AÇÃO DAS ESPÉCIES REATIVAS DE OXIGÊNIO NOS ESPERMATOZOIDES
Keywords:
free radicals, , oxidative stress, sperm cellsAbstract
So that spermatozoa can perform functions and achieve the goal that is fertilization, require
energy from adenosine triphosphate (ATP). During the energy metabolism is stored in the
form of high-energy electrons that are directed to the electron transport chain, comprised of
five supramolecular protein. In this process, there is the formation of a semiquinone anion
(Q¯) an intermediate radical that is eventually able to transfer this unpaired electron to O2 and
form reactive oxygen species,as the main superoxide, hydrogen peroxide and hydroxyl
radical. These molecules are highly reactive and sperm trigger processes that lead to
degradation and decrease in cell quality. However these same molecules that are often
considered great villains, also participate in mechanisms that culminate in fertilization and
zygote formation, thus acquiring great importance. With the advent of semen
cryopreservation and oxidative stress associated with the processing, reactive oxygen species
entered into evidence in the research, making it necessary to study its action and ways to
reduce oxidative stress.
References
Watson PF. The cause of reduced fertility with cryopreserved sêmen. Animal Reproduction Science. 2000; 60:481-492.
Andrade ER, Melo-Sterza FA, Seneda MM, Alfieri AA. Consequências da produção das espécies reativas de oxigênio na reprodução e principais mecanismos antioxidantes. Revista Brasileira de Reprodução Animal. 2010;34(2):79-85.
Lamirande DE, Jiang H, Zini A, Kodama H, Gagnon C. Reactive oxygen species and sperm physiology. Journal of Reproduction and Fertility. 1997;2:48-54.
Baumber J, Ball BA, Gravance CG, Medina V, Davies-Morel MCG. The effect of reactive oxygen species on equine sperm motility, viability, acrosomal integrity, mitochondrial membrane potential and membrane lipid peroxidation. Journal of Andrology. 2000;21:895-902.
Kothari S, Thompson A, Agarwal A, Du Plessis SS. Free radicals: their beneficial and detrimental effects on sperm function. Indian Journal of Experimental Biology. 2010;48:425-435.
Varner DDD, Gibb Z, Aitken RJ. Stallion fertility: a focus on the spermatozoon. Equine Veterinary Journal. 2015;47:16-24.
Varner D, Johnson L. From a sperm’s view – revisiting our perception of this intriguing cell. AEEP Proceedings. 2007;53:104-177.
Brito LFC. evaluation of stallion sperm morphology. Clinical Techniques in Equine Practice. 2007;6:249-264.
Toshimori K, Ito C. Formation and organization of the mammalian sperm head. Archives Histology Cytology. 2003;66(5):383-396.
Miller D, Brinkworth M, Iles D. Paternal dna packaging in spermatozoa: more than the sum of its parts? Dna, histones, protamines and epigenetics. Reproduction. 2010;139(2):287-301.
Braun RE. packaging paternal chromosomes with protamine. Nature Genetics. 2001;28:10-12.
Hermo L, Pelletier RM, Cyr DG, Smith CE. Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 2: changes in spermatid organelles associated with development of spermatozoa. Microscopy Research and Technique. 2010;73:279-319.
Komarek RJ, Pickett BW, Gibson EW, Lanz RN. Composition of lipids in stallion semen. Journal of Reproduction and Fertility. 1965;10:337-342.
Gadella BM, Rathi R, Brouwers JFHM, Stout TAE, Colenbrander B. Capacitation and the acrosome reaction in equine sperm. Animal Reproduction Science. 2001;68:249-265.
Ruiz‐Pesini E, Díez‐Sánchez C, López‐Pérez MJ, Enríquez JA. The role of the mitochondrion in sperm function: is there a place for oxidative phosphorylation or is this a purely glycolytic process? Current Topics in Developmental Biology. 2007;77:3-19.
Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P. Biologia molecular da célula. 5.ed. Porto alegre: Artmed; 2010. p.1396.
Nelson DL, Cox MM. Lehninger princípios da bioquímica. 6.ed. Porto alegre: Artmed; 2014. p.1298.
Champe PC, Harvey RA, Ferrier DR. Bioquímica ilustrada. 3. Ed. Porto alegre: Artmed; 2006. p.534.
Finkel T, Holbrook NJ. oxidants, oxidative stress and the biology of ageing. Nature. 2000;408:239-247.
Raha S, Robinson BH. mitochondria, oxygen free radicals, disease and ageing. Trends in Biochemical Sciences. 2000;25:502-508.
Kussmaul L, Hirst J. The mechanism of superoxide production by nadh:ubiquinone oxidoreductase (complex i) from bovine heart mitochondria. Proceedings of the National Academy of Sciences. 2006;103:7607-7612.
Herrero A, Barja G. Localization of the site of oxygen radical generation inside the complex i of heart and nonsynaptic brain mammalian mitochondria. Journal of Bioenergetics and Biomembranes. 2000;32:609-615.
Turrens JF. mitochondrial formation of reactive oxygen species. The Journal of Physiology. 2003;552:335-344.
Pryde KR, Hirst J. Superoxide is produced by the reduced flavin in mitochondrial complex i: a single, unified mechanism that applies during both forward and reverse electron transfer. The Journal of Biological Chemistry. 2011;286:18056-18065.
Quilan CL, Orr AL, Perevoshchikova IV, Treberg JR, Ackrell BA, Brand MD. mitochondrial complex ii can generate reactive oxygen species at high rates in both the forward and reverse reactions. The Journal of Biological Chemistry. 2012;287:27255-27264.
Bertram r, Gram PM, Luciani DS, Sherman A. A simplified model for mitochondrial ATP production. Journal of Theoretical Biology. 2006;243:575-586.
Capaldi RA. Arrangement of proteins in the mitochondrial inner membrane. Biochimica et Biophysica Acta. 1982;694:292-306.
Sikka SC. Relative impact of oxidative stress on male reproductive function. Current Medical Chemistry. 2001;8:851-862.
Agarwal A, Said TM. Oxidative stress, dna damage and apoptosis in male infertility: a clinical approach. BJU International. 2005;95:503–507.
Nogueira BG, Bitencourt JL, Sampaio BFB, Bender ESC, Costa e Silva EV, Zúccari CESN. Peroxidação lipídica e agentes antioxidantes no sêmen de mamíferos. Revista Electrónica de Veterinaria. 2013;15:1-15.
Ferreira ALA, Matsubara LS. Radicais livres: conceitos, doenças relacionadas, sistemas de defesa e estresse oxidativo. Revista da Associação Médica Brasileira. 1997;43:61-68.
Venditti P, Di Stefano L, Di Meo S. Mitochondrial metabolism of reactive oxygen species. Mitochondrion. 2013;13:71-82.
Pryor WA. Oxy–radicals and related species: their formation, lifetimes and reactions. Annual review of physiology. 1986;48:657-667.
Liochev SI, Fridovich I. Superoxide and iron: partners in crime. International Union of Biochemistry and Molecular Biology Life. 1999;48:157-161.
Ford WCL. regulation of sperm function by reactive oxygen species. Human Reproduction Update. 2004;10:387-399.
Aitken RJ, Clarkson JS, Fisel S. Generation of reactive oxygen species, lipid peroxidation, and human sperm function. Biology of Reproduction. 1989;40:183-197.
Jonge CD. Biological basis for human capacitation. Human Reproduction Update. 2005;11(3):205-214.
Ho HC, Suarez SS. Hyperactivation of mammalian spermatozoa: function and regulation. Reproduction. 2001;122:519-526.
Florman HM, Jungnickel MK, Sutton KA. Regulating the acrosome reaction. The International Journal of Developmental Biology. 2008;52:503-510.
Flesch FM, Gadella BM. Dynamics of the mammalian sperm plasma membrane in the process of fertilization. Biochimica et Biophysica Acta. 2000;1469:197-235.
Naz RK, Rajesh PB. Role of tyrosine phosphorylation in sperm capacitation/ acrosome reaction. Reproductive Biology and Endocrinology. 2004;2(75):1-12.
Florman HM, Corron M, Kim TDH, Babcock D. Activation of voltage-dependent calcium channels of mammalian sperm is required for zona pellucida-induced acrosomal exocytosis. Developmental Biology. 1992;152:304-314.
Nishigaki T, José O, González-Cota AL, Romero F, Treviño CL, Darszon A. Intracellular pH in sperm physiology. Biochemical and Biophysical Research. 2014;450:1149-158.
Pawson T. Specificity in signal transduction: from phosphotyrosine-sh2 domain interactions to complex cellular systems. Cell. 2004;116:191-203.
O’Flaherty CM, Beorlegui NB, Beconi MT. Reactive oxygen species requirements for bovine sperm capacitation and acrosome reaction. Theriogenology. 1999;52:289-301.
Aitken RJ, Paterson M, Fisher H, Buckingham DW, Van Duin M. Redox regulation of tyrosine phosphorylation in human spermatozoa and its role in the control of human sperm function. Journal of Cell Science. 1995;108:2017-2025.
Leclerc P, De Lamirande E, Gagnon C. Regulation of protein-tyrosine phosphorylation and human sperm capacitation by reactive oxygen derivatives. Free Radical Biology and Medicine. 1997;22:643-656.
O’Flaherty C, De Lamirande E, Gagnon C. Positive role of reactive oxygen species in mammalian sperm capacitation: triggering and modulation of phosphorylation events. Free Radical Biology and Medicine. 2006;41:528-540.
Cohen N, Lubart R, Rubinstein S, Breitbart H. Light irradiation of mouse spermatozoa: stimulation of in vitro fertilization and calcium signals. Photochemistry and Photobiology. 1998;68:407-413.
Tremellen K. Oxidative stress and male infertility—a clinical perspective. Human Reproduction Update. 2008;14(3):243-258.
El-Beltagi HS, Mohamed HI. Reactive oxygen species, lipid peroxidation and antioxidative defense mechanism. Notulae Botanicae Horti Agrobotanici Cluj-Napoca. 2013;41(1):44-57.
Repetto MG, Ferrarotti NF, Boveris A. The involvement of transition metal ions on iron-dependent lipid peroxidation. Archives of Toxicology. 2010;84:255-262.
Gardner HW. oxygen radical chemistry of polyunsaturated fatty acids. Free Radical Biology and Medicine. 1989;7:65-86.
Halliwell B. Oxidative stress and neurodegeneration. Where are we now? Journal of Neurochemistry. 2006;97:1634-1658.
Catala A. An overview of lipid peroxidation with emphasis in outer segments of photoreceptors and the chemiluminescence assay. The International Journal of Biochemistry and Cell Biology. 2006;38:1482-1495.
Storey BT. biochemistry of the induction and prevention of lipoperoxidative damage in human spermatozoa. Molecular Human Reproduction. 1997;3:203-213.
Aitken RJ, Lambourne S, Gibb Z. The john hughes memorial lecture: aspects of sperm physiologyd oxidative stress and the functionality of stallion spermatozoa. Journal of Equine Veterinary Science. 2014;34:17–27.
De Lamirande E, Gagnon C. Human sperm hyperactivation and capacitation as parts of an oxidative process. Free Radical Biology and Medicine. 1993;14:157-166.
Li Y, Huang TT, Carlson EJ, Melov S, Ursell PC, Olson JL, Noble LJ, Yoshimura MP, Berger C, Chan PH, Wallace DC, Epstein CJ. dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nature Genetics. 1995;11:376-381.
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