Evaluation of ubiquitination and sumoylation of acrosin inhibitor during in vitro capacitation of porcine sperm

References

• Uhrin P, Dewerchin M, Hilpert M, et al. Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male infertility. J Clin Invest. 2000; 106(12):1531–1539.
   PubMed Web of Science ®Google Scholar
• Charron M, Wright WW. Proteases and protease inhibitors of the serine and metalloprotease subclasses, in testicular physiology - sciencedirect. Sertoli Cell Biology. 2005; 121–152.
   Google Scholar
• Schill WB, Heimburger N, Schiessler H, et al. Reversible attachment and localization of the acid-stable seminal plasma acrosin-trypsin inhibitor on boar sperm as revealed by the indirect immunofluorescent staining technique. Hoppe Seylers Zeitschrift Für Physiologische Chemie. 1975; 356(9):1473–1476.
   PubMedGoogle Scholar
• Nayernia K, Adham I, Kremling H, et al. Stage and developmental specific gene expression during mammalian spermatogenesis. Int J Dev Biol. 1996; 40(1):379–383.
   PubMed Web of Science ®Google Scholar
• Swegen A, Smith ND, Gibb Z, et al. The serine protease testisin is present on the surface of capacitated stallion spermatozoa and interacts with key zona pellucida binding proteins. Andrology. 2019; 7(2):199–212.
   PubMed Web of Science ®Google Scholar
• Kwon WS, Rahman M, Lee JS, et al. A comprehensive proteomic approach to identifying capacitation related proteins in boar spermatozoa. BMC Genomics. 2014; 15(1):897.
   PubMedGoogle Scholar
• Zigo M, Postlerova P, Jonakova V, et al. Ubiquitin-proteasome system (UPS) regulates spermadhesin release during boar sperm capacitation. Animal Reproduction Science. 2018; 194:e17.
   Web of Science ®Google Scholar
• Kerns K, Morales P, Sutovsky P. Regulation of sperm capacitation by the 26S proteasome: an emerging new paradigm in spermatology. Biol Reprod. 2016; 94(5):117.
   PubMed Web of Science ®Google Scholar
• Hay RT. SUMO: a history of modification. Mol Cell. 2005; 18(1):1–12.
   PubMed Web of Science ®Google Scholar
• Han ZJ, Feng YH, Gu BH, et al. The post-translational modification, SUMOylation, and cancer (Review). Int J Oncol. 2018; 52(4):1081–1094.
   PubMed Web of Science ®Google Scholar
• Psakhye I, Castellucci F, Branzei D. SUMO-chain-regulated proteasomal degradation timing exemplified in DNA replication initiation. Mol Cell. 2019; 76(4):632–645.
   PubMed Web of Science ®Google Scholar
• Haase H, Hebel S, Engelhardt G, et al. Flow cytometric measurement of labile zinc in peripheral blood mononuclear cells. Anal Biochem. 2006; 352(2):222–230.
   PubMed Web of Science ®Google Scholar
• Que EL, Duncan FE, Lee HC, et al. Bovine eggs release zinc in response to parthenogenetic and sperm-induced egg activation. Theriogenology. 2019;127:41–48.
   PubMed Web of Science ®Google Scholar
• Chan PJ, Corselli JU, Patton WC, et al. Enhanced fertility after heat-induced hyperactivation. Fertil Steril. 1998; 69(1):118–121.
   PubMed Web of Science ®Google Scholar
• Zapata-Carmona H, Barón L, Zuñiga LM, et al. The activation of the chymotrypsin-like activity of the proteasome is regulated by soluble adenyl cyclase/cAMP/protein kinase A pathway and required for human sperm capacitation. Molecular Human Reproduction. 2019; 25(10):587–600.
   PubMed Web of Science ®Google Scholar
• Rahman MS, Kwon WS, Pang MG. Prediction of male fertility using capacitation-associated proteins in spermatozoa. Mol Reprod Dev. 2017; 84(9):749–759.
   PubMed Web of Science ®Google Scholar
• Tardif S, Dubé C, Bailey JL. Porcine sperm capacitation and tyrosine kinase activity are dependent on bicarbonate and calcium but protein tyrosine phosphorylation is only associated with calcium. Biol Reprod. 2003; 68(1):207–213.
   PubMed Web of Science ®Google Scholar
• Urner F, Sakkas D. Protein phosphorylation in mammalian spermatozoa. Reproduction. 2003; 125(1):17–26.
   PubMed Web of Science ®Google Scholar
• Signorelli J, Diaz ES, Morales P. Kinases, phosphatases and proteases during sperm capacitation. Cell Tissue Res. 2012; 349(3):765–782.
   PubMed Web of Science ®Google Scholar
• Bravo MM, Aparicio IM, M Garcia-Herreros M, et al. Changes in tyrosine phosphorylation associated with true capacitation and capacitation-like state in boar spermatozoa. Mol Reprod Dev. 2005; 71(1):88–96.
   PubMed Web of Science ®Google Scholar
• Kerns K, Sharif M, Zigo M, et al. Sperm cohort-specific zinc signature acquisition and capacitation-induced zinc flux regulate sperm-oviduct and sperm-zona pellucida interactions. Int J Mol Sci. 2020; 21(6):2121.
   Web of Science ®Google Scholar
• Yi YJ, Manandhar G, Sutovsky M, et al. Inhibition of 19S proteasomal regulatory complex subunit PSMD8 increases polyspermy during porcine fertilization in vitro. J Reprod Immunol. 2010; 84(2):154–163.
   PubMed Web of Science ®Google Scholar
• Töpfer-Petersen E, Ekhlasi-Hundrieser M, Tsolova M. Glycobiology of fertilization in the pig. Int J Dev Biol. 2008; 52(5–6):717–736.
   PubMed Web of Science ®Google Scholar
• Zaneveld LJ, Robertson RT, Kessler M, et al. Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors. J Reprod Fertil. 1971; 25(3):387–392.
   PubMedGoogle Scholar
• Sanz L, Calvete JJ, Jonáková V, et al. Boar spermadhesins AQN-1 and AWN are sperm-associated acrosin inhibitor acceptor proteins. FEBS Letters. 1992; 300(1):63–66.
   PubMed Web of Science ®Google Scholar
• Jelı́nková P, Maňásková P, Tichá M, et al. Proteinase inhibitors in aggregated forms of boar seminal plasma proteins. Int J Biol Macromol. 2003;32(3–5):99–107. (
   PubMed Web of Science ®Google Scholar
• Manásková P, Liberda J, Tichá M, et al. Aggregated and monomeric forms of proteins in boar seminal plasma: characterization and binding properties. Folia Biol. 2000; 46(4):143–151.
   PubMed Web of Science ®Google Scholar
• Yi YJ, Zimmerman SW, Manandhar G, et al. Ubiquitin-activating enzyme (UBA1) is required for sperm capacitation, acrosomal exocytosis and sperm-egg coat penetration during porcine fertilization. Int J Androl. 2012; 35(2):196–210.
   PubMedGoogle Scholar
• Maňásková-Postlerová P, Cozlová N, Dorosh A, et al. Acrosin inhibitor detection along the boar epididymis. Int J Biol Macromol. 2016; 82:733–739.
   PubMed Web of Science ®Google Scholar
• Purdy PH. Ubiquitination and its influence in boar sperm physiology and cryopreservation. Theriogenology. 2008;70(5):818–826.
   PubMed Web of Science ®Google Scholar
• Lovercamp KW, Safranski TJ, Fischer KA, et al. Arachidonate 15-lipoxygenase and ubiquitin as fertility markers in boars. Theriogenology. 2007; 67(4):704–718.
   PubMed Web of Science ®Google Scholar
• Eilebrecht S, Smet-Nocca C, Wieruszeski JM, et al. SUMO-1 possesses DNA binding activity. BMC Res Notes. 2010; 3(1):146.
   PubMedGoogle Scholar
• Azuma Y, Tan SH, Cavenagh MM, et al. Expression and regulation of the mammalian SUMO-1 E1 enzyme. Faseb J. 2001;15(10):1825–1827.
   PubMed Web of Science ®Google Scholar