Presence of Fertility-associated antigen on sperm membrane corresponds to greater freezability potential of Frieswal bull semen

MEGHA PANDE; N SRIVASTAVA; Y K SONI; OMERDIN OMERDIN; M KUMAR; S TYAGI; ANKUR SHARMA; SURESH KUMAR

doi:10.56093/ijans.v88i1.79424

Authors

MEGHA PANDE Scientist, ICAR-Central Institute for Research on Cattle, Meerut, Uttar Pradesh 250 001 India
N SRIVASTAVA Senior Scientist, ICAR-Central Institute for Research on Cattle, Meerut, Uttar Pradesh 250 001 India
Y K SONI Scientist, ICAR-Central Institute for Research on Cattle, Meerut, Uttar Pradesh 250 001 India
OMERDIN OMERDIN MVSc Scholar, ICAR-Indian Veterinary Research Institute, Izatnagar, Bareilly, Uttar Pradesh
M KUMAR Research Associate, Semen Freezing Laboratory, ICAR-Central Institute for Research on Cattle, Meerut, Uttar Pradesh 250 001 India
S TYAGI Principal Scientist, ICAR-Central Institute for Research on Cattle, Meerut, Uttar Pradesh 250 001 India
ANKUR SHARMA Research Associate, Semen Freezing Laboratory, ICAR-Central Institute for Research on Cattle, Meerut, Uttar Pradesh 250 001 India
SURESH KUMAR Research Associate, Semen Freezing Laboratory, ICAR-Central Institute for Research on Cattle, Meerut, Uttar Pradesh 250 001 India

https://doi.org/10.56093/ijans.v88i1.79424

Keywords:

Fertility associated antigen, Freezability, Frieswal bull, Sperm membrane proteins

Abstract

Several studies have shown relationship of semen freezability with Fertility-associated antigen (FAA) in purebreds. Objectives of present investigation were to determine presence of FAA in Frieswal bull semen and its relationship with freezability. Study involved separation of seminal plasma (SP, FAA – or +) and sperm membranes (SM, FAA – or +), electrophoresis, protein content and quality assessment (n=36).Five groups were: Group-I (19.4%, SP+ve/SM+ve); Group-II (22.2%, SP-ve/SM+ve); Group-III (25%, SP+ve/SM-ve); Group-IV (16.7%, SP-ve/SM-ve), and Group-V (16.7%, unprocessed, initial progressive motility ≤30%, negative control).At postthaw stage, Group-I and -II showed significantly higher (p< 0.001) freezabilitythan FAA-SM-ve groups. Moreover, Group-III with FAA in seminal plasma but not on membrane showed better post-thaw motility than Group-IV, which totally lacked FAA. Our results have shown that 28–30 kDa protein is present in SP and SM of majority of Frieswal bulls and presence of FAA in SM confers appreciable improvement in freezability.

Downloads

Download data is not yet available.

References

Ardon F and Suarez S S. 2013. Cryopreservation increases coating of bull sperm by seminal plasma binder of sperm proteins BSP1, BSP3 and BSP5. Reproduction 146(2): 111–17. DOI: https://doi.org/10.1530/REP-12-0468

Asadpour R, Alavi-Shoushtari S, Rezaii A and Ansari A H K. 2007. SDS-polyacrylamide gel electrophoresis of buffalo bulls seminal plasma proteins and their relation with semen freezability. Animal Reproduction Science 102: 308–13. DOI: https://doi.org/10.1016/j.anireprosci.2007.03.003

Ax R L. 2004. A new test screens bulls for a protein that enables them to settle more cows earlier. Western Cowman 7: 28–32.

Bellin M E, Hawkins H E, Oyarzo J N, Vanderboom R J and Ax R L. 1996. Monoclonal antibody detection of heparin-binding proteins on sperm corresponds to increased fertility of bulls. Journal of Animal Science 74: 173–82. DOI: https://doi.org/10.2527/1996.741173x

Bellin M E, Oyarzo J N, Hawkins H E, Zhang H, Smith R G, Forrest D W, Sprott L R and Ax R L. 1998. Fertility-associated antigen (FAA) on bull sperm indicates fertility potential. Journal of Animal Science 76: 2032–39. DOI: https://doi.org/10.2527/1998.7682032x

Boe-Hansen G B, Rego J P A, Crisp J M, Moura A A, Nouwens A S, Li Y, Venus B, Burns B M and McGowan M R. 2015.

Seminal plasma proteins and their relationship with percentage of morphologically normal sperm in 2–year-old Brahman (Bos indicus) bulls. Animal Reproduction Science 162: 20–30. DOI: https://doi.org/10.1016/j.anireprosci.2015.09.003

Caballero I, Parrilla I, Alminana C, delOlmo D, Roca J, Martinez E A and Vázquez J M. 2012. Seminal plasma proteins as modulators of the sperm function and their application in sperm biotechnologies. Reproduction in Domestic Animals 47(3): 12– 21. DOI: https://doi.org/10.1111/j.1439-0531.2012.02028.x

Calvete J J and Sanz L. 2007. Insights into structure-function correlations of ungulate seminal plasma proteins. Proceedings of the 10th International Symposium on Spermatology, Spain, pp 201–215.

Campbell R G, Hancock J L and Rothschild L. 1953. Counting live and dead bull spermatozoa. Journal of Experimental Biology 130: 44–45. DOI: https://doi.org/10.1242/jeb.30.1.44

Dhanju C K, Cheema R S and Kaur S P. 2001. Effects of freezing on proteins and protein profiles of sperm membrane extracts and seminal plasma of buffalo bulls. Asian Australasian Journal of Animal Science 14: 1678–1682. DOI: https://doi.org/10.5713/ajas.2001.1678

Drobnis E Z, Crowe L M, Berger T, Anchordoguy T J, Overstreet W and Crowe J H. 1993. Cold shock damage is due to lipid phase transitions in cell membranes, a demonstration using sperm as a model. Journal of Experimental Zoology 265: 432– 37. DOI: https://doi.org/10.1002/jez.1402650413

Fernandes C E, de Souza F F, Souza-Neto J A and Ribola P E M. 2008. Heparin-binding proteins of seminal plasma in Nellore bulls. Ciencia Rural 39: 20–26. DOI: https://doi.org/10.1590/S0103-84782008005000044

Gerena R L, Irikura D, Urade Y, Eguchi N, Chapman D A and Killian G J. 1998. Identification of a fertility-associated protein in bull seminal plasma as lipocalin-type prostaglandin D synthase. Biology of Reproduction 58: 826–33. DOI: https://doi.org/10.1095/biolreprod58.3.826

Januskauskas A, Johannisson A and Rodriguez-Martinez H. 2003. Subtle membrane changes in cryopreserved bull semen in relation with sperm viability, chromatin structure, and field fertility. Theriogenology 60: 743–58. DOI: https://doi.org/10.1016/S0093-691X(03)00050-5

Jeyendran R S, Vander Ven H H, Perz-Pelaez M, Crabo B G and Zaneveld L J D. 1984. Development of an assay to assess the functional integrity of the human sperm membrane and its relationship to other sperm characteristics. Journal of Reproduction and Fertility 70: 219–28. DOI: https://doi.org/10.1530/jrf.0.0700219

Jobim M I M, Oberst E R, Salbego C G, Souza D O, Wald V B, Tramontina F and Mattos R C. 2004. Two-dimensional polyacrylamide gel electrophoresis of bovine seminal plasma proteins and their relation with semen freezability. Theriogenology 61: 255–66. DOI: https://doi.org/10.1016/S0093-691X(03)00230-9

Juyena N S and Stelletta C. 2012. Seminal plasma: An essential attribute to spermatozoa. Journal of Andrology 33: 536–51. DOI: https://doi.org/10.2164/jandrol.110.012583

Karunakaran M and Devanatha T G. 2016. Evaluation of bull semen for fertility-associated protein, in vitro characters and fertility. Journal of Applied Animal Research 45(1): 136–44. DOI: https://doi.org/10.1080/09712119.2015.1129343

Karunakaran M, Devanathan T G, Jawahar T P, Manimaran K, Chitra A, Dhali A and Selvaraju S. 2012. Electrophoretic profile of bull sperm membrane proteins as a tool for selection of breeding bull. Indian Journal of Animal Sciences 82(11): 1303–05.

Krishnan G, Thangvel A, Loganathasamy K, Veerapandian C, Kumarasamy P and Karunakaran M. 2016. The presence of heparin binding proteins and their impact on semen quality of Holstein Friesian bulls. Indian Journal of Animal Sciences 86(4): 392–96.

Laemmli V K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680– 85. DOI: https://doi.org/10.1038/227680a0

Manjunath P, Bergeron A, Lefebvre J and Fan J. 2007. Seminal plasma proteins: functions and interaction with protective agents during semen preservation. Society of Reproduction and Fertility Supplement 65: 217–28.

Manjunath P, Lefebvre J, Jois P S, Fan J and Wright M W. 2009. New nomenclature for mammalian BSP genes. Biology of Reproduction 80: 394–97. DOI: https://doi.org/10.1095/biolreprod.108.074088

Matthew D U. 2016. Prediction of bull fertility. Animal Reproduction Science 169: 37–44. DOI: https://doi.org/10.1016/j.anireprosci.2015.12.011

McCauley T C, Zhang H M, Bellin M E and Ax R X. 2001. Identification of a heparin- binding protein in bovine seminal fluid as tissue inhibitor of metalloproteinases–2. Molecular Reproduction and Development 58: 336–41. DOI: https://doi.org/10.1002/1098-2795(200103)58:3<336::AID-MRD12>3.0.CO;2-Z

Moura A A, Koc H, Chapman D A and Killian G J. 2006. Identification of proteins in the accessory sex gland fluid associated with fertility indexes of dairy bulls: a proteomic approach. Journal of Andrology 27: 201–11. DOI: https://doi.org/10.2164/jandrol.05089

Nass S J, Miller D J, Winner M A and Ax R L. 1990. Male accessory sex glands produce heparin-binding proteins that bind to caudaepididymal spermatozoa and are testosterone dependent. Molecular Reproduction and Development 25: 237–46. DOI: https://doi.org/10.1002/mrd.1080250305

Rodriguez-Martinez H, Kvist U, Ernerudh J, Sanz L and Calvete J J. 2011. Seminal plasma proteins: what role do they play? American Journal of Reproductive Immunology 66 (1): 11– 22. DOI: https://doi.org/10.1111/j.1600-0897.2011.01033.x

Rodriguez-Martinez H. 2014. Semen evaluation and handling. Animal andrology theories and applications. (Eds) Chenoweth P J and Lorton S P. London, UK, pp 526–528.

Rodríguez-Villamil P, Hoyos-Marulanda V, Martins J A M, Oliveira A N, Aguiar L H, Moreno F B, Velho A L M C S, Monteiro-Moreira M C, Moreira R A, Vasconcelos I M, Bertolini M and Moura A A. 2016. Purification of binder of sperm protein 1 (BSP1) and its effects on bovine in vitro embryo development after fertilization with ejaculated and epididymal sperm. Theriogenology 85(3): 540–54. DOI: https://doi.org/10.1016/j.theriogenology.2015.09.044

Snedecor G W and Cochran W G. Statistical methods, 7th ed. The Iowa State University Press, Ames, Iowa, USA, pp 115.

Souza C E, Moura A A, Monaco E and Killian G J. 2008. Binding patterns of bovine seminal plasma proteins A1/A2, 30 kDa and osteopontin on ejaculated sperm before and after incubation with isthmic and ampullary oviductal fluid. Animal Reproduction Science 105: 72–89. DOI: https://doi.org/10.1016/j.anireprosci.2007.11.027

Srivastava N, Jerome A, Srivastava S K, Ghosh S K and Amit K. 2013. Bovine seminal PDC–109 protein: an overview of biochemical and functional properties. Animal Reproduction Science 138: 1–13. DOI: https://doi.org/10.1016/j.anireprosci.2013.02.008

Tyagi S, Mathur A K and Agarwal S C. 2000. Semen production performance of Frieswal bulls. Indian Journal of Animal Reproduction 70: 1032–34.

Watson P F. 1975. Use of Giemsa stain to detect changes in acrosome of frozen ram spermatozoa. Veterinary Record 79: 12–15. DOI: https://doi.org/10.1136/vr.97.1.12

Watson P F. 1995. Recent developments and concepts in the cryopreservation of spermatozoa and the assessment of their post-thawing function. Reproduction Fertility and Development 7: 871–91. DOI: https://doi.org/10.1071/RD9950871

Yanagimachi R. 1994. Fertility of mammalian spermatozoa: its development and relativity. Zygote 3: 371–72. DOI: https://doi.org/10.1017/S0967199400002240