The Effect of Cattle Seminal Plasma Crude Protein on the Cryopreservation of Goat Semen
الموضوعات :ت. وایو سوپرایوگی 1 , س. سوسیلواتی 2
1 - Department of Reproduction, Faculty of Veterinary, Airlangga University, Surabaya, East Java, Indonesia
2 - Department of Reproduction, Faculty of Veterinary, Airlangga University, Surabaya, East Java, Indonesia
الکلمات المفتاحية: viability, cattle seminal plasma crude protein, cytochrome C, motility,
ملخص المقالة :
This study aimed to improve the quality of cryopreserved goat semen for artificial insemination by the addition of cattle seminal plasma crude protein. Semen collected from cattle and centrifuged to obtain seminal plasma. Then it was purified to obtain the crude protein. The diluent used in this study was milk-yolk. There were three groups, control group without crude protein (P0), the addition of 2.5 mg crude protein/mL diluent (P1); and the addition of 5 mg crude protein/mL diluent (P2). The results showed that P1 had the highest percentage of progressive motility and viability. Meanwhile, P1 had the lowest percentage of cytochrome C expression. The lowest cytochrome C expression indicates that the mitochondria have a good function. So, by the addition of 2.5 mg crude protein/mL diluent, the quality of frozen goat semen in terms of sperm motility, viability, and cytochrome C expression in the spermatozoa could be improved.
Aulani’am. (2005). Protein dan analisisnya. Citra Mentari Group, Malang, Indonesia.
Bansal A.K. and Bilaspuri G.S. (2010). Impacts of oxidative stress and antioxidants on semen functions. Vet. Med. Int. 2011, 1-7.
Beatriz B., R-Perez P., Gallego M., Tato A., Osada J., Muino B. and Cebrian P. (2000). Seminal plasma proteins revert the cold shock damage on ram sperm membrane. Biol. Reprod. 63, 1531-1537.
Bergeron A., Villemure M., Lazure C. and Manjunath P. ( 2005). Isolation and characterization of the major proteins of ram seminal plasma. Mol. Reprod. Dev. 71, 461-470.
Blesbois E. (2007). Current status in avian semen cryopreservation. World’s J. Poult. Sci. 63, 213-222.
Castro L.S., Hamilton T.R.S., Mendes C.M., Nichi M., Barnabe V.H., Visintin V. and Assumpcao M.E.O.A. (2016). Sperm cryodamage occurs after rapid freezing phase: Flow cytometry approach and antioxidant enzymes activity at different stages of cryopreservation. J. Anim. Sci. Biotechnol. 7, 17-27.
Crompton M., Virji S. and Ward J.M. (1998). Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. European J. Biochem. 258, 729-735.
Evans G. and Maxwell M.W.C. (1987). Salomon’s Artificial inSemination of Sheep and Goat. Butherworths, Sydney, Australia.
Gazali M. and Tambing S.N. (2002). Kriopreservasi sel spermatozoa. Hayati. 9, 27-32.
Gurler H., Malama E., Heppelmann M., Calisici O., Leiding C., Kastelic J.P. and Bollwein H. (2016). Effects of cryopreservation on sperm viability, synthesis of reactive oxygen species and DNA damage of bovine sperm. Theriogenology. 86, 562-571.
Kassai M. (1996). Simple and efficient methods for vitrification of mammalian embryos. Anim. Reprod. Sci. 42, 67-75.
Kumar S., Sathwara N., Autam A.K.G., Garwal K.A., Shah B., Kulkarni P.K., Patel K., Patel A., Vave L.M., Parikh D.J. and Saiyed H.N. (2005). Semen quality of industrial workers occupationally exposed to chromium. J. Occup. Health. 47, 424-430.
Lessard C., Parent S., Leclerc P., Bailey J.L. and Sullivan R. (2000). Cryopreservation alters the levels of the bull sperm surface protein P25b. J. Androl. 21, 700-707.
Li L.Y., Luo X. and Wang X. (2001). Endonuclease G is an apoptotic DNAse when released from mitochondria. Nature. 412, 95-99.
Lumongga Z. (2008). Interpretasi Mikroskopis Jaringan Dari Biopsi Hati. USU Repository, Medan, Indonesia.
Manjunath P., Chandomet L., Leblonde L. and Denoyers L. (1993). Major proteins of bovine seminal vesicles bind to Spermatozoa. Biol. Reprod. 50, 27-32.
Mugbal D.H., Ahmad I., Muhamad S.M., Fazal W., Umer F., Syed A.M. and Amjad R. (2018). Effect of osmotic pressure an spermatozoa characteristics of cryopreserved buffalo bull (Bubalus bubalus) semen. J. Appl. Anim. Res. 46(1), 274-277.
Naz R.K. and Rajesh P.B. (2004). The role of tyrosin phosphorylation in sperm capacitation / acrosome reaction. Reprod. Biol. Endocrinol. 2, 75-78.
O’Flaherty C., de Lamirande E. and Gagnon C. (2006). Positive role of reactive oxygen species in mammalian sperm capacitation: Triggering and modulation of phosphorylation events. Free Radical Biol. Med. 41, 528-540.
Peterson Q.P., Goode D.R., West D.C., Botham R.C. and Hergenrother P.J. (2010). Preparation of the caspase -3/-7 substrate Ac-DEVD-pNA by solution-phase peptide synthesis. Nat. Protoc. 5, 294-302.
Roncoletta M., Morani E.D.S.C., Franschesini P.H. and Ramos P.R.R. (2000). Caracterização da proteína 26 kDa do plasma seminal e sua relação com a congelabilidade do sêmen de touros. Arq. Fac. Vet. UFRGS. 28, 323-332.
Santoso S. and Fandy T. (2001). Riset Pemasaran: Konsep dan Aplikasi Dengan SPSS. Gramedia, Jakarta, Indonesia.
Sinha M.P., Sinha A.K. and Singh B.K. (1996). The Effect of glutathione on motility, enzyme leakage, and fertility of frozen goat semen. J. Anim. Reprod. Sci. 41, 237-243.
Susilowati S., Hardijanto T., Suprayogi T.W., Sardjito T. dan Hernawati T. (2010). Buku Petunjuk Praktikum Fakultas Kedokteran Hewan. Airlangga University Press, Surabaya, Indonesia.
Toelihere M.R. (1985). Inseminasi Buatan Pada Ternak. Angkasa Bandung, Bandung, Indonesia.
Ustuner B., Zekarya N., Selim Al C., Mehmet B., Toser T., Hakan S. and Mustafa K.S. (2015). Effect of freezing rate on goat sperm morphology and DNA integrity. Turkish J. Vet. Anim. Sci. 39, 110-114.
Wang S. and El-Deiry W.S. (2004). Cytochrom C: A crosslink between the mitochondria and the endoplasmic reticulum in calcium-dependent apoptosis. Cancer Biol. Ther. 3(1), 44-46.
Wach-Gigax L., Buger D., Malana E., Bollein H., Fleisch A. and Jeannerat R. (2017). Seasonal changes of DNA fragmentation and quality of raw and cold stored stallion spermatozoa. Theriogenology. 99, 98-104.
