메뉴 건너뛰기




Volumn 157, Issue 1, 2010, Pages 127-136

Isolation, characterization and cDNA sequencing of acrosin from turkey spermatozoa

Author keywords

Acrosin; CDNA; Semen; Turkey

Indexed keywords

ACROSIN; APROTININ; COMPLEMENTARY DNA; ENZYME PRECURSOR; GLYCOPROTEIN; PROACROSIN; PROLINE; PROTEIN PRECURSOR; SERINE PROTEINASE; SIGNAL PEPTIDE; UREA; AMIDASE; GELATINASE;

EID: 77954143495     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2010.05.011     Document Type: Article
Times cited : (19)

References (51)
  • 1
    • 0028017503 scopus 로고
    • Purification and characterization of a novel acrosin-like enzyme from boar cauda epididymal sperm
    • Akama K., Terao K., Tanaka Y., Noguchi A., Yonezawa N., Nakano M., Tobita T.J. Purification and characterization of a novel acrosin-like enzyme from boar cauda epididymal sperm. J. Biochem. 1994, 116:464-470.
    • (1994) J. Biochem. , vol.116 , pp. 464-470
    • Akama, K.1    Terao, K.2    Tanaka, Y.3    Noguchi, A.4    Yonezawa, N.5    Nakano, M.6    Tobita, T.J.7
  • 3
    • 0024500198 scopus 로고
    • Primary structure of human proacrosin deduced from its cDNA sequence
    • Baba T., Watanabe K., Kashiwabara S., Arai Y. Primary structure of human proacrosin deduced from its cDNA sequence. FEBS Lett. 1989, 244:296-300.
    • (1989) FEBS Lett. , vol.244 , pp. 296-300
    • Baba, T.1    Watanabe, K.2    Kashiwabara, S.3    Arai, Y.4
  • 4
    • 55949101975 scopus 로고    scopus 로고
    • Adaptive evolution of gamete-recognition proteins in birds
    • Berlin S., Qu L., Ellegren H.J. Adaptive evolution of gamete-recognition proteins in birds. J. Mol. Evol. 2008, 67:488-496.
    • (2008) J. Mol. Evol. , vol.67 , pp. 488-496
    • Berlin, S.1    Qu, L.2    Ellegren, H.J.3
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0018160949 scopus 로고
    • Studies on ram acrosin. Activation of proacrosin accompanying the isolation of acrosin from spermatozoa, and purification of the enzyme by affinity chromatography
    • Brown C.R., Hartree E.F. Studies on ram acrosin. Activation of proacrosin accompanying the isolation of acrosin from spermatozoa, and purification of the enzyme by affinity chromatography. Biochem. J. 1978, 175:227-238.
    • (1978) Biochem. J. , vol.175 , pp. 227-238
    • Brown, C.R.1    Hartree, E.F.2
  • 7
    • 0002925172 scopus 로고
    • The collection of spermatozoa from the domestic fowl and turkey
    • Burrows W.H., Quinns J.P. The collection of spermatozoa from the domestic fowl and turkey. Poult. Sci. 1937, 16:19-24.
    • (1937) Poult. Sci. , vol.16 , pp. 19-24
    • Burrows, W.H.1    Quinns, J.P.2
  • 8
    • 15844402755 scopus 로고    scopus 로고
    • Serine protease activity, bovine sperm protease, 66kDa (BSp66), is present in hamster sperm and is involved in sperm-zona interaction
    • Cesari A., Katunar M.R., Monclus M.A., Vincenti A., de Rosas J.C., Fornés M.W. Serine protease activity, bovine sperm protease, 66kDa (BSp66), is present in hamster sperm and is involved in sperm-zona interaction. Reproduction 2005, 129:291-298.
    • (2005) Reproduction , vol.129 , pp. 291-298
    • Cesari, A.1    Katunar, M.R.2    Monclus, M.A.3    Vincenti, A.4    de Rosas, J.C.5    Fornés, M.W.6
  • 9
    • 33644864110 scopus 로고
    • P-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin
    • Chase T., Shaw E. p-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin. Biochem. Biophys. Res. Commun. 1967, 29:508-514.
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 508-514
    • Chase, T.1    Shaw, E.2
  • 11
    • 0029763097 scopus 로고    scopus 로고
    • Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa
    • Ciereszko A., Dabrowski K., Ochkur S.I. Characterization of acrosin-like activity of lake sturgeon (Acipenser fulvescens) spermatozoa. Mol. Reprod. Dev. 1996, 45:72-77.
    • (1996) Mol. Reprod. Dev. , vol.45 , pp. 72-77
    • Ciereszko, A.1    Dabrowski, K.2    Ochkur, S.I.3
  • 12
    • 0002260003 scopus 로고    scopus 로고
    • Effects of season and dietary ascorbic acid on some biochemical characteristics of rainbow trout (Oncorhynchus mykiss) semen
    • Ciereszko A., Liu L., Dabrowski K. Effects of season and dietary ascorbic acid on some biochemical characteristics of rainbow trout (Oncorhynchus mykiss) semen. Fish Physiol. Biochem. 1996, 15:1-10.
    • (1996) Fish Physiol. Biochem. , vol.15 , pp. 1-10
    • Ciereszko, A.1    Liu, L.2    Dabrowski, K.3
  • 13
    • 0032435908 scopus 로고    scopus 로고
    • Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood
    • Ciereszko A., Piros B., Dabrowski K., Kucharczyk D., Łuczyński M.J., Dobosz S., Glogowski J. Serine proteinase inhibitors of seminal plasma of teleost fish: distribution of activity, electrophoretic profiles and relation to proteinase inhibitors of blood. J. Fish Biol. 1998, 53:1292-1305.
    • (1998) J. Fish Biol. , vol.53 , pp. 1292-1305
    • Ciereszko, A.1    Piros, B.2    Dabrowski, K.3    Kucharczyk, D.4    Łuczyński, M.J.5    Dobosz, S.6    Glogowski, J.7
  • 14
    • 0020189573 scopus 로고
    • Effects of holding temperature and storage time on respiratory rate, motility, and fertility of chicken and turkey semen
    • Clarke R.N., Sexton T.J., Ottinger M.A. Effects of holding temperature and storage time on respiratory rate, motility, and fertility of chicken and turkey semen. Poult. Sci. 1982, 61:1912-1917.
    • (1982) Poult. Sci. , vol.61 , pp. 1912-1917
    • Clarke, R.N.1    Sexton, T.J.2    Ottinger, M.A.3
  • 16
    • 0033756003 scopus 로고    scopus 로고
    • Changes in turkey semen lipids during liquid in vitro storage
    • Douard V., Hermier D., Blesbois E. Changes in turkey semen lipids during liquid in vitro storage. Biol. Reprod. 2000, 63:1450-1456.
    • (2000) Biol. Reprod. , vol.63 , pp. 1450-1456
    • Douard, V.1    Hermier, D.2    Blesbois, E.3
  • 17
    • 0347659445 scopus 로고    scopus 로고
    • Impact of changes in composition of storage medium on lipid content and quality of turkey spermatozoa
    • Douard V., Hermier D., Magistrini M., Labbe C., Blesbois E. Impact of changes in composition of storage medium on lipid content and quality of turkey spermatozoa. Theriogenology 2004, 61:1-13.
    • (2004) Theriogenology , vol.61 , pp. 1-13
    • Douard, V.1    Hermier, D.2    Magistrini, M.3    Labbe, C.4    Blesbois, E.5
  • 18
    • 0025986429 scopus 로고
    • Activation and subsequent degradation of proacrosin is mediated by zona pellucida glycoproteins, negatively charged polysaccharides and DNA
    • Eberspächer U., Gerwien J., Habenicht U.F., Schleuning W.-D., Donner P. Activation and subsequent degradation of proacrosin is mediated by zona pellucida glycoproteins, negatively charged polysaccharides and DNA. Mol. Reprod. Dev. 1991, 30:164-170.
    • (1991) Mol. Reprod. Dev. , vol.30 , pp. 164-170
    • Eberspächer, U.1    Gerwien, J.2    Habenicht, U.F.3    Schleuning, W.-D.4    Donner, P.5
  • 19
    • 0020480240 scopus 로고
    • Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: effect on inhibitor interactions with serine proteinases
    • Empie M.W., Laskowski M. Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: effect on inhibitor interactions with serine proteinases. Biochemistry 1982, 21:2274-2284.
    • (1982) Biochemistry , vol.21 , pp. 2274-2284
    • Empie, M.W.1    Laskowski, M.2
  • 20
    • 0027248268 scopus 로고
    • Rapid amplification of complementary DNA ends for generation of full-length complementary cDNAs: thermal RACE
    • Frohmann M.A. Rapid amplification of complementary DNA ends for generation of full-length complementary cDNAs: thermal RACE. Meths Enzymol. 1993, 218:334-356.
    • (1993) Meths Enzymol. , vol.218 , pp. 334-356
    • Frohmann, M.A.1
  • 21
    • 0025423273 scopus 로고
    • Chicken acrosin: extraction and purification
    • Froman D.P. Chicken acrosin: extraction and purification. Poult. Sci. 1990, 69:812-817.
    • (1990) Poult. Sci. , vol.69 , pp. 812-817
    • Froman, D.P.1
  • 23
    • 0001323267 scopus 로고
    • Trypsin
    • Weinheim, Verlag Chemie, H.U. Bergmeyer (Ed.)
    • Geiger R., Fritz H. Trypsin. Methods of Enzymatic Analysis 1983, 121-124. Weinheim, Verlag Chemie. H.U. Bergmeyer (Ed.).
    • (1983) Methods of Enzymatic Analysis , pp. 121-124
    • Geiger, R.1    Fritz, H.2
  • 24
    • 0035883314 scopus 로고    scopus 로고
    • Acrosin activity in turkey spermatozoa: assay by clinical method and effect of zinc and benzamidine on the activity
    • Glogowski J., Jankowski J., Faruga A., Ottobre J.S., Ciereszko A. Acrosin activity in turkey spermatozoa: assay by clinical method and effect of zinc and benzamidine on the activity. Theriogenology 2001, 56:889-901.
    • (2001) Theriogenology , vol.56 , pp. 889-901
    • Glogowski, J.1    Jankowski, J.2    Faruga, A.3    Ottobre, J.S.4    Ciereszko, A.5
  • 25
    • 77049129946 scopus 로고
    • Pancreatic trypsin inhibitor. II. Reaction with trypsin
    • Green N.M., Work E. Pancreatic trypsin inhibitor. II. Reaction with trypsin. Biochem. J. 1953, 54:347-352.
    • (1953) Biochem. J. , vol.54 , pp. 347-352
    • Green, N.M.1    Work, E.2
  • 26
    • 77954142978 scopus 로고    scopus 로고
    • In preparation. Prediction of N-glycosylation sites in human proteins.
    • Gupta, R., Jung, E., Brunak, S., In preparation. Prediction of N-glycosylation sites in human proteins.
    • Gupta, R.1    Jung, E.2    Brunak, S.3
  • 27
    • 0017064920 scopus 로고
    • Biochemical characterization of an avian spermatozoan acrosin and comparison of its properties to those of bovine trypsin and mammalian acrosins
    • Ho J.J., Meizel S. Biochemical characterization of an avian spermatozoan acrosin and comparison of its properties to those of bovine trypsin and mammalian acrosins. Comp. Biochem. Physiol. B. 1976, 54:213-218.
    • (1976) Comp. Biochem. Physiol. B. , vol.54 , pp. 213-218
    • Ho, J.J.1    Meizel, S.2
  • 28
    • 0036751233 scopus 로고    scopus 로고
    • Role of acrosomal matrix proteases in sperm-zona pellucida interactions
    • Honda A., Siruntawineti J., Baba T. Role of acrosomal matrix proteases in sperm-zona pellucida interactions. Hum. Reprod. Update 2002, 8:405-412.
    • (2002) Hum. Reprod. Update , vol.8 , pp. 405-412
    • Honda, A.1    Siruntawineti, J.2    Baba, T.3
  • 29
    • 0026517688 scopus 로고
    • The complete primary structure of three isoforms of a boar sperm-associated acrosin inhibitor
    • Jonakova V., Calvete J.J., Mann K., Schafer W., Schmid E.R., Topfer-Petersen E. The complete primary structure of three isoforms of a boar sperm-associated acrosin inhibitor. FEBS Lett. 1992, 297:147-150.
    • (1992) FEBS Lett. , vol.297 , pp. 147-150
    • Jonakova, V.1    Calvete, J.J.2    Mann, K.3    Schafer, W.4    Schmid, E.R.5    Topfer-Petersen, E.6
  • 30
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites
    • Julenius K., Mølgaard A., Gupta R., Brunak S. Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 2005, 15:153-164.
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Mølgaard, A.2    Gupta, R.3    Brunak, S.4
  • 31
    • 0026058935 scopus 로고
    • Acrosin, the peculiar sperm-specific serine protease
    • Klemm U., Müller-Esterl W., Engel W. Acrosin, the peculiar sperm-specific serine protease. Hum. Genet. 1991, 87:635-641.
    • (1991) Hum. Genet. , vol.87 , pp. 635-641
    • Klemm, U.1    Müller-Esterl, W.2    Engel, W.3
  • 33
    • 14744270463 scopus 로고    scopus 로고
    • Gelatinases and serine proteinase inhibitors of seminal plasma and the reproductive tract of turkey (Meleagris gallopavo)
    • Kotłowska M., Kowalski R., Glogowski J., Jankowski J., Ciereszko A. Gelatinases and serine proteinase inhibitors of seminal plasma and the reproductive tract of turkey (Meleagris gallopavo). Theriogenology 2005, 63:1667-1681.
    • (2005) Theriogenology , vol.63 , pp. 1667-1681
    • Kotłowska, M.1    Kowalski, R.2    Glogowski, J.3    Jankowski, J.4    Ciereszko, A.5
  • 34
    • 33845410704 scopus 로고    scopus 로고
    • Effects of liquid storage on amidase activity, DNA fragmentation and motility of turkey spermatozoa
    • Kotłowska M., Dietrich G., Wojtczak M., Karol H., Ciereszko A. Effects of liquid storage on amidase activity, DNA fragmentation and motility of turkey spermatozoa. Theriogenology 2007, 67:276-286.
    • (2007) Theriogenology , vol.67 , pp. 276-286
    • Kotłowska, M.1    Dietrich, G.2    Wojtczak, M.3    Karol, H.4    Ciereszko, A.5
  • 35
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 1970, 277:680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 1980, 49:593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 37
    • 0018184114 scopus 로고
    • Purification and properties of a proteinase inhibitor from chicken seminal plasma
    • Lessley B.A., Brown K.I. Purification and properties of a proteinase inhibitor from chicken seminal plasma. Biol. Reprod. 1978, 19:223-234.
    • (1978) Biol. Reprod. , vol.19 , pp. 223-234
    • Lessley, B.A.1    Brown, K.I.2
  • 39
    • 0016723571 scopus 로고
    • Proacrosin from rabbit epididymal spermatozoa: partial purification and initial biochemical characterization
    • Meizel S., Mukerji S.K. Proacrosin from rabbit epididymal spermatozoa: partial purification and initial biochemical characterization. Biol. Reprod. 1975, 13:83-93.
    • (1975) Biol. Reprod. , vol.13 , pp. 83-93
    • Meizel, S.1    Mukerji, S.K.2
  • 40
    • 0017227135 scopus 로고
    • Biochemical studies of proacrosin and acrosin from hamster cauda epididymal spermatozoa
    • Meizel S., Mukerji S.K. Biochemical studies of proacrosin and acrosin from hamster cauda epididymal spermatozoa. Biol. Reprod. 1976, 14:444-450.
    • (1976) Biol. Reprod. , vol.14 , pp. 444-450
    • Meizel, S.1    Mukerji, S.K.2
  • 41
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 1997, 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 42
    • 0017365296 scopus 로고
    • Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm
    • Polakoski K.L., Parrish R.F. Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm. J. Biol. Chem. 1977, 252:1888-1894.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1888-1894
    • Polakoski, K.L.1    Parrish, R.F.2
  • 43
    • 77950482175 scopus 로고    scopus 로고
    • Comparative genomic analysis of the zebra finch degradome provides new insights into evolution of proteases in birds and mammals
    • Quesada V., Velasco G., Puente X.S., Warren W.C., López-Otín C. Comparative genomic analysis of the zebra finch degradome provides new insights into evolution of proteases in birds and mammals. BMC Genomics 2010, 11:220.
    • (2010) BMC Genomics , vol.11 , pp. 220
    • Quesada, V.1    Velasco, G.2    Puente, X.S.3    Warren, W.C.4    López-Otín, C.5
  • 44
    • 44849084713 scopus 로고    scopus 로고
    • The molecular evolution of acrosin in placental mammals
    • Raterman D., Springer M.S. The molecular evolution of acrosin in placental mammals. Mol. Reprod. Dev. 2008, 75:1196-1207.
    • (2008) Mol. Reprod. Dev. , vol.75 , pp. 1196-1207
    • Raterman, D.1    Springer, M.S.2
  • 45
    • 0023993353 scopus 로고
    • Turkey acrosin. I. Isolation, purification, and partial characterization
    • Richardson M.E., Bodine A.B., Froman D.P., Thurston R.J. Turkey acrosin. I. Isolation, purification, and partial characterization. Biol. Reprod. 1988, 38:645-651.
    • (1988) Biol. Reprod. , vol.38 , pp. 645-651
    • Richardson, M.E.1    Bodine, A.B.2    Froman, D.P.3    Thurston, R.J.4
  • 46
    • 0026937309 scopus 로고
    • Research note: kinetic and inhibition studies with turkey acrosin
    • Richardson M.E., Korn N., Bodine A.B., Thurston R.J. Research note: kinetic and inhibition studies with turkey acrosin. Poult. Sci. 1992, 71:1789-1793.
    • (1992) Poult. Sci. , vol.71 , pp. 1789-1793
    • Richardson, M.E.1    Korn, N.2    Bodine, A.B.3    Thurston, R.J.4
  • 47
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 1987, 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 48
    • 0021915292 scopus 로고
    • Evaluation of the human sperm proacrosin-acrosin system using gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophesis
    • Siegel M.S., Polakoski K.L. Evaluation of the human sperm proacrosin-acrosin system using gelatin-sodium dodecyl sulfate-polyacrylamide gel electrophesis. Biol. Reprod. 1985, 32:713-720.
    • (1985) Biol. Reprod. , vol.32 , pp. 713-720
    • Siegel, M.S.1    Polakoski, K.L.2
  • 50
    • 0014410887 scopus 로고
    • Characterization of natural inhibitors of trypsin and chymotrypsin by electrophoresis in acrylamide-agarose gels
    • Uriel J., Berges J. Characterization of natural inhibitors of trypsin and chymotrypsin by electrophoresis in acrylamide-agarose gels. Nature 1968, 218:578-580.
    • (1968) Nature , vol.218 , pp. 578-580
    • Uriel, J.1    Berges, J.2
  • 51
    • 0035980106 scopus 로고    scopus 로고
    • Purification and partial peptide sequence analysis of the boar 32kDa sperminogen
    • Yu H., Yi L.S. Purification and partial peptide sequence analysis of the boar 32kDa sperminogen. Mol. Cells 2001, 12:107-111.
    • (2001) Mol. Cells , vol.12 , pp. 107-111
    • Yu, H.1    Yi, L.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.