Polyamines modulate mouse sperm motility

References

• Aitken RJ, Nixon B. 2013. Sperm capacitation: a distant landscape glimpsed but unexplored. Mol Hum Reprod. 19(12):785–793. doi:10.1093/molehr/gat067.
   PubMed Web of Science ®Google Scholar
• Balbach M, Ghanem L, Rossetti T, Kaur N, Ritagliati C, Ferreira J, Krapf D, Puga Molina LC, Santi CM, Hansen JN, et al. 2021. Soluble adenylyl cyclase inhibition prevents human sperm functions essential for fertilization. Mol Hum Reprod. 27(9):gaab054. doi:10.1093/molehr/gaab054.
   PubMed Web of Science ®Google Scholar
• Battistone MA, Da Ros VG, Salicioni AM, Navarrete FA, Krapf D, Visconti PE, Cuasnicú PS. 2013. Functional human sperm capacitation requires both bicarbonate-dependent PKA activation and down-regulation of Ser/Thr phosphatases by Src family kinases. Mol Hum Reprod. 19(9):570–580. doi:10.1093/molehr/gat033.
   PubMed Web of Science ®Google Scholar
• Buffone MG, Wertheimer EV, Visconti PE, Krapf D. 2014. Central role of soluble adenylyl cyclase and cAMP in sperm physiology. Biochim Biophys Acta. 1842(12 Pt B):2610–2620. doi:10.1016/j.bbadis.2014.07.013.
   PubMed Web of Science ®Google Scholar
• Casillas ER, Elder CM, Hoskins DD. 1980. Adenylate cyclase activity of bovine spermatozoa during maturation in the epididymis and the activation of sperm particulate adenylate cyclase by GTP and polyamines. J Reprod Fertil. 59(2):297–302. doi:10.1530/jrf.0.0590297.
   PubMedGoogle Scholar
• Chakraborty S, Saha S. 2022. Understanding sperm motility mechanisms and the implication of sperm surface molecules in promoting motility. Middle East Fertil Soc J. 27(1):4. doi:10.1186/s43043-022-00094-7.
   Web of Science ®Google Scholar
• Chiarante N, Alonso CAI, Plaza J, Lottero-Leconte R, Arroyo-Salvo C, Yaneff A, Osycka-Salut CE, Davio C, Miragaya M, Perez-Martinez S. 2020. Cyclic AMP efflux through MRP4 regulates actin dynamics signalling pathway and sperm motility in bovines. Sci Rep. 10(1):15619. doi:10.1038/s41598-020-72425-5.
   PubMed Web of Science ®Google Scholar
• Cordero-Martínez J, Flores-Alonso JC, Aguirre-Alvarado C, Oviedo N, Alcántara-Farfán V, García-Pérez CA, Bermúdez-Ruiz KF, Jiménez-Gutiérrez GE, Rodríguez-Páez L. 2020. Influence of Echeveria gibbiflora DC aqueous crude extract on mouse sperm energy metabolism and calcium-dependent channels. J Ethnopharmacol. 248:112321. doi:10.1016/j.jep.2019.112321.
   PubMed Web of Science ®Google Scholar
• Ded L, Sebkova N, Cerna M, Elzeinova F, Dostalova P, Peknicova J, Dvorakova-Hortova K. 2013. In vivo exposure to 17β-estradiol triggers premature sperm capacitation in cauda epididymis. Reproduction. 145(3):255–263. doi:10.1530/REP-12-0472.
   PubMed Web of Science ®Google Scholar
• Delgado-Bermúdez A, Yeste M, Bonet S, Pinart E. 2022. A review on the role of bicarbonate and proton transporters during sperm capacitation in mammals. Int J Mol Sci. 23(11):6333. doi:10.3390/ijms23116333
   PubMed Web of Science ®Google Scholar
• Dey S, Roy D, Majumder GC, Mukherjee B, Bhattacharyya D. 2015. Role of forward-motility-stimulating factor as an extracellular activator of soluble adenylyl cyclase. Mol Reprod Dev. 82(12):1001–1014. doi:10.1002/mrd.22586.
   PubMed Web of Science ®Google Scholar
• Escoffier J, Krapf D, Navarrete F, Darszon A, Visconti PE. 2012. Flow cytometry analysis reveals a decrease in intracellular sodium during sperm capacitation. J Cell Sci. 125(Pt 2):473–485. doi:10.1242/jcs.093344.
   PubMed Web of Science ®Google Scholar
• Granados-Gonzalez G, Mendoza-Lujambio I, Rodriguez E, Galindo BE, Beltrán C, Darszon A. 2005. Identification of voltage-dependent Ca2+ channels in sea urchin sperm. FEBS Lett. 579(29):6667–6672. doi:10.1016/j.febslet.2005.10.035.
   PubMed Web of Science ®Google Scholar
• Harayama H. 2013. Roles of intracellular cyclic AMP signal transduction in the capacitation and subsequent hyperactivation of mouse and boar spermatozoa. J Reprod Dev. 59(5):421–430. doi:10.1262/jrd.2013-056.
   PubMed Web of Science ®Google Scholar
• Hess KC, Jones BH, Marquez B, Chen Y, Ord TS, Kamenetsky M, Miyamoto C, Zippin JH, Kopf GS, Suarez SS, et al. 2005. The "soluble" adenylyl cyclase in sperm mediates multiple signaling events required for fertilization. Dev Cell. 9(2):249–259. doi:10.1016/j.devcel.2005.06.007.
   PubMed Web of Science ®Google Scholar
• Hidalgo DM, Romarowski A, Gervasi MG, Navarrete F, Balbach M, Salicioni AM, Levin LR, Buck J, Visconti PE. 2020. Capacitation increases glucose consumption in murine sperm. Molecular Reproduction Devel. 87(10):1037–1047. doi:10.1002/mrd.23421.
   PubMed Web of Science ®Google Scholar
• Jakobsen E, Lange SC, Andersen JV, Desler C, Kihl HF, Hohnholt MC, Stridh MH, Rasmussen LJ, Waagepetersen HS, Bak LK. 2018. The inhibitors of soluble adenylate cyclase 2-OHE, KH7, and bithionol compromise mitochondrial ATP production by distinct mechanisms. Biochem Pharmacol. 155:92–101. doi:10.1016/j.bcp.2018.06.023.
   PubMed Web of Science ®Google Scholar
• Jakobsen H, Rui H, Thomassen Y, Hald T, Purvis K. 1989. Polyamines and other accessory sex gland secretions in human seminal plasma 8 years after vasectomy. J Reprod Fertil. 87(1):39–45.
   PubMedGoogle Scholar
• Jeffree GM. 1956. The maintenance of prostatic acid phosphatase activity by proteins and polyamines. Biochim Biophys Acta. 20(3):503–513.
   PubMedGoogle Scholar
• Jumper J, Evans R, Pritzel A, Green T, Figurnov M, Ronneberger O, Tunyasuvunakool K, Bates R, Žídek A, Potapenko A, et al. 2021. Highly accurate protein structure prediction with AlphaFold. Nature. 596(7873):583–589. doi:10.1038/s41586-021-03819-2.
   PubMed Web of Science ®Google Scholar
• Koo BH, Hong D, Hong HD, Lim HK, Hoe KL, Won MH, Kim YM, Berkowitz DE, Ryoo S. 2019. Arginase II activity regulates cytosolic Ca(2+) level in a p32-dependent manner that contributes to Ca(2+)-dependent vasoconstriction in native low-density lipoprotein-stimulated vascular smooth muscle cells. Exp Mol Med. 51(6):1–12.
   Google Scholar
• Laskowski RA, Swindells MB. 2011. LigPlot+: multiple ligand-protein interaction diagrams for drug discovery. J Chem Inf Model. 51(10):2778–2786. doi:10.1021/ci200227u.
   PubMed Web of Science ®Google Scholar
• Lefèvre PL, Palin MF, Murphy BD. 2011. Polyamines on the reproductive landscape. Endocr Rev. 32(5):694–712. doi:10.1210/er.2011-0012.
   PubMed Web of Science ®Google Scholar
• Lenis YY, Elmetwally MA, Maldonado-Estrada JG, Bazer FW. 2017. Physiological importance of polyamines. Zygote. 25(3):244–255. doi:10.1017/S0967199417000120.
   PubMed Web of Science ®Google Scholar
• Li R, Wu X, Zhu Z, Lv Y, Zheng Y, Lu H, Zhou K, Wu D, Zeng W, Dong W, et al. 2022. Polyamines protect boar sperm from oxidative stress in vitro. J Anim Sci. 100(4)
   Web of Science ®Google Scholar
• Mann T, Lutwak-Mann C. 1981. Secretory function of the prostate, seminal vesicle, Cowper’s gland and other accessory organs of reproduction. In: Mann T, Lutwak-Mann C, editors. Male reproductive function and semen: themes and trends in physiology, biochemistry and investigative andrology. London: Springer London; p. 171–193.
   Google Scholar
• Melendrez CS, Ruttle JL, Hallford DM, Chaudhry PS, Casillas ER. 1992. Polyamines in ejaculated ram spermatozoa and their relationship with sperm motility. J Androl. 13(4):293–296.
   PubMedGoogle Scholar
• Michael AJ. 2016. Biosynthesis of polyamines and polyamine-containing molecules. Biochem J. 473(15):2315–2329. doi:10.1042/BCJ20160185.
   PubMedGoogle Scholar
• Morales ME, Rico G, Bravo C, Tapia R, Alvarez C, Méndez JD. 2003. Progressive motility increase caused by L-arginine and polyamines in sperm from patients with idiopathic and diabetic asthenozoospermia. Ginecol Obstet Mex. 71:297–303.
   PubMedGoogle Scholar
• Morgan DM. 1999. Polyamines. An overview. Mol Biotechnol. 11(3):229–250. doi:10.1007/BF02788682.
   PubMed Web of Science ®Google Scholar
• Morris GM, Huey R, Lindstrom W, Sanner MF, Belew RK, Goodsell DS, Olson AJ. 2009. AutoDock4 and AutoDockTools4: automated docking with selective receptor flexibility. J Comput Chem. 30(16):2785–2791. doi:10.1002/jcc.21256.
   PubMed Web of Science ®Google Scholar
• Nowicka-Bauer K, Szymczak-Cendlak M. 2021. Structure and function of ion channels regulating sperm motility-an overview. Int J Mol Sci. 22(6):3259. doi:10.3390/ijms22063259
   PubMed Web of Science ®Google Scholar
• Pegg AE. 2016. Functions of polyamines in mammals. J Biol Chem. 291(29):14904–14912. doi:10.1074/jbc.R116.731661.
   PubMed Web of Science ®Google Scholar
• Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE. 2004. UCSF Chimera–a visualization system for exploratory research and analysis. J Comput Chem. 25(13):1605–1612. doi:10.1002/jcc.20084.
   PubMed Web of Science ®Google Scholar
• Pietrobon EO, Domínguez LA, Vincenti AE, Burgos MH, Fornés MW. 2001. Detection of the mouse acrosome reaction by acid phosphatase. Comparison with chlortetracycline and electron microscopy. J Androl. 22(1):96–103.
   PubMedGoogle Scholar
• Plant TM, Zeleznik A, Albertini DF, Goodman RL, Herbison A, McCarthy M, Muglia LJ, Richards JS. 2014. Knobil and Neill’s physiology of reproduction: two-volume set. Vol. 1; p. 1–2550.
   Google Scholar
• Rodríguez-Páez L, Aguirre-Alvarado C, Oviedo N, Alcántara-Farfán V, Lara-Ramírez EE, Jimenez-Gutierrez GE, Cordero-Martínez J. 2021. Polyamines influence mouse sperm channels activity. Int J Mol Sci. 22(1)
   PubMed Web of Science ®Google Scholar
• Rubinstein S, Breitbart H. 1991. Role of spermine in mammalian sperm capacitation and acrosome reaction. Biochem J. 278(Pt 1):25–28. doi:10.1042/bj2780025.
   PubMedGoogle Scholar
• Rubinstein S, Lax Y, Shalev Y, Breitbart H. 1995. Dual effect of spermine on acrosomal exocytosis in capacitated bovine spermatozoa. Biochim Biophys Acta. 1266(2):196–200. doi:10.1016/0167-4889(95)00007-f.
   PubMed Web of Science ®Google Scholar
• Santi CM, Martínez-López P, de la Vega-Beltrán JL, Butler A, Alisio A, Darszon A, Salkoff L. 2010. The SLO3 sperm-specific potassium channel plays a vital role in male fertility. FEBS Lett. 584(5):1041–1046. doi:10.1016/j.febslet.2010.02.005.
   PubMed Web of Science ®Google Scholar
• Schlingmann K, Michaut MA, McElwee JL, Wolff CA, Travis AJ, Turner RM. 2007. Calmodulin and CaMKII in the sperm principal piece: evidence for a motility-related calcium/calmodulin pathway. J Androl. 28(5):706–716. doi:10.2164/jandrol.106.001669.
   PubMedGoogle Scholar
• Shah GV, Sheth AR, Mugatwala PP, Rao SS. 1975. Effect of spermine on adenyl cyclase activity of spermatozoa. Experientia. 31(6):631–632. doi:10.1007/BF01944596.
   PubMedGoogle Scholar
• Shi QX, Yuan YY, Friend DS, Marton LJ. 1992. Effect of spermine on sperm capacitation of guinea pig in vitro. Arch Androl. 29(1):33–42. doi:10.3109/01485019208987706.
   PubMed Web of Science ®Google Scholar
• Suarez SS, Pacey AA. 2006. Sperm transport in the female reproductive tract. Hum Reprod Update. 12(1):23–37. doi:10.1093/humupd/dmi047.
   PubMed Web of Science ®Google Scholar
• Suarez SS, Wolfner MF. 2017. Seminal plasma plays important roles in fertility. In: De Jonge CJ and Barratt CLR, editors. The sperm cell: production, maturation, fertilization, regeneration. Cambridge: Cambridge University Press; p. 88–108.
   Google Scholar
• Swaminathan PD, Purohit A, Hund TJ, Anderson ME. 2012. Calmodulin-dependent protein kinase II: linking heart failure and arrhythmias. Circ Res. 110(12):1661–1677. doi:10.1161/CIRCRESAHA.111.243956.
   PubMed Web of Science ®Google Scholar
• Tabor CW, Rosenthal SM. 1956. Pharmacology of spermine and spermidine; some effects on animals and bacteria. J Pharmacol Exp Ther. 116(2):139–155.
   PubMed Web of Science ®Google Scholar
• Tabor H, Tabor CW. 1964. Spermidine, spermine, and related amines. Pharmacol Rev. 16:245–300.
   PubMed Web of Science ®Google Scholar
• Trott O, Olson AJ. 2010. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem. 31(2):455–461. doi:10.1002/jcc.21334.
   PubMed Web of Science ®Google Scholar
• Uemura T, Yerushalmi HF, Tsaprailis G, Stringer DE, Pastorian KE, Hawel L, 3rd, Byus CV, Gerner EW. 2008. Identification and characterization of a diamine exporter in colon epithelial cells. J Biol Chem. 283(39):26428–26435. doi:10.1074/jbc.M804714200.
   PubMed Web of Science ®Google Scholar
• Wertheimer E, Krapf D, de la Vega-Beltran JL, Sánchez-Cárdenas C, Navarrete F, Haddad D, Escoffier J, Salicioni AM, Levin LR, Buck J, et al. 2013. Compartmentalization of distinct cAMP signaling pathways in mammalian sperm. J Biol Chem. 288(49):35307–35320. doi:10.1074/jbc.M113.489476.
   PubMed Web of Science ®Google Scholar
• Williams K. 1997. Interactions of polyamines with ion channels. Biochem J. 325(Pt 2):289–297. doi:10.1042/bj3250289.
   PubMedGoogle Scholar