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Volumn 43, Issue 3, 1996, Pages 366-375

Sperm protein (sp50) binds to acrosome and plasma membranes in a Ca2+-dependent manner: Possible role in acrosome reaction

Author keywords

Annexin like sperm; Calcium dependent proteins; Capacitation; Exocytosis; Testicular proteins

Indexed keywords

CAVIA PORCELLUS; MAMMALIA; SUS SCROFA; ANIMALIA;

EID: 0029989273     PISSN: 1040452X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1098-2795(199603)43:3<366::aid-mrd11>3.0.co;2-%23     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 0024149836 scopus 로고
    • Analysis of calmodulin acceptor proteins and the influence of calmodulin antagonists on human spermatozoa
    • Aitken RJ, Clarkson JS, Hulme MJ, Henderson CJ (1988): Analysis of calmodulin acceptor proteins and the influence of calmodulin antagonists on human spermatozoa. Gamete Res 21:93-111.
    • (1988) Gamete Res , vol.21 , pp. 93-111
    • Aitken, R.J.1    Clarkson, J.S.2    Hulme, M.J.3    Henderson, C.J.4
  • 2
    • 0026552098 scopus 로고
    • Annexins IV (p32) and VI (p38) interact with erythrocyte membrane in a calcium-dependent manner
    • Bandorowicz J, Pikula S, Sobota A (1992): Annexins IV (p32) and VI (p38) interact with erythrocyte membrane in a calcium-dependent manner. Biochim Biophys Acta 1105:201-206.
    • (1992) Biochim Biophys Acta , vol.1105 , pp. 201-206
    • Bandorowicz, J.1    Pikula, S.2    Sobota, A.3
  • 3
    • 0014123988 scopus 로고
    • Membrane vesiculation as a feature of the mammalian acrosome reaction
    • Barros C, Bedford JM, Franklin LE, Austin CR (1967): Membrane vesiculation as a feature of the mammalian acrosome reaction. J Cell Biol 34:C1-C5.
    • (1967) J Cell Biol , vol.34
    • Barros, C.1    Bedford, J.M.2    Franklin, L.E.3    Austin, C.R.4
  • 4
    • 0020973213 scopus 로고
    • Proteins involved in membrane-cytoskeleton association in human erythrocytes: Spectrin, ankyrin, and band 3
    • Bennett V (1983): Proteins involved in membrane-cytoskeleton association in human erythrocytes: Spectrin, ankyrin, and band 3. Methods Enzymol 96:313-324.
    • (1983) Methods Enzymol , vol.96 , pp. 313-324
    • Bennett, V.1
  • 5
    • 0024273763 scopus 로고
    • Calpactin-like proteins in human spermatozoa
    • Berruti G (1988): Calpactin-like proteins in human spermatozoa. Exp Cell Res 179:374-384.
    • (1988) Exp Cell Res , vol.179 , pp. 374-384
    • Berruti, G.1
  • 6
    • 0026410168 scopus 로고
    • 2+-mediated F-actin/phospholipid binding of human sperm calpactin II
    • 2+-mediated F-actin/phospholipid binding of human sperm calpactin II. Cell Biol Int Rep 15:917-927.
    • (1991) Cell Biol Int Rep , vol.15 , pp. 917-927
    • Berruti, G.1
  • 7
    • 0025195030 scopus 로고
    • 2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins
    • 2+-dependent phospholipid binding, vesicle aggregation and membrane fusion by annexins. Biochem J 266:195-200.
    • (1990) Biochem J , vol.266 , pp. 195-200
    • Blackwood, R.A.1    Ernst, J.D.2
  • 8
    • 0023440964 scopus 로고
    • Regulation of sperm flagellar motility by calcium and cAMP-dependent phosphorylation
    • Brokaw CJ (1987): Regulation of sperm flagellar motility by calcium and cAMP-dependent phosphorylation. J Cell Biochem 35:175-184.
    • (1987) J Cell Biochem , vol.35 , pp. 175-184
    • Brokaw, C.J.1
  • 9
    • 0021814750 scopus 로고
    • Modulation of the asymmetry of sea urchin sperm flagellar bending by calmodulin
    • Brokaw CJ, Nagayama SM (1985): Modulation of the asymmetry of sea urchin sperm flagellar bending by calmodulin. J Cell Biol 100: 1875-1883.
    • (1985) J Cell Biol , vol.100 , pp. 1875-1883
    • Brokaw, C.J.1    Nagayama, S.M.2
  • 10
    • 0026060508 scopus 로고
    • Calcium, the cytoskeleton and calpactin (annexin II) in exocytotic secretion from adrenal chromaffin and mammary epithelial cells
    • Burgoyne RD, Handel SE, Morgan A, Rennison ME, Turner MD, Wilde CJ (1991): Calcium, the cytoskeleton and calpactin (annexin II) in exocytotic secretion from adrenal chromaffin and mammary epithelial cells. Biochem Soc Trans 19:1085-1089.
    • (1991) Biochem Soc Trans , vol.19 , pp. 1085-1089
    • Burgoyne, R.D.1    Handel, S.E.2    Morgan, A.3    Rennison, M.E.4    Turner, M.D.5    Wilde, C.J.6
  • 12
    • 0022737848 scopus 로고
    • Immunocytochemical localization of calmodulin in intact and acrosome-reacted boar sperm
    • Camatini M, Anelli G, Casala A (1986): Immunocytochemical localization of calmodulin in intact and acrosome-reacted boar sperm. Eur J Cell Biol 41:89-96.
    • (1986) Eur J Cell Biol , vol.41 , pp. 89-96
    • Camatini, M.1    Anelli, G.2    Casala, A.3
  • 13
    • 0026452240 scopus 로고
    • The annexins and exocytosis
    • Creutz CE (1992): The annexins and exocytosis. Science 258:924-931
    • (1992) Science , vol.258 , pp. 924-931
    • Creutz, C.E.1
  • 14
    • 0020620214 scopus 로고
    • Calcium dependence of the binding of synexin to isolated chromaffin granules
    • Creutze CE, Sterner DC (1983): Calcium dependence of the binding of synexin to isolated chromaffin granules. Biochem Biophys Res Commun 114:335-364.
    • (1983) Biochem Biophys Res Commun , vol.114 , pp. 335-364
    • Creutze, C.E.1    Sterner, D.C.2
  • 15
    • 0025306172 scopus 로고
    • Protein terminology tangle
    • Crumpton MJ, Dedman JR (1990): Protein terminology tangle. Nature 345:212.
    • (1990) Nature , vol.345 , pp. 212
    • Crumpton, M.J.1    Dedman, J.R.2
  • 16
    • 0020514396 scopus 로고
    • Detection of antigens on nitrocellulose paper immunoblots with monoclonal antibodies
    • De Blas AL, Cherwinski HM (1983): Detection of antigens on nitrocellulose paper immunoblots with monoclonal antibodies. Anal Biochem 133:214-219.
    • (1983) Anal Biochem , vol.133 , pp. 214-219
    • De Blas, A.L.1    Cherwinski, H.M.2
  • 18
    • 0023818448 scopus 로고
    • Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
    • Drust DS, Creutz CE (1988): Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature 331:88-91.
    • (1988) Nature , vol.331 , pp. 88-91
    • Drust, D.S.1    Creutz, C.E.2
  • 20
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcome virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke V, Weber K (1984): Identity of p36K phosphorylated upon Rous sarcome virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J 3:227-233.
    • (1984) EMBO J , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 22
    • 0022928659 scopus 로고
    • 2+ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core
    • 2+ binding by the 36-kDa tyrosine kinase substrate (calpactin) and its 33-kDa core. J Biol Chem 261:7247-7252.
    • (1986) J Biol Chem , vol.261 , pp. 7247-7252
    • Glenney, J.1
  • 23
    • 0023139338 scopus 로고
    • 2+ -regulated phospholipid- and actin-binding proteins isolated from lung and placenta
    • 2+ -regulated phospholipid- and actin-binding proteins isolated from lung and placenta. J Cell Biol 104:503-511.
    • (1987) J Cell Biol , vol.104 , pp. 503-511
    • Glenney Jr., J.R.1    Tack, B.2    Powell, M.A.3
  • 25
    • 0015582075 scopus 로고
    • Selective solubilization of mammalian spermatozoa structures
    • Hernández-Montes H, Iglesias G, Mújica A (1973): Selective solubilization of mammalian spermatozoa structures. Exp Cell Res 76:437-440.
    • (1973) Exp Cell Res , vol.76 , pp. 437-440
    • Hernández-Montes, H.1    Iglesias, G.2    Mújica, A.3
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970): Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0022989609 scopus 로고
    • Calcimedins: Purification and characterization from chicken gizzard and rat and bovine livers
    • Mathew JK, Krolak JM, Dedman JR (1986): Calcimedins: Purification and characterization from chicken gizzard and rat and bovine livers. J Cell Biochem 32:223-234.
    • (1986) J Cell Biochem , vol.32 , pp. 223-234
    • Mathew, J.K.1    Krolak, J.M.2    Dedman, J.R.3
  • 31
    • 0021153302 scopus 로고
    • Calmodulin, and calmodulin acceptor protein, and calcimedins: Unique antibody localizations in hamster sperm
    • Moore PB, Dedman JR (1984): Calmodulin, and calmodulin acceptor protein, and calcimedins: Unique antibody localizations in hamster sperm. J Cell Biochem 25:99-107.
    • (1984) J Cell Biochem , vol.25 , pp. 99-107
    • Moore, P.B.1    Dedman, J.R.2
  • 32
    • 0026662066 scopus 로고
    • F-actin in guinea pig spermatozoa: Its role in calmodulin translocation during acrosome reaction
    • Moreno-Fierros L, Hernández EO, Salgado ZO, Mújica A (1992): F-actin in guinea pig spermatozoa: Its role in calmodulin translocation during acrosome reaction. Mol Reprod Dev 33:172-181.
    • (1992) Mol Reprod Dev , vol.33 , pp. 172-181
    • Moreno-Fierros, L.1    Hernández, E.O.2    Salgado, Z.O.3    Mújica, A.4
  • 33
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey JH (1981): Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity. Anal Biochem 117:307-310.
    • (1981) Anal Biochem , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 34
    • 0024006716 scopus 로고
    • Calcium dependence of human sperm fertilizing ability
    • Mortimer D (1988): Calcium dependence of human sperm fertilizing ability. J Exp Zool 246:194-201.
    • (1988) J Exp Zool , vol.246 , pp. 194-201
    • Mortimer, D.1
  • 35
    • 0021037294 scopus 로고
    • On the role of glucose in capacitation and acrosomal reaction of guinea pig sperm
    • Mújica A, Valdes-Ruíz M (1983): On the role of glucose in capacitation and acrosomal reaction of guinea pig sperm. Gamete Res 8:335-344.
    • (1983) Gamete Res , vol.8 , pp. 335-344
    • Mújica, A.1    Valdes-Ruíz, M.2
  • 36
    • 0025160854 scopus 로고
    • Synexin (annexin VH): A cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes
    • Pollard HB, Burns AL, Rojas E (1990): Synexin (annexin VH): A cytosolic calcium-binding protein which promotes membrane fusion and forms calcium channels in artificial bilayer and natural membranes. J Membr Biol 117:101-112.
    • (1990) J Membr Biol , vol.117 , pp. 101-112
    • Pollard, H.B.1    Burns, A.L.2    Rojas, E.3
  • 37
    • 0025635905 scopus 로고
    • Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes
    • Rojas E, Pollard HB, Haigler HT, Parra C, Burns AL (1990): Calcium-activated endonexin II forms calcium channels across acidic phospholipid bilayer membranes. J Biol Chem 265:21207-21215.
    • (1990) J Biol Chem , vol.265 , pp. 21207-21215
    • Rojas, E.1    Pollard, H.B.2    Haigler, H.T.3    Parra, C.4    Burns, A.L.5
  • 38
    • 0018133423 scopus 로고
    • Calcium-dependent binding of mouse epididymal spermatozoa to the zona pellucida
    • Saling PM, Storey BT, Wolf DP (1978): Calcium-dependent binding of mouse epididymal spermatozoa to the zona pellucida. Dev Biol 65: 515-525.
    • (1978) Dev Biol , vol.65 , pp. 515-525
    • Saling, P.M.1    Storey, B.T.2    Wolf, D.P.3
  • 39
    • 0021997305 scopus 로고
    • Synexin binds in a calcium-dependent fashion to oriented chromaffin cell plasma membranes
    • Scott JH, Creutz CE, Pollard HB, Ornberg R (1985): Synexin binds in a calcium-dependent fashion to oriented chromaffin cell plasma membranes. FEBS Lett 180:17-23.
    • (1985) FEBS Lett , vol.180 , pp. 17-23
    • Scott, J.H.1    Creutz, C.E.2    Pollard, H.B.3    Ornberg, R.4
  • 40
    • 0024146951 scopus 로고
    • Phospholipid composition of isolated guinea pig sperm outer acrosomal membrane and plasma membrane during capacitation in vitro
    • Stojanoff A, Bourn H, Andrews AG, Hyne RN (1988): Phospholipid composition of isolated guinea pig sperm outer acrosomal membrane and plasma membrane during capacitation in vitro. Gamete Res 21:297-311.
    • (1988) Gamete Res , vol.21 , pp. 297-311
    • Stojanoff, A.1    Bourn, H.2    Andrews, A.G.3    Hyne, R.N.4
  • 41
    • 0021715640 scopus 로고
    • 2+-regulated proteins with a possible role in cytotoxic processes
    • 2+-regulated proteins with a possible role in cytotoxic processes. Biochem Soc Trans 12:972-974.
    • (1984) Biochem Soc Trans , vol.12 , pp. 972-974
    • Südhof, T.C.1
  • 42
    • 0024329482 scopus 로고
    • Protein phosphorylation: The second messenger signal transducer of flagellar motility
    • Tash JS (1989): Protein phosphorylation: The second messenger signal transducer of flagellar motility. Cell Motil Cytoskeleton 14:332-339.
    • (1989) Cell Motil Cytoskeleton , vol.14 , pp. 332-339
    • Tash, J.S.1
  • 43
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979): Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 44
    • 0025179017 scopus 로고
    • Changes in calmodulin compartmentalization throughout capacitation and acrosome reaction in guinea pig spermatozoa
    • Trejo R, Mújica A (1990): Changes in calmodulin compartmentalization throughout capacitation and acrosome reaction in guinea pig spermatozoa. Mol Reprod Dev 26:366-376.
    • (1990) Mol Reprod Dev , vol.26 , pp. 366-376
    • Trejo, R.1    Mújica, A.2
  • 45
    • 0018253891 scopus 로고
    • Calcium requirement for sperm-egg fusion in mammals
    • Yanagimachi R (1978): Calcium requirement for sperm-egg fusion in mammals. Biol Reprod 19:949-958.
    • (1978) Biol Reprod , vol.19 , pp. 949-958
    • Yanagimachi, R.1
  • 46
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • E Knobil, JD Niell, LL Ewing, GS Greenwald, CL Markert, DW Pfaff (eds): New York: Raven Press
    • Yanagimachi R (1988): Mammalian fertilization. In E Knobil, JD Niell, LL Ewing, GS Greenwald, CL Markert, DW Pfaff (eds): "The Physiology of Reproduction," Volume 1. New York: Raven Press, pp 135-185.
    • (1988) The Physiology of Reproduction , vol.1 , pp. 135-185
    • Yanagimachi, R.1
  • 47
    • 0016132946 scopus 로고
    • Calcium dependence of the acrosome reaction and activation of guinea pig spermatozoa
    • Yanagimachi R, Usui N (1974): Calcium dependence of the acrosome reaction and activation of guinea pig spermatozoa. Exp Cell Res 89:161-174.
    • (1974) Exp Cell Res , vol.89 , pp. 161-174
    • Yanagimachi, R.1    Usui, N.2
  • 48
    • 0025210431 scopus 로고
    • Evaluation of the annexins as potential mediators of membrane fusion in exocytosis
    • Zaks WJ, Creutz CE (1990): Evaluation of the annexins as potential mediators of membrane fusion in exocytosis. J Bioenerg Biomembr 22:97-120.
    • (1990) J Bioenerg Biomembr , vol.22 , pp. 97-120
    • Zaks, W.J.1    Creutz, C.E.2


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