DNA damage, oxidative stress, decreased viability and motility in common carp (Cyprinuscarpio L.) spermatozoa induced by tryptophan, phenylalanine and cysteine amino acids during short-term storage

Free amino acids are found in spermatozoa and seminal plasma. Their qualitative and quantitative presence have been affected by many factors. Under in vitro storage conditions, their effects on spermatozoa in animal species and also human have been concerned over the last decades. In this study, the effects of tryptophan, phenylalanine and cysteine on DNA integrity, lipid peroxidation, viability and motility parameters in spermatozoa of the common carp Cyprinuscarpio were assessed during short-term storage. Spermatozoa were incubated at 1, 5, 25, and 50 mM of these amino acids in vitro at 4 °C in a time?dependent manner 6, 24, and 48 h . The supplementation of cysteine, phenylalanine and >5 mM of tryptophan to the incubation medium attenuated the spermatozoa motility parameters and viability. Particularly, >1 mM of cysteine completely inhibited progressive motility and decreased viability to

Keywords:

DNA damage, oxidative stress, cysteine, phenylalanine tryptophan, spermatozoa motility,

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Billard R, Menezo Y (1984). The amino acid composition of rainbow trout (Salmo gairdneri) seminal fluid and blood plasma: A comparison with carp (Cyprinuscarpio). Aquaculture 41 (3): 255-258. doi: 10.1016/0044-8486(84)90288-6
Bradley H, Gough A, Sokhi RS, Hassell A, Waring R et al. (1994). Sulfate metabolism is abnormal in patients with rheumatoid arthritis. Confirmation by in vivo biochemical findings. Journal of Rheumatology 21: 1192-1196.
Bucak MN, Tuncer PB, Sariözkan S, Ulutaş PA (2009). Comparison of the effects of glutamine and an amino acid solution on postthawed ram sperm parameters, lipid peroxidation and antioxidant activities. Small Ruminant Research 81 (1): 13-17. doi: 10.1016/j.smallrumres.2008.10.003
Chubb LG, Cooper DM (1962). Amino acids in fowl seminal plasma. Journal of Reproduction and Infertility 4: 7-12. doi: 10.1530/ jrf.0.0040007
Ciereszko A, Glogowski J, Dabrowski K (2000). Biochemical characteristics of seminal plasma and spermatozoa of freshwater fishes. In: Tiersch TR, Mazik PM (editors), Cryopreservation in aquatic species. Louisiana, USA: World Aquaculture Society Press, pp. 20-48.
Ciereszko A, Piros B, Dabrowski K, Kucharczyk D, Łuczyński MJ et al. (1998). Serine proteinase inhibitors of seminal plasma of teleost fish: Distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood. Journal of Fish Biology 53 (6): 1292-1305. doi: 10.1111/j.1095-8649.1998. tb00249.x
Dziewulska K, Rzemieniecki A, Domagała J (2008). Basic physico-chemical parameters of milt from sea trout (Salmo trutta m. trutta), brook trout (Salvelinusfontinalis) and rainbow trout (Oncorhynchus mykiss). Journal of Applied Ichthyology 24 (4): 497-502. doi: 10.1111/j.1439-0426.2008.01133.x
Dzyuba V, Dzyuba B, Cosson J, Boryshpolets S, Yamaner G et al. (2014). The antioxidant system of sterlet seminal fluid in testes and Wolffian ducts. Fish Physiology and Biochemistry 40 (6): 1731-1739. doi: 10.1007/s10695-014-9963-2
Garcia RA, Stipanuk MH (1992). The splanchnic organs, liver and kidney have unique roles in the metabolism of sulfur amino acids and their metabolites in rats. Journal of Nutrition 122: 1693-1701. doi: 10.1093/jn/122.8.1693
Gazo I, Shaliutina-Kolešová A, Dietrich MA, Linhartová P, Shaliutina O et al. (2015). The effect of reactive oxygen species on motility parameters, DNA integrity, tyrosine phosphorylation and phosphatase activity of common carp (Cyprinuscarpio L.) spermatozoa. Molecular Reproduction and Development 82 (1): 48-57. doi: 10.1002/mrd.22442
Gilany K, Minai-Tehrani A, Savadi-Shiraz E, Rezadoost H, Lakpour N (2015). Exploring the human seminal plasma proteome: an unexplored gold mine of biomarker for male infertility and male reproduction disorder. Journal of Reproduction and Infertility 16 (2): 61-71.
Griveau JF, Dumont E, Callegari JP, Le Lannou D (1995). Reactive oxygen species, lipid peroxidation and enzymatic defence systems in human spermatozoa. Journal of Reproduction and Infertility 103: 17-26. doi: 10.1530/jrf.0.1030017
He S, Woods LC (2003). Effects of glycine and alanine on short-term storage and cryopreservation of striped bass (Moronesaxatilis) spermatozoa. Cryobiology 46 (1): 17-25. doi: 10.1016/S0011- 2240(02)00159-1
Heafield MT, Fearn S, Steventon GB, Waring RH, Williams AC et al. (1990). Plasma cysteine and sulphate levels in patients with motor neurone, Parkinson’s and Alzheimer’s disease. Neuroscience Letters 110: 216-220. doi: 10.1016/0304-3940(90)90814-P
Juyena NS, Stelletta C (2012). Seminal plasma: an essential attribute to spermatozoa. International Journal of Andrology 33 (4): 536- 551. doi: 10.2164/jandrol.110.012583
Klebanoff SJ, Smith DC (1970). The source of H2 O2 for the uterine fluidmediated sperm-inhibitory system. Biology of Reproduction 3 (2): 236-242. doi: 10.1093/biolreprod/3.2.236
Kledmanee K, Taweedet S, Thaijongruk P, Chanapiwat P, Kaeoket K (2013). Effect of L-cysteine on chilled carp (Cyprinuscarpio) Semen Qualities. Thai Journal of Veterinary Medicine 43 (1): 91-97.
Kundu CN, Das K, Majumder GC (2001). Effect of amino acids on goat cauda epididymal sperm cryopreservation using a chemically defined model system, Cryobiology 41: 21-27.doi: 10.1006/ cryo.2001.2296
Kutluyer F (2018). In vitro Effect of L-Tryptophan on the Quality and Fertilizing Capacity of Sperms of Endangered Species of Trouts. Pakistan Journal of Zoology 50 (3): 903-910. doi: 10.17582/ journal.pjz/2018.50.3.903.910
Kutluyer F, Aksu Ö, Kocabaş M (2019). Effect of L-Tryptophan on sperm quality of tigris scraper (Capoetaumbla) (Pisces: Cyprinidae) after Cryopreservation. Cryo Letters 40 (2): 77-82. Kocabaş M, Kutluyer F, Ertekin Ö, Aksu Ö, Başçınar N (2019).
Improvement of sperm motility of Oncorhynchus mykiss and Salvelinusfontinalis by L-tryptophan. Systems Biology in Reproductive Medicine 65 (3): 187-193. doi: 10.1080/19396368.2019
Kwasek K, Dabrowski K, Nynca J, Wojno M, Wick M (2014). The Influence of Dietary Lysine on Yellow Perch Maturation and the Quality of Sperm. North American Journal of Aquaculture 76(2): 119-126.doi: 10.1080/15222055.2013.856826
Lahnsteiner F (2009). The role of free amino acids in semen of rainbow trout Oncorhynchus mykiss and carp Cyprinuscarpio. Journal of Fish Biology 75 (4): 816-833. doi: 10.1111/j.1095- 8649.2009.02317.x
Lahnsteiner F (2010). A comparative study on the composition and importance of free amino acids in semen of gilthead sea bream, Sparusaurata, and perch, Percafluviatilis. Fish Physiology and Biochemistry 36 (4): 1297-1305. doi: 10.1007/s10695-010-9442- 3
Lahnsteiner F, Berger B, Weismann T (1999). Sperm metabolism of the teleost fishes Chalcalburnuschalcoides and Oncorhynchus mykiss and its relation to motility and viability. Journal of Experimental Zoology 284 (4): 454-465. doi: 10.1002/(SICI)1097- 010X(19990901)284:43.0.CO;2-O
Lahnsteiner F, Patzner RA, Weismann T (1994). The testicular main ducts and spermatic ducts in cyprinid fishes II. Composition of the seminal fluid. Journal of Fish Biology 44: 459-467. doi: 10.1006/jfbi.1994.1047
Lapointe S, Sirard MA (1998). Catalase and oviductal fluid reverse the decreased motility of bovine sperm in culture medium containing specific amino acids. Journal of Andrology 19 (1): 31-36.
Lehmann A (1987). Alterations in hippocampal extracellular amino acids and purine catabolites during limbic seizures induced by folate injections into the rabbit amygdala. Neuroscience 22: 573- 578. doi:10.1016/0306-4522(87)90354-X
Li P, Xi MD, Du H, Qiao XM, Liu ZG et al. (2018). Antioxidant supplementation, effect on post-thaw spermatozoan function in three sturgeon species. Reproduction in Domestic Animals 53 (2): 287-295. doi:10.1111/rda.13103
Li ZH, Li P, Rodina M, Randak T (2010). Effect of human pharmaceutical Carbamazepine on the quality parameters and oxidative stress in common carp (Cyprinuscarpio L.) spermatozoa. Chemosphere 80 (5): 530-534. doi:10.1016/j.chemosphere.2010.04.046
Macmillan KL, Tiku JL, Hart NL (1972). Toxic effects of aromatic amino acids on the livability of bull spermatozoa. Australian Journal of Biological Sciences 25(5): 1039-1045.doi: 10.1071/ BI9721039
Öğretmen F, Inanan BE, Kutluyer F, Kayim M (2015). Effect of semen extender supplementation with cysteine on postthaw sperm quality, DNA damage, and fertilizing ability in the common carp (Cyprinuscarpio). Theriogenology 83 (9): 1548-1552. doi: 10.1016/j.theriogenology.2015.02.001
Özkan Y, Özkan E, Simsek B (2002). Plasma total homocysteine and cysteine levels as cardiovascular risk factors in coronary heart disease. International Journal of Cardiology 82: 269-277. doi:10.1016/S0167-5273(02)00010-4
Perchec G, Jeulin C, Cosson J, André F, Billard R (1995). Relationship between sperm ATP content and motility of carp spermatozoa. Journal of Cell Science 108 (2): 747-753.
Pourkhazaei F, Ebrahimi E, Ghaedi A (2017). Arginine effects on biochemical composition of sperm in rainbow trout, Oncorhynchus mykiss. Aquaculture Research 48 (7): 3464- 3471. doi: 10.1111/are.13172
Sanchez-Partida LG, Maxwell WMC, Paleg LG, Setchell BP (1992). Proline and glycine betaine in cryoprotective diluents for ram spermatozoa. Reproduction, Fertility and Development 4: 113- 118.doi:10.1071/RD9920113
Santiago-Moreno J, Bernal B, Pérez-Cerezales S, Castaño C, Toledano-Díaz A et al. (2019). Seminal plasma amino acid profile in different breeds of chicken: Role of seminal plasma on sperm cryoresistance. PloS One 14 (1): e0209910. doi: 10.1371/journal.pone.0209910
Schmehl MK, Graham EF, Erdahl DA (1987). Chemical constituents of trout seminal plasma after minimal and maximal cell damage treatments with possible applications to semen evaluation assays. Aquaculture 62 (3-4): 311-318. doi: 10.1016/0044- 8486(87)90173-6
Setchell BP, Hinks NT, Voglmayr JK, Scott TW (1967). Amino acids in ram testicular fluid and semen and their metabolism by spermatozoa. Biochemical Journal 105 (3): 1061-1065. doi: 10.1042/bj1051061
Shaliutina-Kolešová A, Kotas P, Štěrba J, Rodina M, Dzyuba B et al. (2016). Protein profile of seminal plasma and functionality of spermatozoa during the reproductive season in the common carp (Cyprinuscarpio) and rainbow trout (Oncorhynchus mykiss). Molecular Reproduction and Development 83 (11): 968-982. doi: 10.1002/mrd.22737
Stejskal K, Svobodova Z, Fabrik I, Adam V, Beklova M et al. (2008). Content of cysteine, reduced and oxidized glutathione in spermatozoa of representatives of Acipenseriformes (Acipenserbaerii and A. ruthenus) as well as teleosts (Percafluviatilis and Sander lucioperca). Journal of Applied Ichthyology 24: 519-521. doi: 10.1111/j.1439- 0426.2008.01128.x
Tantikitti C, March BE (1995). Dynamics of plasma free amino acids in rainbow trout (Oncorhynchus mykiss) under variety of dietary conditions. Fish Physiology and Biochemistry 13: 179- 194. doi:10.1007/BF00004309
Topraggaleh TR, Shahverdi A, Rastegarnia A, Ebrahimi B, Shafiepour V et al. (2014). Effect of cysteine and glutamine added to extender on post-thaw sperm functional parameters of buffalo bull. Andrologia 46 (7): 777-783. doi: 10.1111/and.12148
Trimeche A, Yvon JM, Vidament M, Palmer E, Magistrini M (1999). Effects of glutamine, proline, histidine and betaine on postthaw motility of stallion spermatozoa. Theriogenology 52: 181- 191.doi:10.1016/S0093-691X(99)00120-X
Tuncer PB, Bucak MN, Büyükleblebici S, Sarıözkan S, Yeni D et al. (2010). The effect of cysteine and glutathione on sperm and oxidative stress parameters of post-thawed bull semen. Cryobiology 61: 303-307. doi:10.1016/j.cryobiol.2010.09.009
Yin J, Ren W, Yang G, Duan J, Huang X et al. (2016). L-Cysteine metabolism and its nutritional implications. Molecular Nutrition and Food Research 60 (1): 134-146. doi:10.1002/ mnfr.201500031