Abstract
Sperm proteins in the seminal plasma and spermatozoa of teleostean and chondrostean have evolved adaptations due to the changes in the reproductive environment. Analysis of the composition and functions of these proteins provides new insights into sperm motility and fertilising abilities, thereby creating possibilities for improving artificial reproduction and germplasm resource conservation technologies (e.g. cryopreservation). Seminal plasma proteins are involved in the protection of spermatozoa during storage in the reproductive system, whereas all spermatozoa proteins contribute to the swimming and fertilising abilities of sperm. Compared to mammalian species, little data are available on fish sperm proteins and their functions. We review here the current state of the art in this field and focus on relevant subjects that require attention. Future research should concentrate on protein functions and their mode of action in fish species, especially on the role of spermatozoa surface proteins during fertilisation and on a description of sturgeon sperm proteins.
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References
Afzelius BA (1978) Fine structure of the garfish spermatozoa. J Ultrastruct Res 64:309–314. doi:10.1016/S0022-5320(78)90039-4
Alberts B, Bray D, Lewis J et al (1987) Molecular biology of the cell, vol 4. MIR publications, Moscow, pp 1–200. doi:10.1002/mmnd.4800040102
Babiak I, Glogowski J, Luczynski MJ et al (1997) Cryopreservation of the milt of the northern pike. J Fish Biol 46:819–828. doi:10.1111/j.1095-8649.1995.tb01604.x
Babiak I, Glogowski J, Goryczko K et al (2001) Effect of extender composition and equilibration time on fertilization ability and enzymatic activity of rainbow trout cryopreserved spermatozoa. Theriogenology 56:177–192. doi:10.1016/S0093-691X(01)00553-2
Baccetti B, Pallini A, Burrini AG (1975) Localization and catalytic properties of lactate dehydrogenase in different sperm models. Exp Cell Res 90:183–190. doi:10.1016/0014-4827(75)90372-9
Baccetti B, Burrini AG, Collodel G et al (1989) Localization of acrosomal enzymes in Arthropoda, Echinodermata, Vertebrata. J Submicrosc Cytol Pathol 21:385–389
Bannai H, Yoshimura M, Takahashi K et al (2000) Calcium regulation of microtubule sliding in reactivated sea urchin sperm flagella. J Cell Sci 113:831–839
Billard R, Takashima F (1983) Resorption of spermatozoa in the sperm duct of rainbow trout during the post-spawning period. Bull Jpn Soc Sci Fish 49:387–392
Billard R, Cosson MP (1992) Some problems related to the assessment of sperm motility in freshwater fish. J Exp Zool 261:122–131. doi:10.1002/jez.1402610203
Billard R, Cosson J, Crim LW (1993) Motility of fresh and aged halibut sperm. Aquat Living Resour 6:67–75. doi:10.1051/alr:1993008
Billard R, Cosson J, Crim LW et al (1995) Sperm physiology and quality. In: Bromage NR, Roberts RJ (eds) Brood stock management and egg and larval quality. Blackwell Science, Oxford, pp 25–52
Billard R, Linhart O, Fierville F et al (1997) Motility of Silurus glanis spermatozoa in the testicles and in the milt. Pol Arch Hydrobiol 44:115–122
Boitano S, Omoto CK (1991) Membrane hyperpolarization activates trout sperm without an increase in intracellular pH. J Cell Sci 98:343–349
Boitano S, Omoto CK (1992) Trout sperm swimming patterns and role of intracellular Ca2+. Cell Motil Cytoskeleton 21:74–82. doi:10.1002/cm.970210109
Brandon CI, Heusner GL, Caudle AB et al (1999) Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility. Theriogenology 52:863–873. doi:10.1016/S0093-691X(99)00178-8
Breton B, Menezo Y, Billard R et al (1974) Mise en évidence de quelques enzymes dans le sperme de la carpe Cyprinus carpio L et de la truite Salmo gairdneri Richardson et dans le liquide coelomatique de la truite. C R Acad Sci Paris D 278:1285–1288
Brokaw CJ (1979) Calcium-induced asymmetrical beating of triton-demembranated sea urchin sperm flagella. J Cell Biol 82:401–411. doi:10.1083/jcb.82.2.401
Burness G, Moyes CD, Montgomerie R (2005) Motility, ATP levels and metabolic enzyme activity of sperm from bluegill (Lepomis macrochirus). Comp Biochem Physiol Mol Integr Physiol 140:11–17
Cabrita E, Anel L, Herraéz MP (2001) Effect of external cryoprotectants as membrane stabilizers on cryopreserved rainbow trout sperm. Theriogenology 56:623–635. doi:10.1016/S0093-691X(01)00594-5
Cadel S, Pierotti AR, Foulon T et al (1995) Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules. Mol Cell Endocrinol 110:149–160. doi:10.1016/0303-7207(95)03529-G
Calvete JJ, Sanz L, Topfer-Petersen E (1992) Carbohydrate-binding proteins involved in gamete interaction in the pig. In: Nieschlag E, Habenicht UF (eds) Spermatogenesis–fertilization–contraception. Springer, Berlin, pp 395–417
Cao WL, Wang YX, Xiang ZQ et al (2003) Cryopreservation-induced decrease in heat-shock protein 90 in human spermatozoa and its mechanism. Asian J Androl 5:43–46
Chan PJ, Corselli JU, Patton WC et al (1997) The mechanism of heat-induced hyperactivation of human sperm and the relationship to pregnancy. Fertil Steril 68[Suppl 1]:S61–S62. doi:10.1016/S0015-0282(97)90755-X
Chauvaud L, Cosson J, Suquet M et al (1995) Sperm motility in turbot, Scophthalmus maximus: initiation of movement and changes with time of spawning characteristics. Environ Biol Fishes 43:341–349. doi:10.1007/BF00001167
Cherr GN, Clark WH (1982) Fine-structure of the envelope and micropyles in the eggs of the white sturgeon, Acipenser transmontanus Richardson. Dev Growth Differ 24:341–352. doi:10.1111/j.1440-169X.1982.00341.x
Cherr GN, Clark WN (1985) Gamete interaction in the white sturgeon Acipenser transmontanus: a morphological and physiological review. Environ Biol Fishes 14:11–22. doi:10.1007/BF00001572
Cherr GN, Clark WN (1986) Induction of the acrosomal reaction in sperm from the white sturgeon, Acipenser transmontanus. In: Hedrick JL (ed) Advances in experimental medicine and biology the molecular and cellular biology of fertilization. Plenum Press, New York, pp 235–249
Christen R, Gatti JL, Billard R (1987) Trout sperm motility. The transient movement of trout sperm motility is related to changes in concentrations of ATP following the activation of flagellar movement. Eur J Biochem 166:667–671. doi:10.1111/j.1432-1033.1987.tb13565.x
Cierezko A (2008) Chemical composition of seminal plasma and its physiological relationship with sperm motility, fertilizing capacity and cryopreservation success in fish. In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Fish spermatology. Alpha Science Int, Oxford, pp 215–240
Ciereszko A, Dabrowski K (1994) Relationship between biochemical constituents of fish semen and fertility: the effect of short-term storage. Fish Physiol Biochem 12:357–369. doi:10.1007/BF00004300
Cosson J (1992) The covalent oscillator—a paradigm accounting for the sliding bending mechanism and wave-propagation in cilia and flagella. Biocell 76:319–327
Cosson J (2008) The motility apparatus of fish spermatozoa. In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Fish spermatology. Alpha Science Int, Oxford, pp 281–316
Cosson M-P, Gagnon C (1988) Protease inhibitor and substrates block motility and microtubule sliding of sea urchin and carp spermatozoa. Cell Motil Cytoskeleton 10:518–527. doi:10.1002/cm.970100408
Cosson M-P, Carré D, Cosson J (1984) Sperm chemotaxis in siphonophores II. Calcium-dependent asymmetrical movement of spermatozoa induced by attractant. J Cell Sci 68:163–181
Cosson M-P, Cosson J, André F, Billard R (1995) CAMP/ATP relationship in the activation of trout sperm motility: their interaction in membrane-deprived models and in live spermatozoa. Cell Motil Physiol 143:546–554
Cosson J, Dreanno C, Billard R et al (1999) Regulation of axonemal wave parameters of fish spermatozoa by ionic factors. In: Gagnon C (ed) The male gamete: from basic knowledge to clinical applications. Cache River Press, Montreal, pp 161–186
Cosson J, Linhart O, Mims SD et al (2000) Analysis of motility parameters from paddlefish and shovelnose sturgeon spermatozoa. J Fish Biol 56:1348–1367. doi:10.1111/j.1095-8649.2000.tb02148.x
Cosson J, Groison AL, Suquet M et al (2008) Studying sperm motility in marine fish: an overview on the state of the art. J Appl Ichtyol 24:460–486. doi:10.1111/j.1439-0426.2008.01151.x
Costa M, Canale D, Filicori M et al (1994) l-carnitine in idiopathic asthenozoospermia: a multicenter study Italian study group on carnitine and male infertility. Andrologia 26:155–159
Coward K, Campos-Mendoza A, Larman M et al (2003) Teleost fish spermatozoa contain a cytosolic protein factor that induces calcium release in sea urchin egg homogenates and triggers calcium oscillations when injected into mouse oocytes. Biochem Biophys Res Commun 305:299–304. doi:10.1016/S0006-291X(03)00753-8
Dan JC (1950) Fertilization in the medusan, Spirocodon saltatrix. Biol Bull 99:412–415. doi:10.2307/1538471
Darszon A, Beltrán C, Felix R et al (2001) Ion transport in sperm signaling. Dev Biol 240:1–14. doi:10.1006/dbio.2001.0387
Davis NS, DiSant’Agnese PA, Ewing JF, Mooney RA et al (1989) The neuroendocrine prostate: characterization and quantitation of calcitonin in the human gland. J Urol 142:884–888
De Leeuw FE, De Leeuw AM, Den Daas JHG et al (1993) Effect of various cryoprotectants agents and membrane-stabilizing compounds on bull sperm membrane integrity after cooling and freezing. Cryobiology 30:32–44. doi:10.1006/cryo.1993.1005
Desrosiers P, Légaré C, Leclerc P et al (2006) Membranous and structural damage that occur during cryopreservation of human sperm may be time-related events. Fertil Steril 85:1744–1752. doi:10.1016/j.fertnstert.2005.11.046
Detweiler C, Thomas P (1998) Role of ions and ion channels in the regulation of Atlantic croaker sperm motility. J Exp Zool 281:139–148. doi:10.1002/(SICI)1097-010X(19980601)281:2<139::AID-JEZ8>3.0.CO;2-P
DiLauro MN, Kaboord WS, Walsh RA (2000) Sperm-cell ultrastructure of North American sturgeon I. The Atlantic sturgeon (Acipenser oxyrhynchus). Can J Zool 78:438–447. doi:10.1139/cjz-78-3-438
Dréanno C, Cosson J, Suquet M et al (1999) Effects of osmolality, morphology perturbations and intracellular nucleotide content during the movement of sea bass (Dicentrarchus labrax) spermatozoa. J Reprod Fertil 116:113–125. doi:10.1530/jrf.0.1160113
Evans JP, Kopf GS (1998) Molecular mechanisms of sperm–egg interactions and egg activation. Andrologia 30:297–307
Farrant J (1977) Water transport and cell survival in cryobiological procedures. Philos Trans R Soc Lond Biol Sci 278:191–205. doi:10.1098/rstb.1977.0037
Gadea J, Selles E, Marco MA et al (2004) Decrease in glutathione content in boar sperm after cryopreservation—effect of the addition of reduced glutathione to the freezing and thawing extenders. Theriogenology 62:690–701. doi:10.1016/j.theriogenology.2003.11.013
Gardner AJ, Evans JP (2006) Mammalian membrane block to polyspermy: new insights into how mammalian eggs prevent fertilization by multiple sperm. Reprod Fertil Dev 18:53–61. doi:10.1071/RD05122
Gatti JL, Billard R, Christen R (1990) Ionic regulation of the plasma membrane potential of rainbow trout, Salmo gairdneril, spermatozoa: role in the initiation of sperm motility. J Cell Physiol 143:546–554. doi:10.1002/jcp.1041430320
Ghosh S, Thomas P (1995) Binding characteristics of 20β-S to Atlantic croaker sperm membrane receptor. In: Proc 5th Int Symp Reprod Physiol Fish. University of Texas, Austin, pp 239–245
Gibbons BH, Baccetti B, Gibbons IR (1985) Motility of the 9 + 2 flagellum of Anguilla sperm. Cell Motil 5:333–350. doi:10.1002/cm.970050406
Gilkey JC (1981) Mechanisms of fertilization in fishes. Am Zool 21:359–375
Ginzburg AS (1972) Fertilization in fishes and the problem of polyspermy. Keter Press, Jerusalem
Glogowski J, Babiak I, Goryczko K et al (1996) Activity of aspartate aminotransferase and acid phosphatase in cryopreserved trout sperm. Reprod Fertil Dev 8:1179–1184. doi:10.1071/RD9961179
Gronczewska J, Zietara MS, Biegniewska A et al (2003) Enzyme activities in fish spermatozoa with focus on lactate dehydrogenase isoenzymes from herring Clupea harengus. Comp Biochem Physiol B 134:399–406. doi:10.1016/S1096-4959(02)00192-6
Grzyb K, Rychowski M, Biegniewska A et al (2003) Quantitative determination of creatine kinase release from herring (Clupea harengus) spermatozoa induced by tributyltin. Comp Biochem Physiol C 134:207–213
Hayashi H, Yamamoto K, Richmond J et al (1987) Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa. J Biol Chem 262:16692–16698
Huang CJ, Chen CC, Chen HJ et al (1995a) A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: I Protein purification and characterization. J Neurochem 64:1715–1720
Huang CJ, Lee MS, Huang FL et al (1995b) A protease inhibitor of the serpin family is a major protein in carp perimeningeal fluid: II. cDNA cloning, sequence analysis, and Escherichia coli expression. J Neurochem 64:1721–1727
Huang SY, Kuo YH, Lee WC et al (1999) Substantial decrease of heat-shock protein precedes the decline of sperm motility during cooling of boar spermatozoa. Theriogenology 51:1007–1016. doi:10.1016/S0093-691X(99)00046-1
Inaba K (2003) Molecular architecture of sperm flagella: molecules for motility and signaling. Zool Sci 20:1043–1056. doi:10.2108/zsj.20.1043
Inaba K (2008) Molecular mechanisms of the activation of flagellar motility in sperm. In: Alavi SMH, Cosson JJ, Coward K, Rafiee G (eds) Fish spermatology. Alpha Science Int, Oxford, pp 267–280
Inaba K, Morisawa M (1991) A chymotrypsin-like proteinase involved in motility of sperm in salmonid fish. Biomed Res 12:435–437
Inaba K, Kagami O, Ogawa K (1999) Tctex2-related outer arm dynein light chain is phosphorylated at activation of sperm motility. Biochem Biophys Res Commun 256:177–183. doi:10.1006/bbrc.1999.0309
Inaba K, Padma P, Hozumi A (2002) Isolation of an inner arm dynein intermediate chain IC116 from Ciona intestinalis and its roles in flagellar motility. Zool Sci 19:1435
Inaba K, Dreano C, Cosson J (2003) Control of Flatfish sperm motility by CO2 and carbonic anhydrase. Cell Motil Cytoskeleton 55:174–187. doi:10.1002/cm.10119
Itoh A, Inaba K, Ohtake H et al (2003) Characterization of cAMP-dependent protein kinase catalytic subunit from rainbow trout sperm. Biochem Biophys Res Commun 305:855–861. doi:10.1016/S0006-291X(03)00840-4
Jaffe LA (1990) First messengers at fertilization. J Reprod Fertil Suppl 42:107–116
Jamieson BGM (1991) Fish evolution and systematics: evidence from spermatozoa. Cambridge University Press, Cambridge
Jobim MIM, Oberst ER, Salbego CG et al (2004) Two-dimensional polyacrylamide gel electrophoresis of bovine seminal plasma proteins and their relation with semen freezability. Theriogenology 61:255–266. doi:10.1016/S0093-691X(03)00230-9
Jones R (1990) Identification and functions of mammalian egg recognition molecules during fertilization. J Reprod Fertil Suppl 42:89–105
Kamiya R (2002) Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants. Int Rev Cytol 219:115–155. doi:10.1016/S0074-7696(02)19012-7
Kawabata C, Ichishima E (1997) Miltpain, new cysteine proteinase from the milt of chum salmon, (Oncorhynchus keta). Comp Biochem Physiol B 117:445–452. doi:10.1016/S0305-0491(97)00142-9
Kopeika EF, Zhang T, Rawson DM et al (2005) Effect of cryopreservation on mitochondrial DNA of zebrafish (Danio rerio) blastomere cells. Mutat Res 570:49–61. doi:10.1016/j.mrfmmm.2004.09.007
Kowalski R, Glogowski J, Kucharczyk D et al (2003) Proteolytic activity and electrophoretic profiles of proteases from seminal plasma of teleosts. J Fish Biol 63:1008–1019. doi:10.1046/j.1095-8649.2003.00224.x
Krasznai Z, Marian T, Izumi H et al (2000) Membrane hyperpolarization removes inactivation of Ca2+ channels, leading to Ca2+ influx and subsequent initiation of sperm motility in the common carp. Proc Natl Acad Sci USA 97:2052–2057. doi:10.1073/pnas.040558097
Kudo S (1983) Response to sperm penetration of the cortex of eggs of the fish, Plecoglossus altivelis. Dev Growth Differ 25:163–170. doi:10.1111/j.1440-169X.1983.00163.x
Kudo S (1998) Role of sperm head syndecan at fertilization in fish. J Exp Zool 281:620–625. doi:10.1002/(SICI)1097-010X(19980815)281:6<620::AID-JEZ10>3.0.CO;2-6
Kumaresan A, Ansari MR, Garg A et al (2006) Effect of oviductal proteins on sperm functions and lipid peroxidation levels during cryopreservation in buffaloes. Anim Reprod Sci 93:246–257. doi:10.1016/j.anireprosci.2005.06.030
Labbé C, Loir M (1991) Plasma membrane of trout spermatozoa: I Isolation and partial characterization. Fish Physiol Biochem 9:325–338. doi:10.1007/BF02265153
Lahnsteiner F (2000) Cryopreservation protocols for sperm of salmonid fishes. In: Tiersch TR, Mazik PM (eds) Cryopreservation in aquatic species. World Aquaculture Society, Baton Rouge, pp 91–100
Lahnsteiner F (2003) Morphology, fine structure, biochemistry, and function of the spermatic ducts in marine fish. Tissue Cell 35:363–373. doi:10.1016/S0040-8166(03)00057-0
Lahnsteiner F (2007) Characterization of seminal plasma proteins stabilizing the sperm viability in rainbow trout (Oncorhynchus mykiss). Anim Reprod Sci 97:151–164. doi:10.1016/j.anireprosci.2006.01.003
Lahnsteiner F, Patzner RA, Weismann T (1992) Monosaccharides as energy resources during motility of spermatozoa in Leuciscus cephalus (Cyprinidae, Teleostei). Fish Physiol Biochem 10:283–289. doi:10.1007/BF00004477
Lahnsteiner F, Patzner RA, Weismann T (1993) Energy resources of spermatozoa of the rainbow trout (Oncorhynchus mykiss) (Pisces, Teleostei). Reprod Nutr Dev 33:349–360. doi:10.1051/rnd:19930404
Lahnsteiner F, Patzner RA, Weismann T (1994) Testicular main ducts and spermatic ducts in some cyprinid fishes I. Morphology, fine structure and histochemistry. J Fish Biol 44:937–951. doi:10.1111/j.1095-8649.1994.tb01266.x
Lahnsteiner F, Berger B, Weismann T et al (1998) Determination of semen quality of the rainbow trout by sperm motility, seminal plasma parameters and spermatozoal metabolism. Aquaculture 163:163–181. doi:10.1016/S0044-8486(98)00243-9
Lahnsteiner F, Berger B, Weismann T (1999) Sperm metabolism of the teleost fishes Chalcalburnus chalcoides and Oncorhynchus mykiss and its relation to motility and viability. J Exp Zool 284:454–465. doi:10.1002/(SICI)1097-010X(19990901)284:4<454::AID-JEZ12>3.0.CO;2-O
Lahnsteiner F, Berger B, Horvath A et al (2004) Studies on the semen biology and sperm cryopreservation in the sterlet, Acipenser ruthenus L. Aquacult Res 35:519–528. doi:10.1111/j.1365-2109.2004.01034.x
Lessard C, Parent S, Leclerc P et al (2000) Cryopreservation alters the levels of the bull sperm surface protein P25b. J Androl 21:700–707
Li P, Wei QW, Liu L (2008) DNA integrity of Polyodon spathula cryopreserved sperm. J Appl Ichthyol 24:121–125. doi:10.1111/j.1439-0426.2007.01025.x
Linhart O, Walford J, Sivaloganathan B et al (1999) Effects of osmolality and ions on the motility of stripped and testicular of freshwater- and seawater-acclimated tilapia, Oreochromis mossambicus. J Fish Biol 55:1344–1358
Loir M, Labbé C, Maisse G et al (1990) Proteins of seminal fluid and spermatozoa in the trout (Oncorhynchus mykiss): partial characterization and variations. Fish Physiol Biochem 8:485–495. doi:10.1007/BF00003405
Mak M, Mak P, Olczak M et al (2004) Isolation, characterization, and cDNA sequencing of alpha-1-antiproteinase-like protein from rainbow trout seminal plasma. Biochim Biophys Acta 1671:93–105
Mansour N, Lahnsteiner F, Berger B (2003) Metabolism of intratesticular spermatozoa of a tropical teleost fish (Clarias gariepinus). Comp Biochem Physiol B 135:285–296. doi:10.1016/S1096-4959(03)00083-6
Meryman HT, Williams RJ, Douglas MS (1977) Freezing injury from “solution effects” and its prevention by natural or artificial cryoprotection. Cryobiology 14:287–302
Miller RL (1985) Sperm chemo-orientation in metazoa. In: Metz CB, Monroy A (eds) Biology of fertilization. Academic Press, New York
Mitchell DR (2000) Chlamydomaona flagella. J Physiol 36:261–273
Mochida K, Kondo T, Matsubara T et al (1999) A high molecular weight glycoprotein in seminal plasma is a sperm immobilizing factor in the teleost Nile tilapia, Oreochromis niloticus. Dev Growth Differ 41:619–627. doi:10.1046/j.1440-169x.1999.00463.x
Mochida K, Matsubara T, Kudo H et al (2002) A novel seminal plasma glycoprotein of a teleost, the Nile tilapia (Oreochromis niloticus), contains a partial von Willebrand factor type D domain and a zona pellucida-like domain. Mol Reprod Dev 62:57–68. doi:10.1002/mrd.10071
Morisawa M (1994) Cell signaling mechanisms for sperm motility. Zool Sci 11:647–662
Morisawa M, Ishida K (1987) Short-term changes in levels of cyclic AMP, adenylate cyclase, and phosphodiesterase during the initiation of sperm motility in rainbow trout. J Exp Zool 242:199–204. doi:10.1002/jez.1402420211
Morisawa M, Morisawa S (1990) Acquisition and initiation of sperm motility. In: Gagnon C (ed) Controls of sperm motility: biological and clinical aspects. CRC Press, Boca Raton, pp 137–151
Morita M, Takemura A, Nakajima A et al (2006) Microtubule sliding movement in Tilapia sperm flagella axoneme is regulated by Ca2+/Calmodulin-dependent protein phosphorylation. Cell Motil Cytoskeleton 63:459–470. doi:10.1002/cm.20137
Morris GJ, Watson PF (1984) Cold shock injury—a comprehensive bibliography. Cryo Lett 5:352–372
Müller P, Erlemann KR, Müller K et al (1998) Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles. Eur Biophys J 27:33–41. doi:10.1007/s002490050108
Mungan NA, Mungan G, Basar MM et al (2001) Effect of seminal plasma calcitonin levels on sperm motility. Arch Androl 47:113–117. doi:10.1080/014850101316901316
Nayernia K, Diaconu M, Aumüller G et al (2004) Phospholipid hydroperoxide glutathione peroxidase: expression pattern during testicular development in mouse and evolutionary conservation in spermatozoa. Mol Reprod Dev 67:458–464. doi:10.1002/mrd.20039
Oda S, Igarashi Y, Manaka et al (1998) Sperm-activating proteins obtained from the herring eggs are homologous to trypsin inhibitors and synthesized in follicle cells. Dev Biol 204:55–63. doi:10.1006/dbio.1998.9056
Ohkawa K, Inaba K, Morisawa M (1997) Purification and characterization of 26S proteasomes from sperm flagella of chum salmon and its roles in the regulation of sperm motility. Biomed Res 18:353–363
Osaki A, Okida N, Ishikawa K et al (1999) Identification of ubiquitin in seminal plasma from tilapia, Oreochromis niloticus. Biomed Res 20:249–252
Paju A, Bjartell A, Zhang WM et al (2000) Expression and characterization of trypsinogen produced in the human male genital tract. Am J Pathol 157:2011–2021
Pearse AS (1950) The emigrations of animals from the sea. Sherwood, New York
Pietrobon EO, Dominguez LA, Vincenti AE et al (2001) Detection of the mouse acrosome reaction by acid phosphatase Comparison with chlortetracycline and electron microscopy. J Androl 22:96–103
Piros B, Glogowski J, Kolman R et al (2002) Biochemical characterization of Siberian sturgeon Acipenser baeri and sterlet, Acipenser ruthenus, milt plasma and spermatozoa. Fish Physiol Biochem 26:289–295. doi:10.1023/A:1026280218957
Potempa J, Korzus E, Travis J (1994) The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J Biol Chem 269:15957–15960
Psenicka M, Alavi SMH, Rodina M et al (2007) Morphology and ultrastructure of Siberian sturgeon, Acipenser baerii, spermatozoa using scanning and transmission electron microscopy. Biocell 99:103–115
Punnett T, Miller RL, Yoo BH (1992) Partial purification and some chemical properties of the sperm chemoattractant from the forcipulate starfish Pycnopodia helianthoides (Brandt, 1835). J Exp Zool 262:87–96. doi:10.1002/jez.1402620112
Raijmakers MTM, Roelofs HMJ, Steegers EAP et al (2003) Glutathione and gluthatione S-transferases A1-1 and P1-1 in seminal plasma may play a role in protecting against oxidative damage to spermatozoa. Fertil Steril 79:169–172. doi:10.1016/S0015-0282(02)04404-7
Salzberger Z, Lewin LM, Shalgi R (1992) Loss of acid phosphatase from rat spermatozoa as a method for assessing the acrosome reaction. Andrologia 24:155–159
Sarosiek B, Ciereszko A, Kolman R et al (2004) Characteristics of arylsulfatase present in Russian sturgeon (Acipenser gueldenstaedti Brandt) semen. Comp Biochem Physiol B 139:571–579. doi:10.1016/j.cbpc.2004.03.016
Sarosiek B, Wysocka J, Wysocki P et al (2006) Characteristics of acid phosphatase from Russian sturgeon (Acipenser gueldenstaedii) spermatozoa. J Appl Ichthyol 22[Suppl 1]:375–379. doi:10.1111/j.1439-0426.2007.00989.x
Satorre MM, Breininger E, Beconi MT et al (2007) α-Tocopherol modifies tyrosine phosphorylation and capacitation-like state of cryopreserved porcine sperm. Theriogenology 68:958–965. doi:10.1016/j.theriogenology.2007.06.021
Saudrais C, Fierville F, Loir M et al (1998) The use of phosphocreatine plus ADP as energy source for motility of membrane-deprived trout spermatozoa. Cell Motil Cytoskeleton 41:91–106 doi:10.1002/(SICI)1097-0169(1998)41:2<91::AID-CM1>3.0.CO;2-I
Schiller J, Arnhold J, Glander HJ et al (2000) Lipid analysis of human spermatozoa and seminal plasma by MALDI-TOF mass spectrometry and NMR spectroscopy-effects of freezing and thawing. Chem Phys Lipids 106:145–156. doi:10.1016/S0009-3084(00)00148-1
Schöneck C, Braun J, Einspanier R (1996) Sperm viability is influenced in vitro by the bovine seminal protein a SFP: effects on motility, mitochondrial activity and lipid peroxidation. Theriogenology 45:633–642. doi:10.1016/0093-691X(95)00409-2
Schuffner A, Morshedi M, Oehninger S (2001) Cryopreservation of fractionated, highly motile human spermatozoa: effect on membrane phosphatidylserine externalization and lipid peroxidation. Hum Reprod 16:2148–2153. doi:10.1093/humrep/16.10.2148
Smith EF (2002) Regulation of flagellar dynein by calcium and a role for an axonemal calmodulin and calmodulin-dependent kinase. Mol Biol Cell 13:3303–3313. doi:10.1091/mbc.E02-04-0185
Suquet M, Dreanno C, Petton B et al (1998) Long-term effects of the cryopreservation of turbot (Psetta maxima) spermatozoa. Aquat Living Resour 11:45–48. doi:10.1016/S0990-7440(99)80030-8
Suquet M, Dreanno C, Fauvel C et al (2000) Cryopreservation of sperm in marine fish. Aquacult Res 31:231–243. doi:10.1046/j.1365-2109.2000.00445.x
Swann K, Parrington J (1999) Mechanism of Ca2+ release at fertilization in mammals. J Exp Zool 285:267–275. doi:10.1002/(SICI)1097-010X(19991015)285:3<267::AID-JEZ10>3.0.CO;2-P
Takai H, Morisawa M (1995) Change in intracellular K+ concentration caused by external osmolality change regulates sperm motility of marine and freshwater teleosts. J Cell Biol 126:737–745
Tanimoto S, Kudo R, Nagazawa T et al (1994) Implication that potassium flux and increase in intracellular calcium are necessary for the initiation of sperm motility in salmonid fishes. Mol Reprod Dev 39:409–414. doi:10.1002/mrd.1080390409
Terner C, Korsh G (1963) The oxidative metabolism of pyruvate, acetate and glucose in isolated fish spermatozoa. J Cell Comp Physiol 62:243–249. doi:10.1002/jcp.1030620303
Tibbs J (1959) The adenosine triphosphatase activity of perch sperm flagella. Biochim Biophys Acta 33:220. doi:10.1016/0006-3002(59)90517-7
Thomas P, Breckenridge-Miller D, Detweiler C (1997) Binding characteristics and regulation of the 17, 20ß, 21-trihydroxy–4-pregnen-3-one (20β-S) receptor on testicular and sperm plasma membranes of spotted seatrout (Cynoscion nebulosus). Fish Physiol Biochem 17:109–116. doi:10.1023/A:1007781128677
Tombes RM, Shapiro BM (1989) Energy transport and cell polarity: relationship of phosphagen kinase activity to sperm function. J Exp Zool 251:82–90. doi:10.1002/jez.1402510110
Tulsiani DRP, Yoshida-Komiya H, Araki Y (1997) Mammalian fertilization: a carbohydrate-mediated event. Biol Reprod 57:487–494. doi:10.1095/biolreprod57.3.487
Urner F, Sakkas D (2003) Protein phosphorylation in mammalian spermatozoa. Reproduction 125:17–26. doi:10.1530/rep.0.1250017
Vines CA, Yoshida M, Griffin FJ et al (2002) Motility initiation in herring sperm is regulated by reverse sodium-calcium exchange. Proc Natl Acad Sci USA 99:2026–2031. doi:10.1073/pnas.042700899
Visconti PE, Bailey JL, Moore GD et al (1995a) Capacitation of mouse spermatozoa. 1. Correlation between the capacitation state and protein–tyrosine phosphorylation. Development 121:1129–1137
Visconti PE, Moore GD, Baley JL et al (1995b) Capacitation of mouse spermatozoa. 2. Protein–tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 121:1139–1150
Vitali G, Parente R, Melotti C (1995) Carnitine supplementation in human idiopathic asthenospermia: clinical results. Drugs Exp Clin Res 21:157–159
Ward GE, Brokaw CJ, Garbers DL et al (1985) Chemotaxis of Arbacia punctulata spermatozoa to resact, a peptide from the egg jelly layer. J Cell Biol 101:2324–2329. doi:10.1083/jcb.101.6.2324
Wennemuth ED, Meinhardt A, Mallidis C et al (2001) Assessment of fibronectin as a potential new clinical tool in andrology. Andrologia 33:43–46. doi:10.1046/j.1439-0272.2001.00370.x
Wojtczak M, Dietrich GJ, Ciereszko A (2005) Transferrin and antiproteases are major proteins of common carp seminal plasma. Fish Shellfish Immunol 19:387–391. doi:10.1016/j.fsi.2005.01.009
Wojtczak M, Calka J, Glogowski J et al (2007) Isolation and characterization of α1-proteinase inhibitor from common carp (Cyprinus carpio) seminal plasma. Comp Biochem Physiol B 148:264–276. doi:10.1016/j.cbpb.2007.06.004
Yamamoto TO (1961) Physiology of fertilization in fish eggs. Int Rev Cytol 12:361–405. doi:10.1016/S0074-7696(08)60545-8
Yoshida K, Inaba K, Ohtake H et al (1999) Purification and characterization of prolyl endopeptidase from the Pacific herring, Clupea pallasi, and its role in the activation of sperm motility. Dev Growth Differ 41:217–225. doi:10.1046/j.1440-169x.1999.00424.x
Yousef GM, Diamandis M, Jung K et al (2001) Molecular cloning of a novel human acid phosphatase gene (ACPT) that is highly expressed in the testis. Genomics 74:385–395. doi:10.1006/geno.2001.6556
Zilli L, Schiavone R, Zonno V et al (2004) Adenosine triphosphate concentration and β-d-glucuronidase activity as indicators of sea bass semen quality. Biol Reprod 70:1679–1684. doi:10.1095/biolreprod.103.027177
Zilli L, Schiavone R, Zonno V et al (2005) Effect of cryopreservation on sea bass sperm proteins. Biol Reprod 72:1262–1267. doi:10.1095/biolreprod.104.036202
Acknowledgements
This study was financially supported by USB RIFCH No: MSM 6007665809 and the Granting Agency of the Czech Academy of Science No: IAA608030801.
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Li, P., Hulak, M. & Linhart, O. Sperm proteins in teleostean and chondrostean (sturgeon) fishes. Fish Physiol Biochem 35, 567–581 (2009). https://doi.org/10.1007/s10695-008-9261-y
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DOI: https://doi.org/10.1007/s10695-008-9261-y
Keywords
- Protein
- Spermatozoa
- Seminal plasma
- Motility
- Fertilisation
- Cryopreservation