Artículo

Cesari, A.; Sánchez, J.J.; Biancotti, J.C.; Vazquez-Levin, M.H.; Kaiser, G.; Palma, G.A.; Alberio, R.; Vincenti, A.E.; Fornés, M.W. "Immunolocalization of bovine sperm protease BSp120 by light and electron microscopy during capacitation and the acrosome reaction: Its role in in vitro fertilization" (2004) Molecular Reproduction and Development. 69(4):411-418
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Abstract:

Mammalian fertilization involves various steps in which the participation of specific enzymes has been demonstrated by numerous studies. Acrosin is one of the most widely acrosomal protease in mammalian spermatozoa studied, including bovine; however, other proteases have also been described. A new trypsin-like serine protease named bovine serine protease of 120 kDa (BSp120) and its pre-cursor BSp66 (66 kDa) were identified in bovine spermatozoa. Cytological and ultrastructural immunolocalization studies on BSp120 were performed in live and fixed cells. Immunoflorescence assays with specific polyclonal antibodies revealed localization of BSp120 on the sperm head, with a signal homogeneously distributed over the acrosome resembling a horseshoe. After the acrosome reaction, sperm showed a patchy pattern in the acrosomal cap. Immune electron microscopy analysis indicated that BSp120 is located over the head plasma membrane of capacitated spermatozoa and acrosome reacting spermatozoa. To assess BSp120 function in sperm-oocyte interaction, in vitro fertilization studies were conducted. Oocytes were incubated with spermatozoa pre-treated with anti-BSp120, anti-guinea pig acrosin, and anti-BSp120 plus anti-guinea pig acrosin. Pre-treatment of bovine spermatozoa with antibodies towards each protein did not significantly modify fertilization rates. However, when both anti-acrosin and anti-BSp120 antibodies were simultaneously added, there was a significant decrease in the fertilization rate, suggesting that both enzymes may be required for fertilization. Altogether, the results from the present study described the localization of BSp120 over the acrosome of bovine sperm, and suggest its involvement in fertilization. © 2004 Wiley-Liss, Inc.

Registro:

Documento: Artículo
Título:Immunolocalization of bovine sperm protease BSp120 by light and electron microscopy during capacitation and the acrosome reaction: Its role in in vitro fertilization
Autor:Cesari, A.; Sánchez, J.J.; Biancotti, J.C.; Vazquez-Levin, M.H.; Kaiser, G.; Palma, G.A.; Alberio, R.; Vincenti, A.E.; Fornés, M.W.
Filiación:Inst. de Invest. Biológicas, Fac. de Ciencias Exactas Y Naturales, Univ. Nacional de Mar del Plata, Mar del Plata, Buenos Aires, Argentina
Inst. de Biol. Y Med. Experimental, CONICET-UBA Vuelta de Obligado, Buenos Aires, Argentina
Lab. de Biotecnologia de la Reprod., INTA, Balcarce, Provincia de Buenos Aires, Argentina
Inst. Histol. Y Embriol. Dr. M., Fac. de Cie. Medicas UNCU-CONICET, Mendoza, Argentina
Univ. Nacional de Mar del Plata, Argentina
CONICET, Argentina
INTA
Inst. de Invest. Biológicas, Fac. de Ciencias Exactas Y Naturales, Univ. Nacional de Mar del Plata, CC:1245, Zip Code: 7600, Mar del Plata, Argentina
Idioma: Inglés
Palabras clave:Mammalian fertilization; Membrane sperm protein; Serine protease; acrosin; enzyme antibody; polyclonal antibody; serine proteinase; acrosome reaction; animal cell; article; cattle; cell membrane; controlled study; electron microscopy; enzyme activity; enzyme analysis; enzyme localization; fertilization in vitro; immunofluorescence test; immunolocalization; incubation time; male; microscopy; nonhuman; oocyte; priority journal; spermatozoon capacitation; spermatozoon motility; ultrastructure; Acrosome; Acrosome Reaction; Animals; Cattle; Enzyme Precursors; Fertilization in Vitro; Immunohistochemistry; Male; Peptide Hydrolases; Sperm Capacitation; Bovinae; Cavia porcellus; Mammalia; Sus scrofa
Año:2004
Volumen:69
Número:4
Página de inicio:411
Página de fin:418
DOI: http://dx.doi.org/10.1002/mrd.20100
Título revista:Molecular Reproduction and Development
Título revista abreviado:Mol. Reprod. Dev.
ISSN:1040452X
CODEN:MREDE
CAS:acrosin, 9068-57-9; serine proteinase, 37259-58-8; Enzyme Precursors; Peptide Hydrolases, 3.4.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1040452X_v69_n4_p411_Cesari

Referencias:

  • Baba, T., Azuma, S., Kashiwabara, S., Toyoda, Y., Sperm from mice carrying a targeted mutation of the acrosin gene can penetrate the oocyte zona pellucida and effect fertilization (1994) J Biol Chem, 269, pp. 31845-31849
  • Baba, T., Niida, Y., Michikawa, Y., Kashiwabara, S., Kodaira, K., Takenaka, M., Kohno, N., Arai, Y., An acrosomal protein sp32, in mammalian sperm is a binding protein specific for two proacrosins and an acrosin intermediate (1994) J Biol Chem, 269, pp. 133-140
  • Bavister, B., Yanagimachi, R., The effects of sperm extracts and energy sources on the motility and acrosome reaction of hamster spermatozoa in vitro (1997) Biol Reprod, 16, pp. 228-237
  • Cesari, A., Cacciato, C.S., De Castro, R.E., Sánchez, J.J., Low temperature-induced dimerization of the bovine sperm serine protease, BSp66 (2003) J Cell Biochem, 88, pp. 1057-1065
  • Cesari, A., Cacciato, C.S., De Castro, R.E., Sánchez, J.J., Partial purification and characterization of trypsin-like serine proteases from bovine sperm (2004) Int J Androl, , In press
  • Chatterjee, S., De Lamirande, E., Gagnon, C., Cryopreservation alters membrane sulfhydryl status of bull spermatozoa: Protection by oxidized glutathione (2001) Mol Reprod Dev, 60, pp. 498-506
  • Cherr, G.N., Yudin, A.I., Overstreet, J.W., The dual functions of GPI-anchored PH-20: Hyaluronidase and intracellular signaling (2001) Matrix Biol, 20, pp. 515-525
  • Dell, A., Morris, H.R., Easton, R.L., Patankar, M., Clark, G.F., The glycobiology of gametes and fertilization (1999) Biochim Biophys Acta, 1473, pp. 196-205
  • Fraser, L.R., p-Aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction (1982) J Reprod Fertil, 65, pp. 185-194
  • Furlong, L., Hellman, U., Krimer, A., Tezon, J., Charreau, E., Vazquez-Levin, M., Expression of human proacrosin in Escherichia coli and binding to zona pellucida (2000) Biol Reprod, 62, pp. 602-615
  • Haden, N.P., Hickox, J.R., Whisnant, C.S., Hardy, D.M., Systematic characterization of sperm-specific membrane proteins in swine (2000) Biol Reprod, 63, pp. 1839-1847
  • Hardy, D.M., Wild, G.C., Tung, K.S.K., Purification and initial characterization of proacrosins from guinea pig testes and epididymal spermatozoa (1987) Biol Reprod, 37, pp. 189-199
  • Hasegawa, A., Tsubamoto, H., Hamada, Y., Koyama, K., Blocking effect of antisera to recombinant zona pellucida proteins (r-ZPA) on in vitro fertilization (2000) Am J Reprod Immunol, 44, pp. 59-64
  • Hawk, H.W., Wall, R.J., Improved yields of bovine blastocysts from in vitro produced oocytes. 1. Media and coculture of cells (1994) Theriogenology, 41, pp. 1585-1594
  • Honda, A., Siruntawineti, J., Baba, T., Role of acrosomal matrix proteases in sperm-zona pellucida interactions (2002) Hum Reprod Update, 8, pp. 405-412. , Review
  • Honda, A., Yamagata, K., Sugiura, S., Watanabe, K., Baba, T., A mouse serine protease TESP5 is selectively included into li included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol- anchored protein (2002) J Biol Chem, 277, pp. 16976-16984
  • Hooper, J.D., Clements, J.A., Quigley, J.P., Antalis, T.M., Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes (2001) J Biol Chem, 12 (276), pp. 857-860
  • Hu, Z.H., Liu, Q., Shang, Q., Zheng, M., Yang, J., Zhang, Y.L., Identification and characterization of a new member of serpin family-HongrES1 in rat epididymis (2002) Cell Res, 12, pp. 407-410
  • Klinefelter, G.R., Welch, J.E., Perrault, S.D., Moore, H.D., Zucker, R.M., Suarez, J.D., Roberts, N.L., Jeffay, S., Localization of the sperm protein SP22 and inhibition of fertility in vivo and in vitro (2002) J Andrology, 23, pp. 48-63
  • Kohno, N., Yamagata, K., Yamada, S., Kashiwabara, S., Sakai, Y., Baba, T., Two novel testicular serine proteases, TESP 1 y TESP 2 are present in the mouse sperm acrosome (1998) Biochem Biophys Res Com, 245, pp. 658-665
  • Kovacs, A., Foote, R.H., Viability of acrosome staining of bull, boar and rabbit spermatozoa (1992) Biotech Hitochem, 67, pp. 119-124
  • Lambert, C.C., Someno, T., Sawada, H., Sperm surface proteases in ascidian fertilization (2002) J Exp Zool, 292, pp. 88-95
  • Llanos, M., Vigil, P., Salgado, A.M., Morales, P., Inhibition of the acrosome reaction by trypsin inhibitors and prevention of penetration of spermatozoa through the human zona pellucida (1993) J Reprod Fertil, 97, pp. 173-178
  • Marquínez, A.C., Andreetta, A.M., Chen, J.S., Menesini Chen, M.G., Wolfenstein Todel, C., Scacciati De Cerezo, J.M., Inhibition of acrosine-like protease by a lectin affinity chromatographic bovine seminal plasma fraction containing the PDC-109 and aSFP proteins (2000) J Chromatogr B, 746, pp. 141-150
  • Nakamura, Y., Inoue, M., Okumura, Y., Shiota, M., Nishikawa, M., Arase, S., Kido, H., Cloning, expression analysis, and tissue distribution of esp-1/testisin, a membrane-type serine protease from rat (2003) J Med Invest, 50, pp. 78-86
  • Ohmura, K., Kohno, N., Kobayashi, Y., Yamagata, K., Sato, S., Kashiwabara, S., Baba, T., A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction (1999) JBC, 274, pp. 29426-29432
  • Palma, G.A., Müller, M., Brem, G., Effect of insulin-like growth factor I (IGF-I) at high concentrations on blastocyst development of bovine embryos produced in vitro (1997) J Reprod Fertil, 110, pp. 347-353
  • Peknicova, J., Capkova, J., Geussova, G., Ivanova, M., Mollova, M., Monoclonal antibodies to intra-acrosomal proteins inhibit gamete binding in vitro (2001) Theriogenology, 56, pp. 211-223
  • Pietrobon, E.O., Monclus, M.A., Alberdi, A.J., Fornés, M.W., Progesterone receptor availability in mouse spermatozoa during epididymal transit and capacitation. Ligand blot detection of progesterone binding protein (2003) J Androl, 24, pp. 612-620
  • Ramalho-Santos, J., Moreno, R.D., Sutovsky, P., Wing-Sang Chan, A., Hewitson, L., Wessel, G.M., Simerly, C.R., Schatten, G., SNAREs in mammalian sperm: Possible implications for fertilization (2000) Dev Biol, 223, pp. 54-69
  • Rosenkrans, C.F., First, N.L., Effects of free amino acids and vitamins on cleavage and development rate of bovine zygotes in vitro (1994) J Anim Sci, 72, pp. 434-437
  • Sanchez-Gutierrez, M., Contreras, R.G., Mujica, A., Cytochalasin-D retards sperm incorporation deep into the egg cytoplasm but not membrane fusion with the egg plasma membrane (2002) Mol Reprod Dev, 63, pp. 518-528
  • Sirivaidyapong, S., Bevers, M.M., Gadella, B.M., Colenbrander, B., Induction of the acrosome reaction in dog sperm cells is dependent on epididymal maturation: The generation of a functional progesterone receptor is involved (2001) Mol Reprod Dev, 58, pp. 451-459
  • Tesarik, J., The role of proteases in the mammalian sperm acrosome reaction (1995) Human Sperm Acrosome Reaction, pp. 123-132. , Fènichel P, Parinaud J, editors. Colloque INSERM/John Libbey Eurotext Ltd., France
  • Tesarik, J., Drahorad, J., Peknicova, J., Subcellular immunochemical localization of acrosin in human spermatozoa during acrosome reaction and zona pellucida penetration (1988) Fertil Steril, 50, pp. 133-141
  • Tesarik, J., Drahorad, J., Testart, J., Mendoza, C., Acrosin activation follows its surface exposure and precedes membrane fusion in human sperm acrosome reaction (1990) Development, 110, pp. 391-400
  • Uhrin, P., Dewerchin, M., Hilpert, M., Chrenek, P., Schofer, C., Zechmeister-Machhart, M., Kranke, G., Geiger, M., Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male infertility (2000) J Clin Invest, 106, pp. 1531-1539
  • Urch, U.A., Biochemistry, function of acrosin (1991) Elements of Mammalian Fertilization, 1, pp. 233-248. , Wassarman PM, editor. Florida: CRC Press, Inc
  • Visconti, P.E., Ning, X., Fornes, M.W., Alvarez, J.G., Stein, P., Connors, S.A., Kopf, G.S., Cholesterol efflux-mediated signal transduction in mammalian sperm: Cholesterol release signals an increase in protein tyrosine phosphorylation during mouse sperm capacitation (1999) Dev Biol, 14, pp. 429-443
  • Yanagimachi, R., Mammalian fertilization (1994) The Physiology of Reproduction, pp. 189-317. , Knobil E, Neill J, editors: New York: Raven Press
  • Yoshitani, N., Mori, E., Takasaki, S., Detection of carbohydrate recognition molecules on the plasma membrane of boar sperm by dextran-based multivalent oligosaccharide probes (2001) Glycobiology, 11, pp. 313-320
  • Zaneveld, L.J.D., Polakoski, K.L., Robertson, R.T., Williams, W.L., Trypsin inhibitors and fertilization (1971) Proceedings of the First International Conference on Proteinase Inhibitors, pp. 236-244. , Berlin: Walter de Gruyter
  • Zhang, X., Lou, Y.H., Koopman, M., Doggett, T., Tung, K.S., Curtiss, R., Antibody responses and infertility in mice following oral immunization with attenuated Salmonella typhimurium expressing recombinant murine ZP3 (1997) Biol Reprod, 56, pp. 33-41

Citas:

---------- APA ----------
Cesari, A., Sánchez, J.J., Biancotti, J.C., Vazquez-Levin, M.H., Kaiser, G., Palma, G.A., Alberio, R.,..., Fornés, M.W. (2004) . Immunolocalization of bovine sperm protease BSp120 by light and electron microscopy during capacitation and the acrosome reaction: Its role in in vitro fertilization. Molecular Reproduction and Development, 69(4), 411-418.
http://dx.doi.org/10.1002/mrd.20100
---------- CHICAGO ----------
Cesari, A., Sánchez, J.J., Biancotti, J.C., Vazquez-Levin, M.H., Kaiser, G., Palma, G.A., et al. "Immunolocalization of bovine sperm protease BSp120 by light and electron microscopy during capacitation and the acrosome reaction: Its role in in vitro fertilization" . Molecular Reproduction and Development 69, no. 4 (2004) : 411-418.
http://dx.doi.org/10.1002/mrd.20100
---------- MLA ----------
Cesari, A., Sánchez, J.J., Biancotti, J.C., Vazquez-Levin, M.H., Kaiser, G., Palma, G.A., et al. "Immunolocalization of bovine sperm protease BSp120 by light and electron microscopy during capacitation and the acrosome reaction: Its role in in vitro fertilization" . Molecular Reproduction and Development, vol. 69, no. 4, 2004, pp. 411-418.
http://dx.doi.org/10.1002/mrd.20100
---------- VANCOUVER ----------
Cesari, A., Sánchez, J.J., Biancotti, J.C., Vazquez-Levin, M.H., Kaiser, G., Palma, G.A., et al. Immunolocalization of bovine sperm protease BSp120 by light and electron microscopy during capacitation and the acrosome reaction: Its role in in vitro fertilization. Mol. Reprod. Dev. 2004;69(4):411-418.
http://dx.doi.org/10.1002/mrd.20100