Spermatozoa Molecules in Relation to Bulls Fertility

Subject Areas : Camel

اس.آ. لون ¹ , ر. سینها ² , آ. رحیم ³ , ب.آ. جانایی ⁴ , آ. سینق ⁵ , ن. شاه ⁶

1 - Artificial Breeding Research Station, ICAR-National Dairy Research Institute, Karnal, 132001, Haryana, India
2 - Artificial Breeding Research Station, ICAR-National Dairy Research Institute, Karnal, 132001, Haryana, India
3 - Artificial Breeding Research Station, ICAR-National Dairy Research Institute, Karnal, 132001, Haryana, India
4 - Artificial Breeding Research Station, ICAR-National Dairy Research Institute, Karnal, 132001, Haryana, India
5 - Artificial Breeding Research Station, ICAR-National Dairy Research Institute, Karnal, 132001, Haryana, India
6 - Artificial Breeding Research Station, ICAR-National Dairy Research Institute, Karnal, 132001, Haryana, India

Received: 2016-11-29 Accepted : 2017-03-31 Published : 2017-09-01

Keywords: sperm epigenome markers, sperm proteins, sperm RNAs,

Abstract :

Bull fertility may be defined as the process by which spermatozoa fertilize and activate the ovum and then support embryonic development. Bull fertility is a complex trait having relatively low heritability and plays a vital role for efficient production and reproduction of bovine. Various mechanisms involved in regulating bull fertility associated phenotype and reliable biomarkers are poorly defined. Primary spermatozoa physiology indicators namely sperm molecules and epigenetic factors may play a vital role in predicting sperm physiology and fertility. Spermatozoa and their fingerprints or patterns can play a pivotal role in prediction of fertility in bovine. No reliable tests exist despite genomic selection for evaluating quality of semen and fertility of bull. This review focuses on various molecules related to bull fertility viz., sperm RNAs, seminal plasma proteins, sperm proteins and sperm epigenome. In combination with single-nucleotide polymorphism (SNP), microarrays or sperm molecules and epigenome markers can be used to determine sperm quality and to predict bull fertility.

References:

Aarabi M., Balakier H., Bashar S., Moskovtsev S.I., Sutovsky P., Librach C.L. and Oko R. (2014). Sperm-derived WW domain-binding protein PAWP, elicits calcium oscillations oocyte activation in humans and mice. FASEB J. 28, 4434-4440.

Ashrafzadeh A., Karsani S.A. and Nathan S. (2013). Mammalian sperm fertility related proteins. Int. J. Med. Sci. 10, 1649-1657.

Balhorn R. (2007). The protamine family of sperm nuclear proteins. Genome Biol. 8(9), 227-234.

Bissonnette N., Lévesque-Sergerie J.P., Thibault C. and Boissonneault G. (2009). Spermatozoal transcriptome profiling for bull sperm motility: a potential tool to evaluate semen quality. Reproduction. 138(1), 65-80.

Blaschek M., Kaya A., Zwald N., Memili E. and Kirkpatrick B.W. (2011). A whole-genome association analysis of non compensatory fertility in Holstein bulls. J. Dairy Sci. 94, 4695-4699.

Cancel A.M., Chapman D.A. and Killian G.J. (1997). Osteopontin is the 55-kilodalton fertility-associated proteins in Holstein bull seminal plasma. Biol. Reprod. 57, 1293-1301.

Card C.J., Anderson E.J., Zamberlan S., Krieger K.E., Katropth M. and Sartini B.L. (2013). Cryopreserved bovine spermatozoal transcript profile as revealed by high-throughput ribonucleic acid sequencing. J. Biol. Reprod. 88(2), 49-58.

Chen X., Wang Y., Zhu H., Hao H., Zhao X., Qin T. and Wang D. (2014). Comparative transcript profiling of gene expression of fresh and frozen-thawed bull sperm. Theriogenology. 83(4), 504-511.

Cooper T.G. (1998). Epididymis. Knobil Encyclop. Reprod. 2, 1-17.

Desnoyers L. and Manjunath P. (1992). Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid. J. Biol. Chem. 267(14), 10149-10155.

Desnoyers L., Therien I. and Manjunath P. (1994). Characterization of the major proteins of bovine seminal fluid by two-dimensional polyacrilamide gel electrophoresis. Mol. Reprod. Dev. 37, 425-435.

Dogan S., Varcovic P., de Oliveira R., Belser L.E., Kaya A., Moura A., Sutovsky P., Parrish J., Topper E. and Memili E. (2015). Sperm chromatin structure reflects fertility phenotypes in breeding bulls. J. Biol. Reprod. 92, 92-106.

Einspanier R., Einspaneir A., Wempe F. and Scheit K.H. (1991). Characterization of a new bioactive protein from bovine seminal fluid. Biochem. Biophys. Res. Commun. 179(2), 1006-1010.

Feugang J.M., Rodriguez-Osorio N., Kaya A., Wang H., Page G.P., Ostermeier G.C., Topper E.K. and Memili E. (2010). Transcriptome analyses of bull spermatozoa: implications for male fertility. Reprod. Biomed. Online. 21, 312-324.

Gerena R.L., Irikura D., Eguchi N., Urade Y. and Killian G.J. (2000). Immunocytochemical localization of lipocalintype prostaglandin d synthase in the bull testis and epididymis and on ejaculated sperm. Biol. Reprod. 62, 547-556.

Gilbert I., Bissonnette N., Boissonneault G., Vallée M. and Robert C. (2007). A molecular analysis of the population of mRNA in bovine spermatozoa. Reproduction. 133, 1073-1086.

Gillan L., Kroetsch T., Maxwell W.M. and Evans G. (2008). Assessment of in vitro sperm characteristics in relation to fertility in dairy bulls. Anim. Reprod. Sci. 103, 201-214.

Govindaraju A., Robertson L., Atli O., Kaya A., Topper E., Crate E.A., Uzun A., Padbury J., Perkins A. and Memili E. (2012a). Dynamics of micro RNAs in bull spermatozoa. Reprod. Biol. Endocrinol. 10, 82-95.

Govindaraju A., Dogan S., Rodriguez-Osorio N., Grant K., Kaya A. and Memili E. (2012b). Delivering value from sperm proteomics for fertility. J. Cell. Tissue Res. 349, 783-793.

Jenkins T.G., Aston K.I., Meyer T.D., Hotaling J.M., Shamsi M.B., Johnstone E.B., Cox K.J., Stanford J.B., Porucznik C.A. and Carrell D.T. (2015). Decreased fecundity and sperm DNA methylation patterns. Fertil. Steril. 105(1), 51-57.

Kaya A. and Memili E. (2016). Sperm macromolecules associated with bull fertility. Anim. Reprod. Sci. 169, 88-94.

Killian G.J., Chapman D.A. and Rogowski L.A. (1993). Fertility-associated proteins in Holstein bull seminal plasma. Biol. Reprod. 49, 1202-1207.

Krawetz S.A., Kruger A., Lalancette C., Tagett R., Anton E., Draghici S. and Diamond M.P. (2011). A survey of small RNAs in human sperm. Hum. Reprod. 26, 3401-3412.

Labas V., Grasseau I., Cahier K., Gargaros A., Harichaux G., Teixeira-Gomes A.P., Alves S., Bourin M., Gerard N. and Blesbois E. (2015). Qualitative and quantitative peptidomic and proteomic approaches to phenotyping chicken semen. J. Proteom. 112, 313-335.

Lalancette C., Thibault C., Bachand I., Caron N. and Bissonnette N. (2008). Transcriptome analysis of bull semen with extreme non-return rate: use of suppression-subtractive hybridization to identify functional markers for fertility. Biol. Reprod. 78(4), 618-635.

Lucy M.C. (2001). Reproductive loss in high-producing dairy cattle: where will it end? J. Dairy Sci. 84, 1277-1293.

Manjunath P., Chandonnet L., Leblond E. and Desnoyers L. (1994). Major proteins of bovine seminal vesicles bind to spermatozoa. Biol. Reprod. 50, 27-37.

Manjunath P., Nauc V., Bergeron A. and M´enard M. (2002). Major proteins of bovine seminal plasma bind to the low-density lipoprotein fraction of hen’s egg yolk. Biol. Reprod. 67, 1250-1258.

Miller D., Ostermeier C. and Krawetz S.A. (2005). The controversy, potential and roles of spermatozoal RNA. Trends Mol. Med. 11, 156-163.

Naaby-Hansen S., Flickinger C.J. and Herr J.C. (1997). Two-dimensional gel electrophoretic analysis of vectorially labeled surface proteins of human spermatozoa. Biol. Reprod. 56, 771-787.

Oliva R. (2006). Protamines and male infertility. Hum. Reprod. Update. 12, 417-435.

Oliveira R.V., Dogan S., Belser L.E., Kaya A., Topper E., Moura A., Thibaudeau G. and Memili E. (2013). Molecular morphology and function of bull spermatozoa linked to histones and associated with fertility. J. Reprod. 146, 263-272.

Park Y.J., Kwon W.S., Oh S.A. and Pang M.G. (2012). Fertility-related proteomic profiling bull spermatozoa separated by percoll. J. Proteom. Res. 11(8), 4162-4168.

Peddinti D., Nanduri B., Kaya A., Feugang J.M., Burgess S.C. and Memili E. (2008). Comprehensive proteomic analysis of bovine spermatozoa of varying fertility rates and identification of biomarkers associated with fertility. BMC Syst. Biol. 2, 19-25.

Rodríguez-Lozano I., Ávalos-Rodríguez A., Castillo-Juárez H., Borderas-Tordesillas F., Roa-Vidal J.J. and Rosales-Torres A.M. (2014). Percentage of ubiquitinated spermatozoa does not correlate with fertilizing capacity of thawed bovine semen. Reprod. Domest. Anim. 49(1), 27-31.

Rodríguez-Martínez H. (2003). Laboratory semen assessment and prediction of fertility: still utopia? Reprod. Domest. Anim. 38, 312-318.

Roncoletta M., Morani Eda S., Esper C.R., Barnabe V.H. and Franceschini P.H. (2006). Fertility-associated proteins in Nelore bull sperm membranes. Anim. Reprod. Sci. 91, 77-87.

Royal M.D., Darwash A.O., Flint A.P.F., Webb R., Wooliams J.A. and Lamming G.E. (2000). Declining fertility in dairy cattle: changes in traditional and endocrine parameters of fertility. Anim. Sci. 70, 487-501.

Schoneck C., Baun J. and Einspaneir R. (1996). Sperm viability is influenced in vitro by the bovine seminal protein aSFP: effects on motility, mitochondrial activity and the lipid peroxidation. Theriogenology. 45, 633-642.

Shojaei Saadi H.A., O’Doherty A.M., Gagné D., Fournier É., Grant J.R., Sirard M.A. and Robert C. (2014). An integrated platform for bovine DNA methylome analysis suitable for small samples. BMC Genomics. 15, 451-457.

Soggiu A., Piras C., Hussein H.A., De Canio M., Gaviraghi A., Galli A., Urbani A., Bonizzi L. and Roncada P. (2013). Unravelling the bull fertility proteome. Mol. Biosyst. 9(6), 1188-1195.

Sutovsky P., Aarabi M., Miranda-Vizuete A. and Oko R. (2015). Negative biomarker based male fertility evaluation: sperm phenotypes associated with molecular-level anomalies. Asian J. Androl. 17(4), 554-560.

Therien I., Soubeyrand S. and Manjunath P. (1997). Major proteins of bovine seminal plasma modulate sperm capacitation by high-density lipoprotein. Biol. Reprod. 57, 1080-1088.

Therien I., Moreau R. and Manjunath P. (1998). Major proteins of bovine seminal plasma and high-density lipoprotein induce cholesterol efflux from epididymal sperm. Biol. Reprod. 59, 768-776.

Therien I., Moreau R. and Manjunath P. (1999). Bovine seminal plasma phospholipid-binding proteins stimulate phospholipid efflux from epididymal sperm. Biol. Reprod. 61, 590-598.

Verma A., Rajput S., De S., Kumar R., Chakravarty A.K. and Datta T.K. (2014). Genome-wide profiling of sperm DNA methylation in relation to buffalo (Bubalus bubalis) bull fertility. Theriogenology. 82, 750-758.

Ward W.S. and Coffey D.S. (1991). DNA packaging and organization in mammalian spermatozoa: comparison with Somatic Cells. Biol. Reprod. 44, 569-574.

Wempe F., Einspaneir R. and Scheit K.H. (1992). Characterization by cDNA cloning of the mRNA of a new growth factor from bovine seminal plasma: acid seminal plasma. Biochem. Biophys. Res. Commun. 183, 232-237.

Zhao C., Huo R., Wang F.Q., Lin M., Zhou Z.M. and Sha J.H. (2007). Identification of several proteins involved in regulation of sperm motility by proteomic analysis. Fertil. Steril. 87, 436-438.