SEARCH

SEARCH BY CITATION

References

  • Brandelli, A., Miranda, P. V. & Tezon, J. G. 1994. Participation of glycosylated residues in the human sperm acrosome reaction – possible role of N-acetylglucosaminidase. Biochim. Biophys. Acta Mol. Cell Res. 1220, 299304.
  • Brown, C. A. & Mahuran, D. J. 1991. Active arginine residues in β-hexosaminidase. Identification through studies of the B1 variant of Tay-Sachs disease. J. Biol. Chem. 266, 15 85515 862.
  • Cattaneo, F., Pasini, M. E. & Perotti, M. 1997. Glycosidases are present on the surface of Drosophila melanogaster spermatozoa. Mol. Reprod. Dev. 48, 276281.
  • Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J. & Rutter, W. J. 1979. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18, 52945299.
  • Chomczynski, P. & Sacchi, N. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156159.
  • Downey, J. C. & Lambert, C. C. 1994. Attachment of the ascidian sperm surface egg receptor N-acetylglucosaminidase to the cell membrane. Mol. Reprod. Dev. 38, 453458.
  • Eisenhut, M. 2001. Biochemical characterization of egg hexosaminidases from Phallusia mammillata and ultrastructural analysis of the ascidian vitelline coat (PhD Thesis). University of Zürich, Zürich.
  • Eisenhut, M. & Honegger, T. G. 2001. Identification of Phallusia mammillata egg β-N-acetylhexosaminidase with potential role in prevention of polyspermy. In The Biology of Ascidians (eds H.Sawada, H.Yokosawa & C. C. Lambert), pp. 97101. Springer-Verlag, Tokyo.
  • Farooqui, A. A. & Srivastava, P. N. 1980. Isolation of β-N-acetylhexosaminidase from rabbit semen and its role in fertilization. Biochem. J. 191, 827834.
  • Fernandes, M. J., Yew, S., Leclerc, D. et al. 1997. Identification of candidate active site residues in lysosomal β-hexosaminidase A. J. Biol. Chem. 272, 814820.
  • Frohman, M. A., Dush, M. K. & Martin, G. R. 1988. Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer. Proc. Natl Acad. Sci. USA 85, 89989002.
  • Glardon, S., Callaerts, P., Halder, G. & Gehring, W. J. 1997. Conservation of Pax-6 in a lower chordate, the ascidian Phallusia mammillata. Development 124, 817825.
  • Glisin, V., Crkvenjakov, R. & Byus, C. 1974. Ribonucleic acid isolated by cesium chloride centrifugation. Biochemistry 13, 26332637.
  • Godknecht, A. J. 1991. Untersuchungen zur Befruchtung von Phallusia Mammillata (Ascidiacea): Charakterisierung und Funktion verschiedener Spermien- und Eienzyme (PhD Thesis). University of Zürich, Zürich.
  • Godknecht, A. J. & Honegger, T. G. 1991. Isolation, characterization, and localization of a sperm-bound N-acetylglucosaminidase that is indispensable for fertilization in the ascidian, Phallusia mammillata. Dev. Biol. 143, 398407.
  • Godknecht, A. J. & Honegger, T. G. 1995. Specific inhibition of sperm β-N-acetylglucosaminidase by the synthetic inhibitor N-acetylglucosaminono-1,5-lactone O-(phenylcarbamoyl) oxime inhibits fertilization in the ascidian, Phallusia mammillata. Dev. Growth Differ. 37, 183189.
  • Graham, T. R., Zassenhaus, H. P. & Kaplan, A. 1988. Molecular cloning of the cDNA which encodes beta-N-acetylhexosaminidase A from Dictyostelium discoideum. Complete amino acid sequence and homology with the human enzyme. J. Biol. Chem. 263, 16 82316 829.
  • Greve, L. C., Pordy, G. A. & Hedrick, J. L. 1985. N-acetyl-β-D-glucosaminidase activity in the cortical granules of Xenopus laevis eggs. Gamete Res. 12, 305312.
  • Henrissat, B. & Bairoch, A. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293, 781788.
  • Holland, P. W., Garcia-Fernandez, J., Williams, N. A. & Sidow, A. 1994. Gene duplications and the origins of vertebrate development. Development Suppl., 125133.
  • Honegger, T. G. 1986. Fertilization in ascidians: studies on the egg envelope, sperm and gamete interactions in Phallusia mammillata. Dev. Biol. 118, 118128.
  • Honegger, T. G. 1992. The involvement of sperm and egg glycosidases in animal fertilization. Trends Glycosc. Glycotechnol. 4, 437444.
  • Hoshi, M. 1984. Roles of sperm glycosidases and proteases in the ascidian fertilization. In Advances in Invertebrate Reproduction (ed. W. E. A.Engels), pp. 2740. Elsevier Science, Amsterdam.
  • Hoshi, M. 1986. Sperm glycosidase as a plausible mediator of sperm binding to the vitelline envelope in Ascidians. Adv. Exp. Med. Biol. 207, 251260.
  • Hoshi, M., Santis, R. D., Pinto, M. R., Cotelli, F. & Rosati, F. 1983. Is sperm α-L-fucosidase responsible for sperm-egg binding in Ciona intestinalis? In The Sperm Cell, (ed. J.André), pp. 107110. Martius Nijhoff Publishers, The Hague.
  • Hoshi, M., Santis, R. D., Pinto, M. R., Cotelli, F. & Rosati, F. 1985. Sperm glycosidases as mediators of sperm-egg binding in the ascidians. Zool. Sci. 2, 6569.
  • Hoshi, M., Takizawa, S. & Hirohashi, N. 1994. Glycosidases, proteases and ascidian fertilization. Seminars Dev. Biol. 5, 201208.
  • Inaba, K., Padma, P., Satouh, Y. et al. 2002. EST analysis of gene expression in testis of the ascidian Ciona intestinalis. Mol. Reprod. Dev. 62, 431445.
  • Korneluk, R. G., Mahuran, D. J., Neote, K. et al. 1986. Isolation of cDNA clones coding for the α-subunit of human β-hexosaminidase. Extensive homology between the α- and β-subunits and studies on Tay-Sachs disease. J. Biol. Chem. 261, 84078413.
  • Lambert, C. C. 1989a. Ascidian eggs release glycosidase activity which aids in the block against polyspermy. Development 105, 415420.
  • Lambert, C. C. 1989b. Ascidian sperm penetration and the translocation of a cell surface glycosidase. J. Exp. Zool. 249, 308315.
  • Lambert, C. C. & Goode, C. A. 1992. Glycolipid linkage of a polyspermy blocking glycosidase to the ascidian egg surface. Dev. Biol. 154, 95100.
  • Lambert, C. C., Goudeau, H., Franchet, C., Lambert, G. & Goudeau, M. 1997. Ascidian eggs block polyspermy by two independent mechanisms: one at the egg plasma membrane, the other involving the follicle cells. Mol. Reprod. Dev. 48, 137143.
  • Liessem, B., Glombitza, G. J., Knoll, F. et al. 1995. Photoaffinity labeling of human lysosomal β-hexosaminidase B. Identification of Glu-355 at the substrate binding site. J. Biol. Chem. 270, 23 69323 699.
  • Matsuura, K., Sawada, H. & Yokosawa, H. 1993. Purification and properties of N-acetylglucosaminidase from eggs of the ascidian, Halocynthia roretzi. Eur. J. Biochem. 218, 535541.
  • Matsuura, K., Sawada, H. & Yokosawa, H. 1995. N-acetylglucosaminidase inhibitor isolated from the vitelline coat of ascidian eggs is a candidate sperm receptor. Biochem. Biophys. Res. Commun. 213, 311316.
  • Miller, D. J., Gong, X. H., Decker, G. & Shur, B. D. 1993a. Egg cortical granule N-acetylglucosaminidase is required for the mouse zona block to polyspermy. J. Cell Biol. 123, 14311440.
  • Miller, D. J., Gong, X. & Shur, B. D. 1993b. Sperm require β-N-acetylglucosaminidase to penetrate through the egg zona pellucida. Development 118, 12791289.
  • Miranda, P. V., Brandelli, A. & Tezon, J. G. 1995. Characterization of β-N-acetylglucosaminidase from human epididymis. Int. J. Androl. 18, 263270.
  • Miranda, P. V., Gonzalez-Echeverriia, F., Blaquier, J. A., Mahuran, D. J. & Tezon, J. G. 2000. Evidence for the participation of β-hexosaminidase in human sperm–zona pellucida interaction in vitro. Mol. Human Reprod. 6, 699706.
  • Myerowitz, R., Piekarz, R., Neufeld, E. F., Shows, T. B. & Suzuki, K. 1985. Human β-hexosaminidase alpha chain: coding sequence and homology with the beta chain. Proc. Natl Acad. Sci. USA 82, 78307834.
  • Neote, K., Bapat, B., Dumbrille-Ross, A. et al. 1988. Characterization of the human HEXB gene encoding lysosomal β-hexosaminidase. Genomics 3, 279286.
  • Nielsen, H., Engelbrecht, J., Brunak, S. & Von Heijne, G. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10, 16.
  • Perotti, M., Cattaneo, F., Pasini, M. E., Verni, F. & Hackenstein, J. H. P. 2001. Male sterile mutant casanova gives clues to mechanisms of sperm–egg interactions in Drosophila melanogaster. Mol. Reprod. Dev. 60, 248259.
  • Prody, G. A., Greve, L. C. & Hedrick, J. L. 1985. Purification and characterization of an N-acetyl-β-D-glucosaminidase from cortical granules of Xenopus laevis eggs. J. Exp. Zool. 235, 335340.
  • Proia, R. L. 1988. Gene encoding the human β-hexosaminidase β chain: extensive homology of intron placement in the α- and β-chain genes. Proc. Natl Acad. Sci. USA 85, 18831887.
  • Proia, R. L. & Soravia, E. 1987. Organization of the gene encoding the human β-hexosaminidase alpha-chain. J. Biol. Chem. 262, 56775681.
  • Saitou, N. & Nei, M. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406425.
  • Sonderfeld-Fresko, S. & Proia, R. L. 1989. Analysis of the glycosylation and phosphorylation of the lysosomal enzyme, β-hexosaminidase B, by site-directed mutagenesis. J. Biol. Chem. 264, 76927697.
  • Syntin, P., Dacheux, F., Druart, X., Gatti, J. L., Okamura, N. & Dacheux, J. L. 1996. Characterization and identification of proteins secreted in the various regions of the adult boar epididymis. Biol. Reprod. 55, 956974.
  • Takada, M., Yonezawa, N., Yoshizawa, M. et al. 1994. pH–sensitive dissociation and association of β-N-acetylhexosaminidase from boar sperm acrosome. Biol. Reprod. 50, 860868.
  • Tews, I., Perrakis, A., Oppenheim, A., Dauter, Z., Wilson, K. S. & Vorgias, C. E. 1996. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat. Struct. Biol. 3, 638648.
  • Tse, R., Vavougios, G., Hou, Y. & Mahuran, D. J. 1996. Identification of an active acidic residue in the catalytic site of β-hexosaminidase. Biochemistry 35, 75997607.
  • Weitz, G. & Proia, R. L. 1992. Analysis of the glycosylation and phosphorylation of the alpha-subunit of the lysosomal enzyme, β-hexosaminidase A, by site-directed mutagenesis. J. Biol. Chem. 267, 10 03910 044.
  • Zao, P. Z. R., Meizel, S. & Talbot, P. 1985. Release of hyaluronidase and β-N-acetylhexosaminidase during in vitro incubation of hamster sperm. J. Exp. Zool. 234, 6374.