Skip to main content
Erschienen in: Anatomical Science International 2/2016

01.03.2016 | Review Article

Acrosome markers of human sperm

verfasst von: Chizuru Ito, Kiyotaka Toshimori

Erschienen in: Anatomical Science International | Ausgabe 2/2016

Einloggen, um Zugang zu erhalten

Abstract

Molecular biomarkers that can assess sperm acrosome status are very useful for evaluating sperm quality in the field of assisted reproductive technology. In this review, we introduce and discuss the localization and function of acrosomal proteins that have been well studied. Journal databases were searched using keywords, including “human acrosome”, “localization”, “fertilization-related protein”, “acrosomal membrane”, “acrosomal matrix”, “acrosome reaction”, “knockout mouse”, and “acrosome marker”.
Literatur
Zurück zum Zitat Adekunle AO, Arboleda CE, Zervos PH, Gerton GL, Teuscher C (1987) Purification and initial characterization of guinea pig testicular acrosin. Biol Reprod 37:201–210PubMedCrossRef Adekunle AO, Arboleda CE, Zervos PH, Gerton GL, Teuscher C (1987) Purification and initial characterization of guinea pig testicular acrosin. Biol Reprod 37:201–210PubMedCrossRef
Zurück zum Zitat Adham IM, Nayernia K, Engel W (1997) Spermatozoa lacking acrosin protein show delayed fertilization. Mol Reprod Dev 46:370–376PubMedCrossRef Adham IM, Nayernia K, Engel W (1997) Spermatozoa lacking acrosin protein show delayed fertilization. Mol Reprod Dev 46:370–376PubMedCrossRef
Zurück zum Zitat Anakwe OO, Gerton GL (1990) Acrosome biogenesis begins during meiosis: evidence from the synthesis and distribution of an acrosomal glycoprotein, acrogranin, during guinea pig spermatogenesis. Biol Reprod 42:317–328PubMedCrossRef Anakwe OO, Gerton GL (1990) Acrosome biogenesis begins during meiosis: evidence from the synthesis and distribution of an acrosomal glycoprotein, acrogranin, during guinea pig spermatogenesis. Biol Reprod 42:317–328PubMedCrossRef
Zurück zum Zitat Anderson DJ, Michaelson JS, Johnson PM (1989) Trophoblast/leukocyte-common antigen is expressed by human testicular germ cells and appears on the surface of acrosome-reacted sperm. Biol Reprod 41:285–293PubMedCrossRef Anderson DJ, Michaelson JS, Johnson PM (1989) Trophoblast/leukocyte-common antigen is expressed by human testicular germ cells and appears on the surface of acrosome-reacted sperm. Biol Reprod 41:285–293PubMedCrossRef
Zurück zum Zitat Baba T, Kashiwabara S, Watanabe K et al (1989) Activation and maturation mechanisms of boar acrosin zymogen based on the deduced primary structure. J Biol Chem 264:11920–11927PubMed Baba T, Kashiwabara S, Watanabe K et al (1989) Activation and maturation mechanisms of boar acrosin zymogen based on the deduced primary structure. J Biol Chem 264:11920–11927PubMed
Zurück zum Zitat Baba T, Azuma S, Kashiwabara S, Toyoda Y (1994) Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J Biol Chem 269:31845–31849PubMed Baba T, Azuma S, Kashiwabara S, Toyoda Y (1994) Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization. J Biol Chem 269:31845–31849PubMed
Zurück zum Zitat Baba D, Kashiwabara S, Honda A et al (2002) Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg. J Biol Chem 277:30310–30314PubMedCrossRef Baba D, Kashiwabara S, Honda A et al (2002) Mouse sperm lacking cell surface hyaluronidase PH-20 can pass through the layer of cumulus cells and fertilize the egg. J Biol Chem 277:30310–30314PubMedCrossRef
Zurück zum Zitat Bi M, Hickox JR, Winfrey VP, Olson GE, Hardy DM (2003) Processing, localization and binding activity of zonadhesin suggest a function in sperm adhesion to the zona pellucida during exocytosis of the acrosome. Biochem J 375:477–488PubMedCentralPubMedCrossRef Bi M, Hickox JR, Winfrey VP, Olson GE, Hardy DM (2003) Processing, localization and binding activity of zonadhesin suggest a function in sperm adhesion to the zona pellucida during exocytosis of the acrosome. Biochem J 375:477–488PubMedCentralPubMedCrossRef
Zurück zum Zitat Bleil JD, Wassarman PM (1990) Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking. Proc Natl Acad Sci USA 87:5563–5567PubMedCentralPubMedCrossRef Bleil JD, Wassarman PM (1990) Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking. Proc Natl Acad Sci USA 87:5563–5567PubMedCentralPubMedCrossRef
Zurück zum Zitat Brandon CI Jr, Srivastava PN, Heusner GL, Fayrer-Hosken RA (1997) Extraction and quantification of acrosin, beta-N-acetylglucosaminidase, and arylsulfatase-A from equine ejaculated spermatozoa. J Exp Zool 279:301–308PubMedCrossRef Brandon CI Jr, Srivastava PN, Heusner GL, Fayrer-Hosken RA (1997) Extraction and quantification of acrosin, beta-N-acetylglucosaminidase, and arylsulfatase-A from equine ejaculated spermatozoa. J Exp Zool 279:301–308PubMedCrossRef
Zurück zum Zitat Busso D, Cohen DJ, Hayashi M, Kasahara M, Cuasnicu PS (2005) Human testicular protein TPX1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction. Mol Hum Reprod 11:299–305PubMedCrossRef Busso D, Cohen DJ, Hayashi M, Kasahara M, Cuasnicu PS (2005) Human testicular protein TPX1/CRISP-2: localization in spermatozoa, fate after capacitation and relevance for gamete interaction. Mol Hum Reprod 11:299–305PubMedCrossRef
Zurück zum Zitat Busso D, Goldweic NM, Hayashi M, Kasahara M, Cuasnicu PS (2007) Evidence for the involvement of testicular protein CRISP2 in mouse sperm–egg fusion. Biol Reprod 76:701–708PubMedCrossRef Busso D, Goldweic NM, Hayashi M, Kasahara M, Cuasnicu PS (2007) Evidence for the involvement of testicular protein CRISP2 in mouse sperm–egg fusion. Biol Reprod 76:701–708PubMedCrossRef
Zurück zum Zitat Chalbi M, Barraud-Lange V, Ravaux B et al (2014) 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 141:3732–3739PubMedCrossRef Chalbi M, Barraud-Lange V, Ravaux B et al (2014) 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 141:3732–3739PubMedCrossRef
Zurück zum Zitat Cheng A, Le T, Palacios M et al (1994) sperm–egg recognition in the mouse: characterization of sp56, a sperm protein having specific affinity for ZP3. J Cell Biol 125:867–878PubMedCrossRef Cheng A, Le T, Palacios M et al (1994) sperm–egg recognition in the mouse: characterization of sp56, a sperm protein having specific affinity for ZP3. J Cell Biol 125:867–878PubMedCrossRef
Zurück zum Zitat Dörig RE, Marcil A, Chopra A, Richardson CD (1993) The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 75:295–305PubMedCrossRef Dörig RE, Marcil A, Chopra A, Richardson CD (1993) The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 75:295–305PubMedCrossRef
Zurück zum Zitat Fénichel P, Dohr G, Grivaux C, Cervoni F, Donzeau M, Hsi BL (1990) Localization and characterization of the acrosomal antigen recognized by GB24 on human spermatozoa. Mol Reprod Dev 27:173–178PubMedCrossRef Fénichel P, Dohr G, Grivaux C, Cervoni F, Donzeau M, Hsi BL (1990) Localization and characterization of the acrosomal antigen recognized by GB24 on human spermatozoa. Mol Reprod Dev 27:173–178PubMedCrossRef
Zurück zum Zitat Ferrer M, Xu W, Oko R (2012a) The composition, protein genesis and significance of the inner acrosomal membrane of eutherian sperm. Cell Tissue Res 349:733–748PubMedCrossRef Ferrer M, Xu W, Oko R (2012a) The composition, protein genesis and significance of the inner acrosomal membrane of eutherian sperm. Cell Tissue Res 349:733–748PubMedCrossRef
Zurück zum Zitat Ferrer M, Rodriguez H, Zara L, Yu Y, Xu W, Oko R (2012b) MMP2 and acrosin are major proteinases associated with the inner acrosomal membrane and may cooperate in sperm penetration of the zona pellucida during fertilization. Cell Tissue Res 349:881–895PubMedCentralPubMedCrossRef Ferrer M, Rodriguez H, Zara L, Yu Y, Xu W, Oko R (2012b) MMP2 and acrosin are major proteinases associated with the inner acrosomal membrane and may cooperate in sperm penetration of the zona pellucida during fertilization. Cell Tissue Res 349:881–895PubMedCentralPubMedCrossRef
Zurück zum Zitat Florman HM, Fissore RA (2014) Fertilization in mammals. In: Plant TM, Zeleznik A (eds) Knobil and Neill’s physiology of reproduction, vol 1, 4th edn. Acaemic Press, New York, pp 149–196 Florman HM, Fissore RA (2014) Fertilization in mammals. In: Plant TM, Zeleznik A (eds) Knobil and Neill’s physiology of reproduction, vol 1, 4th edn. Acaemic Press, New York, pp 149–196
Zurück zum Zitat Forsbach A, Heinlein UA (1998) Intratesticular distribution of cyritestin, a protein involved in gamete interaction. J Exp Biol 201:861–867PubMed Forsbach A, Heinlein UA (1998) Intratesticular distribution of cyritestin, a protein involved in gamete interaction. J Exp Biol 201:861–867PubMed
Zurück zum Zitat Foster JA, Klotz KL, Flickinger CJ et al (1994) Human SP-10: acrosomal distribution, processing, and fate after the acrosome reaction. Biol Reprod 51:1222–1231PubMedCrossRef Foster JA, Klotz KL, Flickinger CJ et al (1994) Human SP-10: acrosomal distribution, processing, and fate after the acrosome reaction. Biol Reprod 51:1222–1231PubMedCrossRef
Zurück zum Zitat Foster JA, Friday BB, Maulit MT et al (1997) AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins. J Biol Chem 272:12714–12722PubMedCrossRef Foster JA, Friday BB, Maulit MT et al (1997) AM67, a secretory component of the guinea pig sperm acrosomal matrix, is related to mouse sperm protein sp56 and the complement component 4-binding proteins. J Biol Chem 272:12714–12722PubMedCrossRef
Zurück zum Zitat Freemerman AJ, Wright RM, Flickinger CJ, Herr JC (1993) Cloning and sequencing of baboon and cynomolgus monkey intra-acrosomal protein SP-10: homology with human SP-10 and a mouse sperm antigen (MSA-63). Mol Reprod Dev 34:140–148PubMedCrossRef Freemerman AJ, Wright RM, Flickinger CJ, Herr JC (1993) Cloning and sequencing of baboon and cynomolgus monkey intra-acrosomal protein SP-10: homology with human SP-10 and a mouse sperm antigen (MSA-63). Mol Reprod Dev 34:140–148PubMedCrossRef
Zurück zum Zitat Fujihara Y, Murakami M, Inoue N et al (2010) Sperm equatorial segment protein 1, SPESP1, is required for fully fertile sperm in mouse. J Cell Sci 123:1531–1536PubMedCrossRef Fujihara Y, Murakami M, Inoue N et al (2010) Sperm equatorial segment protein 1, SPESP1, is required for fully fertile sperm in mouse. J Cell Sci 123:1531–1536PubMedCrossRef
Zurück zum Zitat Fujihara Y, Satouh Y, Inoue N, Isotani A, Ikawa M, Okabe M (2012) SPACA1-deficient male mice are infertile with abnormally shaped sperm heads reminiscent of globozoospermia. Development 139:3583–3589PubMedCrossRef Fujihara Y, Satouh Y, Inoue N, Isotani A, Ikawa M, Okabe M (2012) SPACA1-deficient male mice are infertile with abnormally shaped sperm heads reminiscent of globozoospermia. Development 139:3583–3589PubMedCrossRef
Zurück zum Zitat Fujihara Y, Okabe M, Ikawa M (2014) GPI-anchored protein complex, LY6K/TEX101, is required for sperm migration into the oviduct and male fertility in mice. Biol Reprod 90:1–6CrossRef Fujihara Y, Okabe M, Ikawa M (2014) GPI-anchored protein complex, LY6K/TEX101, is required for sperm migration into the oviduct and male fertility in mice. Biol Reprod 90:1–6CrossRef
Zurück zum Zitat Gao Z, Garbers DL (1998) Species diversity in the structure of zonadhesin, a sperm-specific membrane protein containing multiple cell adhesion molecule-like domains. J Biol Chem 273:3415–3421PubMedCrossRef Gao Z, Garbers DL (1998) Species diversity in the structure of zonadhesin, a sperm-specific membrane protein containing multiple cell adhesion molecule-like domains. J Biol Chem 273:3415–3421PubMedCrossRef
Zurück zum Zitat Gao Z, Harumi T, Garbers DL (1997) Chromosome localization of the mouse zonadhesin gene and the human zonadhesin gene (ZAN). Genomics 41:119–122PubMedCrossRef Gao Z, Harumi T, Garbers DL (1997) Chromosome localization of the mouse zonadhesin gene and the human zonadhesin gene (ZAN). Genomics 41:119–122PubMedCrossRef
Zurück zum Zitat Gibbs GM, Scanlon MJ, Swarbrick J et al (2006) The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signaling. J Biol Chem 281:4156–4163PubMedCrossRef Gibbs GM, Scanlon MJ, Swarbrick J et al (2006) The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signaling. J Biol Chem 281:4156–4163PubMedCrossRef
Zurück zum Zitat Greenstone HL, Santoro F, Lusso P, Berger EA (2002) Human herpesvirus 6 and measles virus employ distinct CD46 domains for receptor function. J Biol Chem 277:39112–39118PubMedCrossRef Greenstone HL, Santoro F, Lusso P, Berger EA (2002) Human herpesvirus 6 and measles virus employ distinct CD46 domains for receptor function. J Biol Chem 277:39112–39118PubMedCrossRef
Zurück zum Zitat Griffiths GS, Galileo DS, Reese K, Martin-Deleon PA (2008a) Investigating the role of murine epididymosomes and uterosomes in GPI-linked protein transfer to sperm using SPAM1 as a model. Mol Reprod Dev 75:1627–1636PubMedCrossRef Griffiths GS, Galileo DS, Reese K, Martin-Deleon PA (2008a) Investigating the role of murine epididymosomes and uterosomes in GPI-linked protein transfer to sperm using SPAM1 as a model. Mol Reprod Dev 75:1627–1636PubMedCrossRef
Zurück zum Zitat Griffiths GS, Miller KA, Galileo DS, Martin-DeLeon PA (2008b) Murine SPAM1 is secreted by the estrous uterus and oviduct in a form that can bind to sperm during capacitation: acquisition enhances hyaluronic acid-binding ability and cumulus dispersal efficiency. Reproduction 135:293–301PubMedCrossRef Griffiths GS, Miller KA, Galileo DS, Martin-DeLeon PA (2008b) Murine SPAM1 is secreted by the estrous uterus and oviduct in a form that can bind to sperm during capacitation: acquisition enhances hyaluronic acid-binding ability and cumulus dispersal efficiency. Reproduction 135:293–301PubMedCrossRef
Zurück zum Zitat Hamatani T, Tanabe K, Kamei K, Sakai N, Yamamoto Y, Yoshimura Y (2000) A monoclonal antibody to human SP-10 inhibits in vitro the binding of human sperm to hamster oolemma but not to human Zona pellucida. Biol Reprod 62:1201–1208PubMedCrossRef Hamatani T, Tanabe K, Kamei K, Sakai N, Yamamoto Y, Yoshimura Y (2000) A monoclonal antibody to human SP-10 inhibits in vitro the binding of human sperm to hamster oolemma but not to human Zona pellucida. Biol Reprod 62:1201–1208PubMedCrossRef
Zurück zum Zitat Hao Z, Wolkowicz MJ, Shetty J et al (2002) SAMP32, a testis-specific, isoantigenic sperm acrosomal membrane-associated protein. Biol Reprod 66:735–744PubMedCrossRef Hao Z, Wolkowicz MJ, Shetty J et al (2002) SAMP32, a testis-specific, isoantigenic sperm acrosomal membrane-associated protein. Biol Reprod 66:735–744PubMedCrossRef
Zurück zum Zitat Hao J, Chen M, Ji S et al (2014) Equatorin is not essential for acrosome biogenesis but is required for the acrosome reaction. Biochem Biophys Res Commun 444:537–542PubMedCrossRef Hao J, Chen M, Ji S et al (2014) Equatorin is not essential for acrosome biogenesis but is required for the acrosome reaction. Biochem Biophys Res Commun 444:537–542PubMedCrossRef
Zurück zum Zitat Hardy DM, Garbers DL (1994) Species-specific binding of sperm proteins to the extracellular matrix (zona pellucida) of the egg. J Biol Chem 269:19000–19004PubMed Hardy DM, Garbers DL (1994) Species-specific binding of sperm proteins to the extracellular matrix (zona pellucida) of the egg. J Biol Chem 269:19000–19004PubMed
Zurück zum Zitat Hardy DM, Garbers DL (1995) A sperm membrane protein that binds in a species-specific manner to the egg extracellular matrix is homologous to von Willebrand factor. J Biol Chem 270:26025–26028PubMedCrossRef Hardy DM, Garbers DL (1995) A sperm membrane protein that binds in a species-specific manner to the egg extracellular matrix is homologous to von Willebrand factor. J Biol Chem 270:26025–26028PubMedCrossRef
Zurück zum Zitat Hardy DM, Wild GC, Tung KS (1987) Purification and initial characterization of proacrosins from guinea pig testes and epididymal spermatozoa. Biol Reprod 37:189–199PubMedCrossRef Hardy DM, Wild GC, Tung KS (1987) Purification and initial characterization of proacrosins from guinea pig testes and epididymal spermatozoa. Biol Reprod 37:189–199PubMedCrossRef
Zurück zum Zitat Hardy DM, Oda MN, Friend DS, Huang TT Jr (1991) A mechanism for differential release of acrosomal enzymes during the acrosome reaction. Biochem J 275(Pt 3):759–766PubMedCentralPubMedCrossRef Hardy DM, Oda MN, Friend DS, Huang TT Jr (1991) A mechanism for differential release of acrosomal enzymes during the acrosome reaction. Biochem J 275(Pt 3):759–766PubMedCentralPubMedCrossRef
Zurück zum Zitat He XB, Yan YC, Li YP, Koide SS (2003) Cloning of rat sp56, the homologue of mouse sperm ZP3 receptor-sp56. Cell Res 13:121–129PubMedCrossRef He XB, Yan YC, Li YP, Koide SS (2003) Cloning of rat sp56, the homologue of mouse sperm ZP3 receptor-sp56. Cell Res 13:121–129PubMedCrossRef
Zurück zum Zitat Herlyn H, Zischler H (2008) The molecular evolution of sperm zonadhesin. Int J Dev Biol 52:781–790PubMedCrossRef Herlyn H, Zischler H (2008) The molecular evolution of sperm zonadhesin. Int J Dev Biol 52:781–790PubMedCrossRef
Zurück zum Zitat Herr JC, Flickinger CJ, Homyk M, Klotz K, John E (1990a) Biochemical and morphological characterization of the intra-acrosomal antigen SP-10 from human sperm. Biol Reprod 42:181–193PubMedCrossRef Herr JC, Flickinger CJ, Homyk M, Klotz K, John E (1990a) Biochemical and morphological characterization of the intra-acrosomal antigen SP-10 from human sperm. Biol Reprod 42:181–193PubMedCrossRef
Zurück zum Zitat Herr JC, Wright RM, John E, Foster J, Kays T, Flickinger CJ (1990b) Identification of human acrosomal antigen SP-10 in primates and pigs. Biol Reprod 42:377–382PubMedCrossRef Herr JC, Wright RM, John E, Foster J, Kays T, Flickinger CJ (1990b) Identification of human acrosomal antigen SP-10 in primates and pigs. Biol Reprod 42:377–382PubMedCrossRef
Zurück zum Zitat Herrero MB, Mandal A, Digilio LC, Coonrod SA, Maier B, Herr JC (2005) Mouse SLLP1, a sperm lysozyme-like protein involved in sperm–egg binding and fertilization. Dev Biol 284:126–142PubMedCrossRef Herrero MB, Mandal A, Digilio LC, Coonrod SA, Maier B, Herr JC (2005) Mouse SLLP1, a sperm lysozyme-like protein involved in sperm–egg binding and fertilization. Dev Biol 284:126–142PubMedCrossRef
Zurück zum Zitat Honda A, Siruntawineti J, Baba T (2002) Role of acrosomal matrix proteases in sperm–zona pellucida interactions. Hum Reprod Update 8:405–412PubMedCrossRef Honda A, Siruntawineti J, Baba T (2002) Role of acrosomal matrix proteases in sperm–zona pellucida interactions. Hum Reprod Update 8:405–412PubMedCrossRef
Zurück zum Zitat Hsu YC, Perin MS (1995) Human neuronal pentraxin II (NPTX2): conservation, genomic structure, and chromosomal localization. Genomics 28:220–227PubMedCrossRef Hsu YC, Perin MS (1995) Human neuronal pentraxin II (NPTX2): conservation, genomic structure, and chromosomal localization. Genomics 28:220–227PubMedCrossRef
Zurück zum Zitat Inoue N, Ikawa M, Nakanishi T et al (2003) Disruption of mouse CD46 causes an accelerated spontaneous acrosome reaction in sperm. Mol Cell Biol 23:2614–2622PubMedCentralPubMedCrossRef Inoue N, Ikawa M, Nakanishi T et al (2003) Disruption of mouse CD46 causes an accelerated spontaneous acrosome reaction in sperm. Mol Cell Biol 23:2614–2622PubMedCentralPubMedCrossRef
Zurück zum Zitat Inoue N, Ikawa M, Isotani A, Okabe M (2005) The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 434:234–238PubMedCrossRef Inoue N, Ikawa M, Isotani A, Okabe M (2005) The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 434:234–238PubMedCrossRef
Zurück zum Zitat Inoue N, Hamada D, Kamikubo H et al (2013) Molecular dissection of IZUMO1, a sperm protein essential for sperm–egg fusion. Development 140:3221–3229PubMedCrossRef Inoue N, Hamada D, Kamikubo H et al (2013) Molecular dissection of IZUMO1, a sperm protein essential for sperm–egg fusion. Development 140:3221–3229PubMedCrossRef
Zurück zum Zitat Ito M, Yamatoya K, Yoshida K et al (2010) Appearance of an oocyte activation-related substance during spermatogenesis in mouse and human. Hum Reprod 25:2734–2744PubMedCrossRef Ito M, Yamatoya K, Yoshida K et al (2010) Appearance of an oocyte activation-related substance during spermatogenesis in mouse and human. Hum Reprod 25:2734–2744PubMedCrossRef
Zurück zum Zitat Ito C, Yamatoya K, Yoshida K et al (2013) Integration of the mouse sperm fertilization-related protein equatorin into the acrosome during spermatogenesis as revealed by super-resolution and immunoelectron microscopy. Cell Tissue Res 352:739–750PubMedCrossRef Ito C, Yamatoya K, Yoshida K et al (2013) Integration of the mouse sperm fertilization-related protein equatorin into the acrosome during spermatogenesis as revealed by super-resolution and immunoelectron microscopy. Cell Tissue Res 352:739–750PubMedCrossRef
Zurück zum Zitat Ito C, Yamatoya K, Toshimori K (2015) Analysis of the complexity of the sperm acrosomal membrane by super-resolution stimulated emission depletion microscopy compared with transmission electron microscopy. Microscopy 64:279–287PubMedCrossRef Ito C, Yamatoya K, Toshimori K (2015) Analysis of the complexity of the sperm acrosomal membrane by super-resolution stimulated emission depletion microscopy compared with transmission electron microscopy. Microscopy 64:279–287PubMedCrossRef
Zurück zum Zitat Jin M, Fujiwara E, Kakiuchi Y et al (2011) Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization. Proc Natl Acad Sci USA 108:4892–4896PubMedCentralPubMedCrossRef Jin M, Fujiwara E, Kakiuchi Y et al (2011) Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization. Proc Natl Acad Sci USA 108:4892–4896PubMedCentralPubMedCrossRef
Zurück zum Zitat Kawano N, Kang W, Yamashita M et al (2010) Mice lacking two sperm serine proteases, ACR and PRSS21, are subfertile, but the mutant sperm are infertile in vitro. Biol Reprod 83:359–369PubMedCrossRef Kawano N, Kang W, Yamashita M et al (2010) Mice lacking two sperm serine proteases, ACR and PRSS21, are subfertile, but the mutant sperm are infertile in vitro. Biol Reprod 83:359–369PubMedCrossRef
Zurück zum Zitat Kemper C, Chan AC, Green JM et al (2003) Activation of human CD4+ cells with CD3 and CD46 induces a T-regulatory cell 1 phenotype. Nature 421:388–392PubMedCrossRef Kemper C, Chan AC, Green JM et al (2003) Activation of human CD4+ cells with CD3 and CD46 induces a T-regulatory cell 1 phenotype. Nature 421:388–392PubMedCrossRef
Zurück zum Zitat Kierszenbaum AL, Tres LL (2004) The acrosome–acroplaxome–manchette complex and the shaping of the spermatid head. Arch Histol Cytol 67:271–284PubMedCrossRef Kierszenbaum AL, Tres LL (2004) The acrosome–acroplaxome–manchette complex and the shaping of the spermatid head. Arch Histol Cytol 67:271–284PubMedCrossRef
Zurück zum Zitat Kim KS, Gerton GL (2003) Differential release of soluble and matrix components: evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm. Dev Biol 264:141–152PubMedCrossRef Kim KS, Gerton GL (2003) Differential release of soluble and matrix components: evidence for intermediate states of secretion during spontaneous acrosomal exocytosis in mouse sperm. Dev Biol 264:141–152PubMedCrossRef
Zurück zum Zitat Kim KS, Cha MC, Gerton GL (2001) Mouse sperm protein sp56 is a component of the acrosomal matrix. Biol Reprod 64:36–43PubMedCrossRef Kim KS, Cha MC, Gerton GL (2001) Mouse sperm protein sp56 is a component of the acrosomal matrix. Biol Reprod 64:36–43PubMedCrossRef
Zurück zum Zitat Kim E, Nishimura H, Iwase S, Yamagata K, Kashiwabara S, Baba T (2004) Synthesis, processing, and subcellular localization of mouse ADAM3 during spermatogenesis and epididymal sperm transport. J Reprod Dev 50:571–578PubMedCrossRef Kim E, Nishimura H, Iwase S, Yamagata K, Kashiwabara S, Baba T (2004) Synthesis, processing, and subcellular localization of mouse ADAM3 during spermatogenesis and epididymal sperm transport. J Reprod Dev 50:571–578PubMedCrossRef
Zurück zum Zitat Kim KS, Foster JA, Kvasnicka KW, Gerton GL (2011) Transitional states of acrosomal exocytosis and proteolytic processing of the acrosomal matrix in guinea pig sperm. Mol Reprod Dev 78:930–941PubMedCentralPubMedCrossRef Kim KS, Foster JA, Kvasnicka KW, Gerton GL (2011) Transitional states of acrosomal exocytosis and proteolytic processing of the acrosomal matrix in guinea pig sperm. Mol Reprod Dev 78:930–941PubMedCentralPubMedCrossRef
Zurück zum Zitat Klemm U, Muller-Esterl W, Engel W (1991) Acrosin, the peculiar sperm-specific serine protease. Hum Genet 87:635–641PubMedCrossRef Klemm U, Muller-Esterl W, Engel W (1991) Acrosin, the peculiar sperm-specific serine protease. Hum Genet 87:635–641PubMedCrossRef
Zurück zum Zitat Kurth BE, Klotz K, Flickinger CJ, Herr JC (1991) Localization of sperm antigen SP-10 during the six stages of the cycle of the seminiferous epithelium in man. Biol Reprod 44:814–821PubMedCrossRef Kurth BE, Klotz K, Flickinger CJ, Herr JC (1991) Localization of sperm antigen SP-10 during the six stages of the cycle of the seminiferous epithelium in man. Biol Reprod 44:814–821PubMedCrossRef
Zurück zum Zitat Lea IA, Sivashanmugam P, O’Rand MG (2001) Zonadhesin: characterization, localization, and zona pellucida binding. Biol Reprod 65:1691–1700PubMedCrossRef Lea IA, Sivashanmugam P, O’Rand MG (2001) Zonadhesin: characterization, localization, and zona pellucida binding. Biol Reprod 65:1691–1700PubMedCrossRef
Zurück zum Zitat Lin YN, Roy A, Yan W, Burns KH, Matzuk MM (2007) Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis. Mol Cell Biol 27:6794–6805PubMedCentralPubMedCrossRef Lin YN, Roy A, Yan W, Burns KH, Matzuk MM (2007) Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis. Mol Cell Biol 27:6794–6805PubMedCentralPubMedCrossRef
Zurück zum Zitat Linder B, Bammer S, Heinlein UA (1995) Delayed translation and posttranslational processing of cyritestin, an integral transmembrane protein of the mouse acrosome. Exp Cell Res 221:66–72PubMedCrossRef Linder B, Bammer S, Heinlein UA (1995) Delayed translation and posttranslational processing of cyritestin, an integral transmembrane protein of the mouse acrosome. Exp Cell Res 221:66–72PubMedCrossRef
Zurück zum Zitat Liu MS, Aebersold R, Fann CH, Lee CY (1992) Molecular and developmental studies of a sperm acrosome antigen recognized by HS-63 monoclonal antibody. Biol Reprod 46:937–948PubMedCrossRef Liu MS, Aebersold R, Fann CH, Lee CY (1992) Molecular and developmental studies of a sperm acrosome antigen recognized by HS-63 monoclonal antibody. Biol Reprod 46:937–948PubMedCrossRef
Zurück zum Zitat Maeda T, Sakashita M, Ohba Y, Nakanishi Y (1998) Molecular cloning of the rat Tpx-1 responsible for the interaction between spermatogenic and sertoli cells. Biochem Biophys Res Commun 248:140–146PubMedCrossRef Maeda T, Sakashita M, Ohba Y, Nakanishi Y (1998) Molecular cloning of the rat Tpx-1 responsible for the interaction between spermatogenic and sertoli cells. Biochem Biophys Res Commun 248:140–146PubMedCrossRef
Zurück zum Zitat Maeda T, Nishida J, Nakanishi Y (1999) Expression pattern, subcellular localization and structure–function relationship of rat Tpx-1, a spermatogenic cell adhesion molecule responsible for association with sertoli cells. Dev Growth Differ 41:715–722PubMedCrossRef Maeda T, Nishida J, Nakanishi Y (1999) Expression pattern, subcellular localization and structure–function relationship of rat Tpx-1, a spermatogenic cell adhesion molecule responsible for association with sertoli cells. Dev Growth Differ 41:715–722PubMedCrossRef
Zurück zum Zitat Manandhar G, Toshimori K (2001) Exposure of sperm head equatorin after acrosome reaction and its fate after fertilization in mice. Biol Reprod 65:1425–1436PubMedCrossRef Manandhar G, Toshimori K (2001) Exposure of sperm head equatorin after acrosome reaction and its fate after fertilization in mice. Biol Reprod 65:1425–1436PubMedCrossRef
Zurück zum Zitat Mandal A, Klotz KL, Shetty J et al (2003) SLLP1, a unique, intra-acrosomal, non-bacteriolytic, c lysozyme-like protein of human spermatozoa. Biol Reprod 68:1525–1537PubMedCrossRef Mandal A, Klotz KL, Shetty J et al (2003) SLLP1, a unique, intra-acrosomal, non-bacteriolytic, c lysozyme-like protein of human spermatozoa. Biol Reprod 68:1525–1537PubMedCrossRef
Zurück zum Zitat Marie JC, Astier AL, Rivailler P, Rabourdin-Combe C, Wild TF, Horvat B (2002) Linking innate and acquired immunity: divergent role of CD46 cytoplasmic domains in T cell induced inflammation. Nat Immunol 3:659–666PubMed Marie JC, Astier AL, Rivailler P, Rabourdin-Combe C, Wild TF, Horvat B (2002) Linking innate and acquired immunity: divergent role of CD46 cytoplasmic domains in T cell induced inflammation. Nat Immunol 3:659–666PubMed
Zurück zum Zitat Mizuno M, Harris CL, Johnson PM, Morgan BP (2004) Rat membrane cofactor protein (MCP; CD46) is expressed only in the acrosome of developing and mature spermatozoa and mediates binding to immobilized activated C3. Biol Reprod 71:1374–1383PubMedCrossRef Mizuno M, Harris CL, Johnson PM, Morgan BP (2004) Rat membrane cofactor protein (MCP; CD46) is expressed only in the acrosome of developing and mature spermatozoa and mediates binding to immobilized activated C3. Biol Reprod 71:1374–1383PubMedCrossRef
Zurück zum Zitat Mizuno M, Harris CL, Suzuki N, Matsuo S, Morgan BP (2005) Expression of CD46 in developing rat spermatozoa: ultrastructural localization and utility as a marker of the various stages of the seminiferous tubuli. Biol Reprod 72:908–915PubMedCrossRef Mizuno M, Harris CL, Suzuki N, Matsuo S, Morgan BP (2005) Expression of CD46 in developing rat spermatozoa: ultrastructural localization and utility as a marker of the various stages of the seminiferous tubuli. Biol Reprod 72:908–915PubMedCrossRef
Zurück zum Zitat Mori E, Baba T, Iwamatsu A, Mori T (1993) Purification and characterization of a 38-kDa protein, sp38, with zona pellucida-binding property from porcine epididymal sperm. Biochem Biophys Res Commun 196:196–202PubMedCrossRef Mori E, Baba T, Iwamatsu A, Mori T (1993) Purification and characterization of a 38-kDa protein, sp38, with zona pellucida-binding property from porcine epididymal sperm. Biochem Biophys Res Commun 196:196–202PubMedCrossRef
Zurück zum Zitat Mori E, Kashiwabara S, Baba T, Inagaki Y, Mori T (1995) Amino acid sequences of porcine Sp38 and proacrosin required for binding to the zona pellucida. Dev Biol 168:575–583PubMedCrossRef Mori E, Kashiwabara S, Baba T, Inagaki Y, Mori T (1995) Amino acid sequences of porcine Sp38 and proacrosin required for binding to the zona pellucida. Dev Biol 168:575–583PubMedCrossRef
Zurück zum Zitat Morin G, Lalancette C, Sullivan R, Leclerc P (2005) Identification of the bull sperm p80 protein as a PH-20 ortholog and its modification during the epididymal transit. Mol Reprod Dev 71:523–534PubMedCrossRef Morin G, Lalancette C, Sullivan R, Leclerc P (2005) Identification of the bull sperm p80 protein as a PH-20 ortholog and its modification during the epididymal transit. Mol Reprod Dev 71:523–534PubMedCrossRef
Zurück zum Zitat Morin G, Sullivan R, Laflamme I, Robert C, Leclerc P (2010) SPAM1 isoforms from two tissue origins are differentially localized within ejaculated bull sperm membranes and have different roles during fertilization. Biol Reprod 82:271–281PubMedCrossRef Morin G, Sullivan R, Laflamme I, Robert C, Leclerc P (2010) SPAM1 isoforms from two tissue origins are differentially localized within ejaculated bull sperm membranes and have different roles during fertilization. Biol Reprod 82:271–281PubMedCrossRef
Zurück zum Zitat Muro Y, Buffone MG, Okabe M, Gerton GL (2012) Function of the acrosomal matrix: zona pellucida 3 receptor (ZP3R/sp56) is not essential for mouse fertilization. Biol Reprod 86:1–6PubMedCrossRef Muro Y, Buffone MG, Okabe M, Gerton GL (2012) Function of the acrosomal matrix: zona pellucida 3 receptor (ZP3R/sp56) is not essential for mouse fertilization. Biol Reprod 86:1–6PubMedCrossRef
Zurück zum Zitat Nakanishi T, Ikawa M, Yamada S et al (1999) Real-time observation of acrosomal dispersal from mouse sperm using GFP as a marker protein. FEBS Lett 449:277–283PubMedCrossRef Nakanishi T, Ikawa M, Yamada S et al (1999) Real-time observation of acrosomal dispersal from mouse sperm using GFP as a marker protein. FEBS Lett 449:277–283PubMedCrossRef
Zurück zum Zitat Nayernia K, Adham IM, Shamsadin R, Müller C, Sancken U, Engel W (2002) Proacrosin-deficient mice and zona pellucida modifications in an experimental model of multifactorial infertility. Mol Hum Reprod 8:434–440PubMedCrossRef Nayernia K, Adham IM, Shamsadin R, Müller C, Sancken U, Engel W (2002) Proacrosin-deficient mice and zona pellucida modifications in an experimental model of multifactorial infertility. Mol Hum Reprod 8:434–440PubMedCrossRef
Zurück zum Zitat Nimlamool W, Bean BS, Lowe-Krentz LJ (2013) Human sperm CRISP2 is released from the acrosome during the acrosome reaction and re-associates at the equatorial segment. Mol Reprod Dev 80:488–502PubMed Nimlamool W, Bean BS, Lowe-Krentz LJ (2013) Human sperm CRISP2 is released from the acrosome during the acrosome reaction and re-associates at the equatorial segment. Mol Reprod Dev 80:488–502PubMed
Zurück zum Zitat Nishimura H, Cho C, Branciforte DR, Myles DG, Primakoff P (2001) Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev Biol 233:204–213PubMedCrossRef Nishimura H, Cho C, Branciforte DR, Myles DG, Primakoff P (2001) Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev Biol 233:204–213PubMedCrossRef
Zurück zum Zitat Nishimura H, Gupta S, Myles DG, Primakoff P (2011) Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins. Reproduction 141:437–451PubMedCrossRef Nishimura H, Gupta S, Myles DG, Primakoff P (2011) Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins. Reproduction 141:437–451PubMedCrossRef
Zurück zum Zitat Noland TD, Friday BB, Maulit MT, Gerton GL (1994) The sperm acrosomal matrix contains a novel member of the pentaxin family of calcium-dependent binding proteins. J Biol Chem 269:32607–32614PubMed Noland TD, Friday BB, Maulit MT, Gerton GL (1994) The sperm acrosomal matrix contains a novel member of the pentaxin family of calcium-dependent binding proteins. J Biol Chem 269:32607–32614PubMed
Zurück zum Zitat O’Bryan MK, Loveland KL, Herszfeld D, McFarlane JR, Hearn MT, de Kretser DM (1998) Identification of a rat testis-specific gene encoding a potential rat outer dense fibre protein. Mol Reprod Dev 50:313–322PubMedCrossRef O’Bryan MK, Loveland KL, Herszfeld D, McFarlane JR, Hearn MT, de Kretser DM (1998) Identification of a rat testis-specific gene encoding a potential rat outer dense fibre protein. Mol Reprod Dev 50:313–322PubMedCrossRef
Zurück zum Zitat O’Bryan MK, Sebire K, Meinhardt A et al (2001) Tpx-1 is a component of the outer dense fibers and acrosome of rat spermatozoa. Mol Reprod Dev 58:116–125PubMedCrossRef O’Bryan MK, Sebire K, Meinhardt A et al (2001) Tpx-1 is a component of the outer dense fibers and acrosome of rat spermatozoa. Mol Reprod Dev 58:116–125PubMedCrossRef
Zurück zum Zitat Oh-Oka T, Tanii I, Wakayama T, Yoshinaga K, Watanabe K, Toshimori K (2001) Partial characterization of an intra-acrosomal protein, human acrin1 (MN7). J Androl 22:17–24PubMed Oh-Oka T, Tanii I, Wakayama T, Yoshinaga K, Watanabe K, Toshimori K (2001) Partial characterization of an intra-acrosomal protein, human acrin1 (MN7). J Androl 22:17–24PubMed
Zurück zum Zitat Okabe M, Yagasaki M, Oda H, Matzno S, Kohama Y, Mimura T (1988) Effect of a monoclonal anti-mouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs. J Reprod Immunol 13:211–219PubMedCrossRef Okabe M, Yagasaki M, Oda H, Matzno S, Kohama Y, Mimura T (1988) Effect of a monoclonal anti-mouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs. J Reprod Immunol 13:211–219PubMedCrossRef
Zurück zum Zitat Okada N, Liszewski MK, Atkinson JP, Caparon M (1995) Membrane cofactor protein (CD46) is a keratinocyte receptor for the M protein of the group A streptococcus. Proc Natl Acad Sci USA 92:2489–2493PubMedCentralPubMedCrossRef Okada N, Liszewski MK, Atkinson JP, Caparon M (1995) Membrane cofactor protein (CD46) is a keratinocyte receptor for the M protein of the group A streptococcus. Proc Natl Acad Sci USA 92:2489–2493PubMedCentralPubMedCrossRef
Zurück zum Zitat Olson GE, Winfrey VP, Bi M, Hardy DM, NagDas SK (2004) Zonadhesin assembly into the hamster sperm acrosomal matrix occurs by distinct targeting strategies during spermiogenesis and maturation in the epididymis. Biol Reprod 71:1128–1134PubMedCrossRef Olson GE, Winfrey VP, Bi M, Hardy DM, NagDas SK (2004) Zonadhesin assembly into the hamster sperm acrosomal matrix occurs by distinct targeting strategies during spermiogenesis and maturation in the epididymis. Biol Reprod 71:1128–1134PubMedCrossRef
Zurück zum Zitat Overstreet JW, Lin Y, Yudin AI et al (1995) Location of the PH-20 protein on acrosome-intact and acrosome-reacted spermatozoa of cynomolgus macaques. Biol Reprod 52:105–114PubMedCrossRef Overstreet JW, Lin Y, Yudin AI et al (1995) Location of the PH-20 protein on acrosome-intact and acrosome-reacted spermatozoa of cynomolgus macaques. Biol Reprod 52:105–114PubMedCrossRef
Zurück zum Zitat Phelps BM, Primakoff P, Koppel DE, Low MG, Myles DG (1988) Restricted lateral diffusion of PH-20, a PI-anchored sperm membrane protein. Science 240:1780–1782PubMedCrossRef Phelps BM, Primakoff P, Koppel DE, Low MG, Myles DG (1988) Restricted lateral diffusion of PH-20, a PI-anchored sperm membrane protein. Science 240:1780–1782PubMedCrossRef
Zurück zum Zitat Polakoski KL, Parrish RF (1977) Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm. J Biol Chem 252:1888–1894PubMed Polakoski KL, Parrish RF (1977) Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm. J Biol Chem 252:1888–1894PubMed
Zurück zum Zitat Post TW, Liszewski MK, Adams EM, Tedja I, Miller EA, Atkinson JP (1991) Membrane cofactor protein of the complement system: alternative splicing of serine/threonine/proline-rich exons and cytoplasmic tails produces multiple isoforms that correlate with protein phenotype. J Exp Med 174:93–102PubMedCrossRef Post TW, Liszewski MK, Adams EM, Tedja I, Miller EA, Atkinson JP (1991) Membrane cofactor protein of the complement system: alternative splicing of serine/threonine/proline-rich exons and cytoplasmic tails produces multiple isoforms that correlate with protein phenotype. J Exp Med 174:93–102PubMedCrossRef
Zurück zum Zitat Primakoff P, Hyatt H, Myles DG (1985) A role for the migrating sperm surface antigen PH-20 in guinea pig sperm binding to the egg zona pellucida. J Cell Biol 101:2239–2244PubMedCrossRef Primakoff P, Hyatt H, Myles DG (1985) A role for the migrating sperm surface antigen PH-20 in guinea pig sperm binding to the egg zona pellucida. J Cell Biol 101:2239–2244PubMedCrossRef
Zurück zum Zitat Ramalho-Santos J, Terada Y, Schatten G (2002) VAMP/synaptobrevin as an acrosomal marker for human sperm. Fertil Steril 77:159–161PubMedCrossRef Ramalho-Santos J, Terada Y, Schatten G (2002) VAMP/synaptobrevin as an acrosomal marker for human sperm. Fertil Steril 77:159–161PubMedCrossRef
Zurück zum Zitat Reddi PP, Naaby-Hansen S, Aguolnik I et al (1995) Complementary deoxyribonucleic acid cloning and characterization of mSP-10: the mouse homologue of human acrosomal protein SP-10. Biol Reprod 53:873–881PubMedCrossRef Reddi PP, Naaby-Hansen S, Aguolnik I et al (1995) Complementary deoxyribonucleic acid cloning and characterization of mSP-10: the mouse homologue of human acrosomal protein SP-10. Biol Reprod 53:873–881PubMedCrossRef
Zurück zum Zitat Reddi PP, Shore AN, Acharya KK, Herr JC (2002) Transcriptional regulation of spermiogenesis: insights from the study of the gene encoding the acrosomal protein SP-10. J Reprod Immunol 53:25–36PubMedCrossRef Reddi PP, Shore AN, Acharya KK, Herr JC (2002) Transcriptional regulation of spermiogenesis: insights from the study of the gene encoding the acrosomal protein SP-10. J Reprod Immunol 53:25–36PubMedCrossRef
Zurück zum Zitat Reid MS, Blobel CP (1994) Apexin, an acrosomal pentaxin. J Biol Chem 269:32615–32620PubMed Reid MS, Blobel CP (1994) Apexin, an acrosomal pentaxin. J Biol Chem 269:32615–32620PubMed
Zurück zum Zitat Russell LD, Ettlin RA, Sinha-Hikim A, Clegg E (1990) Hitological and histopathological evaluation of the testis. Cache River Press, USA Russell LD, Ettlin RA, Sinha-Hikim A, Clegg E (1990) Hitological and histopathological evaluation of the testis. Cache River Press, USA
Zurück zum Zitat Sabeur K, Cherr GN, Yudin AI, Primakoff P, Li MW, Overstreet JW (1997) The PH-20 protein in human spermatozoa. J Androl 18:151–158PubMed Sabeur K, Cherr GN, Yudin AI, Primakoff P, Li MW, Overstreet JW (1997) The PH-20 protein in human spermatozoa. J Androl 18:151–158PubMed
Zurück zum Zitat Sachdev M, Mandal A, Mulders S et al (2012) Oocyte specific oolemmal SAS1B involved in sperm binding through intra-acrosomal SLLP1 during fertilization. Dev Biol 363:40–51PubMedCentralPubMedCrossRef Sachdev M, Mandal A, Mulders S et al (2012) Oocyte specific oolemmal SAS1B involved in sperm binding through intra-acrosomal SLLP1 during fertilization. Dev Biol 363:40–51PubMedCentralPubMedCrossRef
Zurück zum Zitat Satouh Y, Inoue N, Ikawa M, Okabe M (2012) Visualization of the moment of mouse sperm–egg fusion and dynamic localization of IZUMO1. J Cell Sci 125:4985–4990PubMedCrossRef Satouh Y, Inoue N, Ikawa M, Okabe M (2012) Visualization of the moment of mouse sperm–egg fusion and dynamic localization of IZUMO1. J Cell Sci 125:4985–4990PubMedCrossRef
Zurück zum Zitat Saxena DK, Tanii I, Yoshinaga K, Toshimori K (1999) Role of intra-acrosomal antigenic molecules acrin 1 (MN7) and acrin 2 (MC41) in penetration of the zona pellucida in fertilization in mice. J Reprod Fertil 117:17–25PubMedCrossRef Saxena DK, Tanii I, Yoshinaga K, Toshimori K (1999) Role of intra-acrosomal antigenic molecules acrin 1 (MN7) and acrin 2 (MC41) in penetration of the zona pellucida in fertilization in mice. J Reprod Fertil 117:17–25PubMedCrossRef
Zurück zum Zitat Shamsadin R, Adham IM, Nayernia K, Heinlein UA, Oberwinkler H, Engel W (1999) Male mice deficient for germ-cell cyritestin are infertile. Biol Reprod 61:1445–1451PubMedCrossRef Shamsadin R, Adham IM, Nayernia K, Heinlein UA, Oberwinkler H, Engel W (1999) Male mice deficient for germ-cell cyritestin are infertile. Biol Reprod 61:1445–1451PubMedCrossRef
Zurück zum Zitat Shetty J, Wolkowicz MJ, Digilio LC et al (2003) SAMP14, a novel, acrosomal membrane-associated, glycosylphosphatidylinositol-anchored member of the Ly-6/urokinase-type plasminogen activator receptor superfamily with a role in sperm–egg interaction. J Biol Chem 278:30506–30515PubMedCrossRef Shetty J, Wolkowicz MJ, Digilio LC et al (2003) SAMP14, a novel, acrosomal membrane-associated, glycosylphosphatidylinositol-anchored member of the Ly-6/urokinase-type plasminogen activator receptor superfamily with a role in sperm–egg interaction. J Biol Chem 278:30506–30515PubMedCrossRef
Zurück zum Zitat Siegel MS, Bechtold DS, Kopta CI, Polakoski KL (1986) The rapid purification and partial characterization of human sperm proacrosin using an automated fast protein liquid chromatography (FPLC) system. Biochim Biophys Acta 883:567–573PubMedCrossRef Siegel MS, Bechtold DS, Kopta CI, Polakoski KL (1986) The rapid purification and partial characterization of human sperm proacrosin using an automated fast protein liquid chromatography (FPLC) system. Biochim Biophys Acta 883:567–573PubMedCrossRef
Zurück zum Zitat Sosnik J, Miranda PV, Spiridonov NA et al (2009) Tssk6 is required for Izumo relocalization and gamete fusion in the mouse. J Cell Sci 122:2741–2749PubMedCentralPubMedCrossRef Sosnik J, Miranda PV, Spiridonov NA et al (2009) Tssk6 is required for Izumo relocalization and gamete fusion in the mouse. J Cell Sci 122:2741–2749PubMedCentralPubMedCrossRef
Zurück zum Zitat Suryavathi V, Panneerdoss S, Wolkowicz MJ et al (2015) Dynamic changes in equatorial segment protein 1 (SPESP1) glycosylation during mouse spermiogenesis. Biol Reprod 92:1–16CrossRef Suryavathi V, Panneerdoss S, Wolkowicz MJ et al (2015) Dynamic changes in equatorial segment protein 1 (SPESP1) glycosylation during mouse spermiogenesis. Biol Reprod 92:1–16CrossRef
Zurück zum Zitat Tanii I, Araki S, Toshimori K (1994) Intra-acrosomal organization of a 90-kilodalton antigen during spermiogenesis in the rat. Cell Tissue Res 277:61–67PubMedCrossRef Tanii I, Araki S, Toshimori K (1994) Intra-acrosomal organization of a 90-kilodalton antigen during spermiogenesis in the rat. Cell Tissue Res 277:61–67PubMedCrossRef
Zurück zum Zitat Tardif S, Cormier N (2011) Role of zonadhesin during sperm–egg interaction: a species-specific acrosomal molecule with multiple functions. Mol Hum Reprod 17:661–668PubMedCrossRef Tardif S, Cormier N (2011) Role of zonadhesin during sperm–egg interaction: a species-specific acrosomal molecule with multiple functions. Mol Hum Reprod 17:661–668PubMedCrossRef
Zurück zum Zitat Tardif S, Wilson MD, Wagner R et al (2010) Zonadhesin is essential for species specificity of sperm adhesion to the egg zona pellucida. J Biol Chem 285:24863–24870PubMedCentralPubMedCrossRef Tardif S, Wilson MD, Wagner R et al (2010) Zonadhesin is essential for species specificity of sperm adhesion to the egg zona pellucida. J Biol Chem 285:24863–24870PubMedCentralPubMedCrossRef
Zurück zum Zitat Thaler CD, Cardullo RA (1995) Biochemical characterization of a glycosylphosphatidylinositol-linked hyaluronidase on mouse sperm. Biochemistry 34:7788–7795PubMedCrossRef Thaler CD, Cardullo RA (1995) Biochemical characterization of a glycosylphosphatidylinositol-linked hyaluronidase on mouse sperm. Biochemistry 34:7788–7795PubMedCrossRef
Zurück zum Zitat Tokuhiro K, Ikawa M, Benham AM, Okabe M (2012) Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility. Proc Natl Acad Sci USA 109:3850–3855PubMedCentralPubMedCrossRef Tokuhiro K, Ikawa M, Benham AM, Okabe M (2012) Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male fertility. Proc Natl Acad Sci USA 109:3850–3855PubMedCentralPubMedCrossRef
Zurück zum Zitat Toshimori K (2009) Dynamics of the mammalian sperm head: modifications and maturation events from spermatogenesis to egg activation. Adv Anat Embryol Cell Biol 204:5–94PubMed Toshimori K (2009) Dynamics of the mammalian sperm head: modifications and maturation events from spermatogenesis to egg activation. Adv Anat Embryol Cell Biol 204:5–94PubMed
Zurück zum Zitat Toshimori K (2011) Dynamics of the mammalian sperm membrane modification leading to fertilization: a cytological study. J Electron Microsc (Tokyo) 60[Suppl 1]:S31–S42CrossRef Toshimori K (2011) Dynamics of the mammalian sperm membrane modification leading to fertilization: a cytological study. J Electron Microsc (Tokyo) 60[Suppl 1]:S31–S42CrossRef
Zurück zum Zitat Toshimori K, Eddy EM (2014) The Spermatozoon. In: Plant TM, Zeleznik A (eds) Knobil and Neill’s physiology of reproduction, vol 1, 4th edn. Acaemic Press, New York, pp 99–148 Toshimori K, Eddy EM (2014) The Spermatozoon. In: Plant TM, Zeleznik A (eds) Knobil and Neill’s physiology of reproduction, vol 1, 4th edn. Acaemic Press, New York, pp 99–148
Zurück zum Zitat Toshimori K, Ito C (2003) Formation and organization of the mammalian sperm head. Arch Histol Cytol 66:383–396PubMedCrossRef Toshimori K, Ito C (2003) Formation and organization of the mammalian sperm head. Arch Histol Cytol 66:383–396PubMedCrossRef
Zurück zum Zitat Toshimori K, Tanii I, Araki S, Oura C (1992) Characterization of the antigen recognized by a monoclonal antibody MN9: unique transport pathway to the equatorial segment of sperm head during spermiogenesis. Cell Tissue Res 270:459–468PubMedCrossRef Toshimori K, Tanii I, Araki S, Oura C (1992) Characterization of the antigen recognized by a monoclonal antibody MN9: unique transport pathway to the equatorial segment of sperm head during spermiogenesis. Cell Tissue Res 270:459–468PubMedCrossRef
Zurück zum Zitat Toshimori K, Saxena DK, Tanii I, Yoshinaga K (1998) An MN9 antigenic molecule, equatorin, is required for successful sperm–oocyte fusion in mice. Biol Reprod 59:22–29PubMedCrossRef Toshimori K, Saxena DK, Tanii I, Yoshinaga K (1998) An MN9 antigenic molecule, equatorin, is required for successful sperm–oocyte fusion in mice. Biol Reprod 59:22–29PubMedCrossRef
Zurück zum Zitat Tulsiani DR, Abou-Haila A, Loeser CR, Pereira BM (1998) The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization. Exp Cell Res 240:151–164PubMedCrossRef Tulsiani DR, Abou-Haila A, Loeser CR, Pereira BM (1998) The biological and functional significance of the sperm acrosome and acrosomal enzymes in mammalian fertilization. Exp Cell Res 240:151–164PubMedCrossRef
Zurück zum Zitat Wassarman PM (2009) Mammalian fertilization: the strange case of sperm protein 56. BioEssays 31:153–158PubMedCrossRef Wassarman PM (2009) Mammalian fertilization: the strange case of sperm protein 56. BioEssays 31:153–158PubMedCrossRef
Zurück zum Zitat Westbrook-Case VA, Winfrey VP, Olson GE (1994) A domain-specific 50-kilodalton structural protein of the acrosomal matrix is processed and released during the acrosome reaction in the guinea pig. Biol Reprod 51:1–13PubMedCrossRef Westbrook-Case VA, Winfrey VP, Olson GE (1994) A domain-specific 50-kilodalton structural protein of the acrosomal matrix is processed and released during the acrosome reaction in the guinea pig. Biol Reprod 51:1–13PubMedCrossRef
Zurück zum Zitat Westbrook-Case VA, Winfrey VP, Olson GE (1995) Sorting of the domain-specific acrosomal matrix protein AM50 during spermiogenesis in the guinea pig. Dev Biol 167:338–349PubMedCrossRef Westbrook-Case VA, Winfrey VP, Olson GE (1995) Sorting of the domain-specific acrosomal matrix protein AM50 during spermiogenesis in the guinea pig. Dev Biol 167:338–349PubMedCrossRef
Zurück zum Zitat Wolkowicz MJ, Shetty J, Westbrook A et al (2003) Equatorial segment protein defines a discrete acrosomal subcompartment persisting throughout acrosomal biogenesis. Biol Reprod 69:735–745PubMedCrossRef Wolkowicz MJ, Shetty J, Westbrook A et al (2003) Equatorial segment protein defines a discrete acrosomal subcompartment persisting throughout acrosomal biogenesis. Biol Reprod 69:735–745PubMedCrossRef
Zurück zum Zitat Wolkowicz MJ, Digilio L, Klotz K, Flickinger CJ, Herr JC (2008) Equatorial segment protein (ESP) is a human alloantigen involved in sperm–egg binding and fusion. J Androl 29:272–282PubMedCentralPubMedCrossRef Wolkowicz MJ, Digilio L, Klotz K, Flickinger CJ, Herr JC (2008) Equatorial segment protein (ESP) is a human alloantigen involved in sperm–egg binding and fusion. J Androl 29:272–282PubMedCentralPubMedCrossRef
Zurück zum Zitat Wright RM, Suri AK, Kornreich B, Flickinger CJ, Herr JC (1993) Cloning and characterization of the gene coding for the human acrosomal protein SP-10. Biol Reprod 49:316–325PubMedCrossRef Wright RM, Suri AK, Kornreich B, Flickinger CJ, Herr JC (1993) Cloning and characterization of the gene coding for the human acrosomal protein SP-10. Biol Reprod 49:316–325PubMedCrossRef
Zurück zum Zitat Yamagata K, Murayama K, Okabe M et al (1998) Acrosin accelerates the dispersal of sperm acrosomal proteins during acrosome reaction. J Biol Chem 273:10470–10474PubMedCrossRef Yamagata K, Murayama K, Okabe M et al (1998) Acrosin accelerates the dispersal of sperm acrosomal proteins during acrosome reaction. J Biol Chem 273:10470–10474PubMedCrossRef
Zurück zum Zitat Yamaguchi R, Muro Y, Isotani A et al (2009) Disruption of ADAM3 impairs the migration of sperm into oviduct in mouse. Biol Reprod 81:142–146PubMedCrossRef Yamaguchi R, Muro Y, Isotani A et al (2009) Disruption of ADAM3 impairs the migration of sperm into oviduct in mouse. Biol Reprod 81:142–146PubMedCrossRef
Zurück zum Zitat Yamatoya K, Yoshida K, Ito C et al (2009) Equatorin: identification and characterization of the epitope of the MN9 antibody in the mouse. Biol Reprod 81:889–897PubMedCrossRef Yamatoya K, Yoshida K, Ito C et al (2009) Equatorin: identification and characterization of the epitope of the MN9 antibody in the mouse. Biol Reprod 81:889–897PubMedCrossRef
Zurück zum Zitat Yanagimachi R (1994) Fertilization. In: Knobil E, Neill JD (eds) The physiology of reproduction, vol 1. Raven Press, New York, pp 189–317 Yanagimachi R (1994) Fertilization. In: Knobil E, Neill JD (eds) The physiology of reproduction, vol 1. Raven Press, New York, pp 189–317
Zurück zum Zitat Yatsenko AN, O’Neil DS, Roy A et al (2012) Association of mutations in the zona pellucida binding protein 1 (ZPBP1) gene with abnormal sperm head morphology in infertile men. Mol Hum Reprod 18:14–21PubMedCentralPubMedCrossRef Yatsenko AN, O’Neil DS, Roy A et al (2012) Association of mutations in the zona pellucida binding protein 1 (ZPBP1) gene with abnormal sperm head morphology in infertile men. Mol Hum Reprod 18:14–21PubMedCentralPubMedCrossRef
Zurück zum Zitat Yoshida K, Ito C, Yamatoya K et al (2010) A model of the acrosome reaction progression via the acrosomal membrane-anchored protein equatorin. Reproduction 139:533–544PubMedCrossRef Yoshida K, Ito C, Yamatoya K et al (2010) A model of the acrosome reaction progression via the acrosomal membrane-anchored protein equatorin. Reproduction 139:533–544PubMedCrossRef
Zurück zum Zitat Yoshinaga K, Tanii I, Saxena DK, Toshimori K (1998) Immunocytochemical alterations in the intra-acrosomal antigen MN7 during epididymal maturation of guinea pig spermatozoa. Cell Tissue Res 292:427–433PubMedCrossRef Yoshinaga K, Tanii I, Saxena DK, Toshimori K (1998) Immunocytochemical alterations in the intra-acrosomal antigen MN7 during epididymal maturation of guinea pig spermatozoa. Cell Tissue Res 292:427–433PubMedCrossRef
Zurück zum Zitat Yoshinaga K, Tanii I, Oh-Oka T, Toshimori K (2000) Transport and rearrangement of the intra-acrosomal protein acrin1 (MN7) during spermiogenesis in the guinea pig testis. Anat Rec 259:131–140PubMedCrossRef Yoshinaga K, Tanii I, Oh-Oka T, Toshimori K (2000) Transport and rearrangement of the intra-acrosomal protein acrin1 (MN7) during spermiogenesis in the guinea pig testis. Anat Rec 259:131–140PubMedCrossRef
Zurück zum Zitat Yoshinaga K, Saxena DK, Oh-oka T, Tanii I, Toshimori K (2001) Inhibition of mouse fertilization in vivo by intra-oviductal injection of an anti-equatorin monoclonal antibody. Reproduction 122:649–655PubMedCrossRef Yoshinaga K, Saxena DK, Oh-oka T, Tanii I, Toshimori K (2001) Inhibition of mouse fertilization in vivo by intra-oviductal injection of an anti-equatorin monoclonal antibody. Reproduction 122:649–655PubMedCrossRef
Zurück zum Zitat Yu Y, Xu W, Yi YJ, Sutovsky P, Oko R (2006) The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: characterization of its most prominent polypeptide (IAM38). Dev Biol 290:32–43PubMedCrossRef Yu Y, Xu W, Yi YJ, Sutovsky P, Oko R (2006) The extracellular protein coat of the inner acrosomal membrane is involved in zona pellucida binding and penetration during fertilization: characterization of its most prominent polypeptide (IAM38). Dev Biol 290:32–43PubMedCrossRef
Zurück zum Zitat Yu Y, Vanhorne J, Oko R (2009) The origin and assembly of a zona pellucida binding protein, IAM38, during spermiogenesis. Microsc Res Tech 72:558–565PubMedCrossRef Yu Y, Vanhorne J, Oko R (2009) The origin and assembly of a zona pellucida binding protein, IAM38, during spermiogenesis. Microsc Res Tech 72:558–565PubMedCrossRef
Zurück zum Zitat Yuan R, Primakoff P, Myles DG (1997) A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm–egg plasma membrane adhesion and fusion. J Cell Biol 137:105–112PubMedCentralPubMedCrossRef Yuan R, Primakoff P, Myles DG (1997) A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm–egg plasma membrane adhesion and fusion. J Cell Biol 137:105–112PubMedCentralPubMedCrossRef
Zurück zum Zitat Zaneveld LJ, De Jonge CJ (1991) Mammalian sperm acrosomal enzymes and the acrosome reaction. In: Dunbar B, O’Rand M (eds) A comparative overview of mammalian fertilization. Plenum, New York Zaneveld LJ, De Jonge CJ (1991) Mammalian sperm acrosomal enzymes and the acrosome reaction. In: Dunbar B, O’Rand M (eds) A comparative overview of mammalian fertilization. Plenum, New York
Zurück zum Zitat Zhang H, Martin-DeLeon PA (2003) Mouse Spam1 (PH-20) is a multifunctional protein: evidence for its expression in the female reproductive tract. Biol Reprod 69:446–454PubMedCrossRef Zhang H, Martin-DeLeon PA (2003) Mouse Spam1 (PH-20) is a multifunctional protein: evidence for its expression in the female reproductive tract. Biol Reprod 69:446–454PubMedCrossRef
Zurück zum Zitat Zhang H, Morales CR, Badran H, El-Alfy M, Martin-DeLeon PA (2004) Spam1 (PH-20) expression in the extratesticular duct and accessory organs of the mouse: a possible role in sperm fluid reabsorption. Biol Reprod 71:1101–1107PubMedCrossRef Zhang H, Morales CR, Badran H, El-Alfy M, Martin-DeLeon PA (2004) Spam1 (PH-20) expression in the extratesticular duct and accessory organs of the mouse: a possible role in sperm fluid reabsorption. Biol Reprod 71:1101–1107PubMedCrossRef
Zurück zum Zitat Zhou C, Kang W, Baba T (2012) Functional characterization of double-knockout mouse sperm lacking SPAM1 and ACR or SPAM1 and PRSS21 in fertilization. J Reprod Dev 58:330–337PubMedCrossRef Zhou C, Kang W, Baba T (2012) Functional characterization of double-knockout mouse sperm lacking SPAM1 and ACR or SPAM1 and PRSS21 in fertilization. J Reprod Dev 58:330–337PubMedCrossRef
Metadaten
Titel
Acrosome markers of human sperm
verfasst von
Chizuru Ito
Kiyotaka Toshimori
Publikationsdatum
01.03.2016
Verlag
Springer Japan
Erschienen in
Anatomical Science International / Ausgabe 2/2016
Print ISSN: 1447-6959
Elektronische ISSN: 1447-073X
DOI
https://doi.org/10.1007/s12565-015-0323-9

Weitere Artikel der Ausgabe 2/2016

Anatomical Science International 2/2016 Zur Ausgabe

Leitlinien kompakt für die Innere Medizin

Mit medbee Pocketcards sicher entscheiden.

Seit 2022 gehört die medbee GmbH zum Springer Medizin Verlag

Update Innere Medizin

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert.