Knockout
        Type: general
      – SubjectFull: Female
        Type: general
      – SubjectFull: Fertilization in Vitro
        Type: general
      – SubjectFull: ADAM Proteins genetics
        Type: general
      – SubjectFull: ADAM Proteins metabolism
        Type: general
      – SubjectFull: ADAM Proteins deficiency
        Type: general
      – SubjectFull: Infertility, Male genetics
        Type: general
      – SubjectFull: Infertility, Male metabolism
        Type: general
      – SubjectFull: Fertilization
        Type: general
      – SubjectFull: Fertility
        Type: general
    Titles:
      – TitleFull: ADAM20 Participates Modestly to Fertilization as Its Absence Leads to In Vitro Hypofertility in Mouse.
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            – D: 01
              M: 07
              Text: 2026 Jul
              Type: published
              Y: 2026
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            – Type: issn-electronic
              Value: 1099-0844
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            – TitleFull: Cell biochemistry and function
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