Differential Decondensation of Class I (Rat) and Class II (Mouse) Spermatozoa Nuclei by Physiological Concentrations of Heparin and Glutathione

References

• Allen M J, Lee C, Lee J D, Pogany G C, Balloch M, Siekhaus W J, Balhorn R. Atomic force microscopy of mammalian sperm chromatin. Chromosoma 1993; 102: 623–630
   PubMed Web of Science ®Google Scholar
• Bellini M B, Ax R L. Purification of glycosaminoglycans from bovine follicular fluid. J Dairy Sci 1987; 70: 1913–1919
   PubMedGoogle Scholar
• Calvin H I. Comparative analysis of the nuclear basic proteins in rat, human, guinea pig, mouse and rabbit spermatozoa. Biochim Biophys Acta 1976; 434: 377–389
   PubMed Web of Science ®Google Scholar
• Carranco A, Reyes R, Magdaleno V M, Huacuja L, Hernandez O, Rosado A, Merchant H, Delgado N M. Heparin induced nuclei decondensation of mammalian epididymal spermatozoa. Arch Androl 1983; 10: 213–218
   PubMed Web of Science ®Google Scholar
• Delgado N M, Huacuja L, Merchant H, Reyes R, Rosado A. Species specific decondensation of human spermatozoa nuclei by heparin. Arch Androl 1980; 4: 305–313
   PubMed Web of Science ®Google Scholar
• Delgado N M, Reyes R, Huacuja L, Carranco A, Merchant H, Rosado A. Decondensation of human sperm nuclei by glycosaminoglycans sulfate from sea urchin egg. J Exp Zool 1982; 224: 457–460
   PubMedGoogle Scholar
• Gall W E, Ohsumi Y. Decondensation of sperm nuclei in vitro. Exp Cell Res 1976; 102: 349–358
   PubMed Web of Science ®Google Scholar
• Gebaver H, Linder H E, Amsterdam A. Synthesis of heparin like glycosaminoglycans in rat ovarian slices. Biol Reprod 1978; 18: 350–358
   PubMedGoogle Scholar
• Hernández O, Bello M A, Rosado A. The human spermatozoa genome analysis by DNA reassociation kinetics. Biochim Biophys Acta 1977; 521: 557–565
   Google Scholar
• Jager S, Wijchman J, Kremer J. Studies on the decondensation of human, mouse and bull sperm nuclei by heparin and other polyanions. J Exp Zool 1990; 256: 317–322
   Google Scholar
• Keyhani E, Storey B T. Energy conservation capacity and morphological integrity of mitochondria in hypotonically treated rabbit epididymal spermatozoa. Biochim Biophys Acta 1973; 305: 557–569
   PubMed Web of Science ®Google Scholar
• Koehler J K, Wurchmidt U, Larsen M P. Nuclear and chromatin structure in rat spermatozoa. Gamete Res 1983; 8: 357–370
   Google Scholar
• Roller C A, Kohli V. Purification of genoma DNA using heparin to remove nuclear proteins. Nucleic Acid Res 1993; 21: 2952
   PubMedGoogle Scholar
• Kvist U, Eliasson R. Influence of seminal plasma on the chromatin stability of ejaculated human spermatozoa. Int J Androl 1980; 3: 130–142
   PubMedGoogle Scholar
• Luft J H. Improvements in epoxy resin embedding methods. J Biophys Biochem Cytol 1961; 9: 409–414
   PubMedGoogle Scholar
• Mahi C A, Yanagimachi R. Induction of nuclear decondensation of mammalian spermatozoa in vitro. J Reprod Fertil 1975; 44: 293–296
   PubMedGoogle Scholar
• Marushige Y, Marushige K. Enzymatic unpacking of bull sperm chromatin. Biochim Biophys Acta 1975; 403: 180–191
   PubMed Web of Science ®Google Scholar
• Perreault S D, Barbee R R, Elstein K H, Zucker R M, Reefer C L. Interspecies differences in the stability of mammalian sperm nuclei assessed in vivo by sperm microinjection and in vitro by flow cytometry. Biol Reprod 1988; 39: 157–167
   PubMed Web of Science ®Google Scholar
• Perreault S D, Barbee R R, Slott V L. Importance of glutathione in the acquisition and maintenance of sperm: Nuclear decondensing activity in maturing hamster oocytes. Dev Biol 1988; 125: 181–186
   PubMedGoogle Scholar
• Reyes R, Carranco A, Hernández O, Rosado A, Merchant H, Delgado N M. Glycosaminoglycans-sulfate as acrosomal reaction-inducing factor of follicular fluid. Arch Androl 1984; 12: 203–209
   PubMed Web of Science ®Google Scholar
• Reyes R, Carranco A, Huacuja L, Delgado N M. Male pronuclei formation release of phosphorylation of histone H-3 during decondensation of human sperm nuclei activated in vitro by heparin. Arch Androl 1991; 26: 53–60
   PubMed Web of Science ®Google Scholar
• Reyes R, Rosado A, Hernández O, Delgado N M. Heparin and glutathione: physiological decondensing agents of human sperm nuclei. Gamete Res 1989; 23: 39–47
   PubMedGoogle Scholar
• Reynolds E S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol 1963; 17: 208–212
   PubMed Web of Science ®Google Scholar
• Sipski M L, Wagner T E. The total structure and organization of chromosomal fibers in eutherian sperm nuclei. Biol Reprod 1977; 16: 428–440
   PubMed Web of Science ®Google Scholar
• Swan M A. A method for reactivation of the movement of demembranated ram sperm models with decondensed nuclei and a description of their ultrastructure. Biol Reprod 1993; 48: 987–997
   PubMedGoogle Scholar
• Tadano Y, Yamada K. The histochemistry of complex carbohydrates in the ovarian follicles of adult mice. Histochemistry 1978; 57: 203–215
   PubMedGoogle Scholar
• Tesarik J, Kopecny V. Development of human male pronucleus: ultrastructure and timing. Gamete Res 1989; 24: 135–149
   PubMedGoogle Scholar
• Thibault C, Gérard M. Cytoplasmatic and nuclear maturation of rabbit oocytes in vitro. Ann Biol Anim Biochim Biophys 1973; 13: 145–156
   Google Scholar
• Valencia A, Wens M A, Merchant H, Reyes R, Delgado N M. Capacitation of human spermatozoa by heparin. Arch Androl (Suppl) 1984; 12: 109–113
   PubMedGoogle Scholar
• Yanagimachi R. Mechanism of fertilization in mammals. Fertilization and Embryonic Development in Vitro, L Mastroiani, Jr., J D Biggers. Plenum, New York 1981; 81–182
   Google Scholar
• Yanagimachi R. Mammalian fertilization. Physiology of Reproduction, E Knobil, J D Neill. Raven, New York 1994; Vol. 1: A189–A317
   Google Scholar
• Yoshida M. Role of glutathione in the maturation and fertilization of pig oocytes in vitro. Mol Reprod Development 1993; 35: 76–81
   PubMedGoogle Scholar
• Zetterqvist H. The ultrastructural organization of the columnar absorbing cells of the mouse jejunum. Thesis, Karolinska Institute, Stockholm 1956
   Google Scholar
• Zirkin B R, Chang T SK. Involvement of endogenous proteolytic activity in thiol-induced release of DNA template restrictions in rabbit sperm nuclei. Biol Reprod 1977; 17: 131–137
   PubMedGoogle Scholar
• Zirkin B R, Soucek D A, Chang T SK, Perreauit S D. In vitro and in vivo studies of mammalian sperm nuclear decondensation. Gamete Res 1985; 11: 349–365
   Google Scholar