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Volumn 34, Issue 2, 2012, Pages 126-134

Starting a new life: Sperm PLC-zeta mobilizes the Ca 2+ signal that induces egg activation and embryo development: An essential phospholipase C with implications for male infertility

Author keywords

Calcium signalling; Fertilization; Oocyte activation; Phospholipase C; Sperm

Indexed keywords

CALCIUM; INOSITOL 1,4,5 TRISPHOSPHATE; MEMBRANE LIPID; PHOSPHOLIPASE; PHOSPHOLIPASE C ZETA; UNCLASSIFIED DRUG;

EID: 84855808340     PISSN: 02659247     EISSN: 15211878     Source Type: Journal    
DOI: 10.1002/bies.201100127     Document Type: Review
Times cited : (80)

References (88)
  • 1
    • 0033566185 scopus 로고    scopus 로고
    • Comparative biology of calcium signaling during fertilization and egg activation in animals
    • Stricker SA. 1999. Comparative biology of calcium signaling during fertilization and egg activation in animals. Dev Biol 211: 157-76.
    • (1999) Dev Biol , vol.211 , pp. 157-176
    • Stricker, S.A.1
  • 2
    • 0037092883 scopus 로고    scopus 로고
    • Egg activation at fertilization: where it all begins
    • Runft LL, Jaffe LA, Mehlmann LM. 2002. Egg activation at fertilization: where it all begins. Dev Biol 245: 237-54.
    • (2002) Dev Biol , vol.245 , pp. 237-254
    • Runft, L.L.1    Jaffe, L.A.2    Mehlmann, L.M.3
  • 4
    • 0025637730 scopus 로고
    • A cytosolic sperm factor stimulates repetitive calcium increases and mimics fertilization in hamster eggs
    • Swann K. 1990. A cytosolic sperm factor stimulates repetitive calcium increases and mimics fertilization in hamster eggs. Development 110: 1295-302.
    • (1990) Development , vol.110 , pp. 1295-1302
    • Swann, K.1
  • 6
    • 0026551829 scopus 로고
    • Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg
    • Kline D, Kline JT. 1992. Repetitive calcium transients and the role of calcium in exocytosis and cell cycle activation in the mouse egg. Dev Biol 149: 80-9.
    • (1992) Dev Biol , vol.149 , pp. 80-89
    • Kline, D.1    Kline, J.T.2
  • 8
    • 0028795988 scopus 로고
    • Molecular basis of mammalian egg activation
    • Schultz RM, Kopf GS. 1995. Molecular basis of mammalian egg activation. Curr Top Dev Biol 30: 21-62.
    • (1995) Curr Top Dev Biol , vol.30 , pp. 21-62
    • Schultz, R.M.1    Kopf, G.S.2
  • 9
    • 0023741431 scopus 로고
    • Initiation of the cortical reaction in hamster and sheep oocytes in response to inositol trisphosphate
    • Cran DG, Moor RM, Irvine RF. 1988. Initiation of the cortical reaction in hamster and sheep oocytes in response to inositol trisphosphate. J Cell Sci 91: 139-44.
    • (1988) J Cell Sci , vol.91 , pp. 139-144
    • Cran, D.G.1    Moor, R.M.2    Irvine, R.F.3
  • 10
    • 0031594507 scopus 로고    scopus 로고
    • 2+ oscillations in the activation of the egg and development of the embryo in mammals
    • 2+ oscillations in the activation of the egg and development of the embryo in mammals. Int J Dev Biol 42: 1-10.
    • (1998) Int J Dev Biol , vol.42 , pp. 1-10
    • Jones, K.T.1
  • 11
    • 0028363794 scopus 로고
    • Dynamics of the calcium signal that triggers mammalian egg activation
    • Swann K, Ozil JP. 1994. Dynamics of the calcium signal that triggers mammalian egg activation. Int Rev Cytol 152: 183-222.
    • (1994) Int Rev Cytol , vol.152 , pp. 183-222
    • Swann, K.1    Ozil, J.P.2
  • 12
    • 46249091922 scopus 로고    scopus 로고
    • Multiple roles of phosphoinositide-specific phospholipase C isozymes
    • Suh PG, Park JI, Manzoli L, Cocco L, et al. 2008. Multiple roles of phosphoinositide-specific phospholipase C isozymes. BMB Rep 41: 415-34.
    • (2008) BMB Rep , vol.41 , pp. 415-434
    • Suh, P.G.1    Park, J.I.2    Manzoli, L.3    Cocco, L.4
  • 13
    • 0026611212 scopus 로고
    • 2+ oscillation by antibody to the inositol 1,4,5-trisphosphate receptor in fertilized hamster eggs
    • 2+ oscillation by antibody to the inositol 1, 4, 5-trisphosphate receptor in fertilized hamster eggs. Science 257: 251-5.
    • (1992) Science , vol.257 , pp. 251-255
    • Miyazaki, S.1    Yuzaki, M.2    Nakada, K.3    Shirakawa, H.4
  • 15
    • 0343952976 scopus 로고    scopus 로고
    • Down-regulation of the inositol 1,4,5-trisphosphate receptor in mouse eggs following fertilization or parthenogenetic activation
    • Jellerette T, He CL, Wu H, Parys JB, et al. 2000. Down-regulation of the inositol 1, 4, 5-trisphosphate receptor in mouse eggs following fertilization or parthenogenetic activation. Dev Biol 223: 238-50.
    • (2000) Dev Biol , vol.223 , pp. 238-250
    • Jellerette, T.1    He, C.L.2    Wu, H.3    Parys, J.B.4
  • 16
    • 0035041688 scopus 로고    scopus 로고
    • Sperm factor induces intracellular free calcium oscillations by stimulating the phosphoinositide pathway
    • Wu H, Smyth J, Luzzi V, Fukami K, et al. 2001. Sperm factor induces intracellular free calcium oscillations by stimulating the phosphoinositide pathway. Biol Reprod 64: 1338-49.
    • (2001) Biol Reprod , vol.64 , pp. 1338-1349
    • Wu, H.1    Smyth, J.2    Luzzi, V.3    Fukami, K.4
  • 17
    • 0028177777 scopus 로고
    • 2+ oscillations and sensitization of Ca2+ release in unfertilized mouse eggs injected with a sperm factor
    • 2+ oscillations and sensitization of Ca2+ release in unfertilized mouse eggs injected with a sperm factor. Cell Calcium 15: 331-9.
    • (1994) Cell Calcium , vol.15 , pp. 331-339
    • Swann, K.1
  • 18
    • 0034284694 scopus 로고    scopus 로고
    • 2+ oscillations in mouse oocytes and eggs can be mimicked by photolysis of caged inositol 1,4,5-trisphosphate: evidence to support a continuous low level production of inositol 1, 4,5-trisphosphate during mammalian fertilization
    • 2+ oscillations in mouse oocytes and eggs can be mimicked by photolysis of caged inositol 1, 4, 5-trisphosphate: evidence to support a continuous low level production of inositol 1, 4, 5-trisphosphate during mammalian fertilization. Dev Biol 225: 1-12.
    • (2000) Dev Biol , vol.225 , pp. 1-12
    • Jones, K.T.1    Nixon, V.L.2
  • 19
    • 0020841230 scopus 로고
    • Sources of calcium in egg activation: a review and hypothesis
    • Jaffe LF. 1983. Sources of calcium in egg activation: a review and hypothesis. Dev Biol 99: 265-76.
    • (1983) Dev Biol , vol.99 , pp. 265-276
    • Jaffe, L.F.1
  • 20
    • 0016357186 scopus 로고
    • Is calcium ionophore a universal activator for unfertilised eggs
    • Steinhardt RA, Epel D, Carroll EJ Jr, Yanagimachi R. 1974. Is calcium ionophore a universal activator for unfertilised eggs? Nature 252: 41-3.
    • (1974) Nature , vol.252 , pp. 41-43
    • Steinhardt, R.A.1    Epel, D.2    Carroll Jr., E.J.3    Yanagimachi, R.4
  • 21
    • 0018084733 scopus 로고
    • Activation of mammalian oocytes by intracellular injection of calcium
    • Fulton BP, Whittingham DG. 1978. Activation of mammalian oocytes by intracellular injection of calcium. Nature 273: 149-51.
    • (1978) Nature , vol.273 , pp. 149-151
    • Fulton, B.P.1    Whittingham, D.G.2
  • 23
    • 0026006483 scopus 로고
    • The path of calcium in cytosolic calcium oscillations: a unifying hypothesis
    • Jaffe LF. 1991. The path of calcium in cytosolic calcium oscillations: a unifying hypothesis. Proc Natl Acad Sci USA 88: 9883-7.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9883-9887
    • Jaffe, L.F.1
  • 24
    • 0032217313 scopus 로고    scopus 로고
    • 2+ and fluorescent markers between the sperm and egg after fusion in the mouse
    • 2+ and fluorescent markers between the sperm and egg after fusion in the mouse. Development 125: 4627-35.
    • (1998) Development , vol.125 , pp. 4627-4635
    • Jones, K.T.1    Soeller, C.2    Cannell, M.B.3
  • 25
    • 0023872015 scopus 로고
    • Inositol 1,4,5-trisphosphate-induced calcium release and guanine nucleotide-binding protein-mediated periodic calcium rises in golden hamster eggs
    • Miyazaki S. 1988. Inositol 1, 4, 5-trisphosphate-induced calcium release and guanine nucleotide-binding protein-mediated periodic calcium rises in golden hamster eggs. J Cell Biol 106: 345-53.
    • (1988) J Cell Biol , vol.106 , pp. 345-353
    • Miyazaki, S.1
  • 26
    • 0028578120 scopus 로고
    • Mechanism of calcium oscillations in fertilized rabbit eggs
    • Fissore RA, Robl JM. 1994. Mechanism of calcium oscillations in fertilized rabbit eggs. Dev Biol 166: 634-42.
    • (1994) Dev Biol , vol.166 , pp. 634-642
    • Fissore, R.A.1    Robl, J.M.2
  • 27
    • 0032084556 scopus 로고    scopus 로고
    • Evidence that Gq family G proteins do not function in mouse egg activation at fertilization
    • Williams CJ, Mehlmann LM, Jaffe LA, Kopf GS, et al. 1998. Evidence that Gq family G proteins do not function in mouse egg activation at fertilization. Dev Biol 198: 116-27.
    • (1998) Dev Biol , vol.198 , pp. 116-127
    • Williams, C.J.1    Mehlmann, L.M.2    Jaffe, L.A.3    Kopf, G.S.4
  • 28
    • 0030881256 scopus 로고    scopus 로고
    • Calcium release at fertilization in starfish eggs is mediated by phospholipase Cgamma
    • Carroll DJ, Ramarao CS, Mehlmann LM, Roche S, et al. 1997. Calcium release at fertilization in starfish eggs is mediated by phospholipase Cgamma. J Cell Biol 138: 1303-11.
    • (1997) J Cell Biol , vol.138 , pp. 1303-1311
    • Carroll, D.J.1    Ramarao, C.S.2    Mehlmann, L.M.3    Roche, S.4
  • 29
    • 0032588627 scopus 로고    scopus 로고
    • Role of phospholipase Cgamma at fertilization and during mitosis in sea urchin eggs and embryos
    • Shearer J, De Nadai C, Emily-Fenouil F, Gache C, et al. 1999. Role of phospholipase Cgamma at fertilization and during mitosis in sea urchin eggs and embryos. Development 126: 2273-84.
    • (1999) Development , vol.126 , pp. 2273-2284
    • Shearer, J.1    De Nadai, C.2    Emily-Fenouil, F.3    Gache, C.4
  • 30
    • 0034663334 scopus 로고    scopus 로고
    • Tyrosine kinase-dependent activation of phospholipase Cgamma is required for calcium transient in Xenopus egg fertilization
    • Sato K, Tokmakov AA, Iwasaki T, Fukami Y. 2000. Tyrosine kinase-dependent activation of phospholipase Cgamma is required for calcium transient in Xenopus egg fertilization. Dev Biol 224: 453-69.
    • (2000) Dev Biol , vol.224 , pp. 453-469
    • Sato, K.1    Tokmakov, A.A.2    Iwasaki, T.3    Fukami, Y.4
  • 32
    • 0033570085 scopus 로고    scopus 로고
    • Calcium release at fertilization of Xenopus eggs requires type I IP3 receptors, but not SH2 domain-mediated activation of PLCgamma or G(q)-mediated activation of PLCbeta
    • Runft LL, Watras J, Jaffe LA. 1999. Calcium release at fertilization of Xenopus eggs requires type I IP3 receptors, but not SH2 domain-mediated activation of PLCgamma or G(q)-mediated activation of PLCbeta. Dev Biol 214: 399-411.
    • (1999) Dev Biol , vol.214 , pp. 399-411
    • Runft, L.L.1    Watras, J.2    Jaffe, L.A.3
  • 34
    • 0030877839 scopus 로고    scopus 로고
    • Intracellular injections of a soluble sperm factor trigger calcium oscillations and meiotic maturation in unfertilized oocytes of a marine worm
    • Stricker SA. 1997. Intracellular injections of a soluble sperm factor trigger calcium oscillations and meiotic maturation in unfertilized oocytes of a marine worm. Dev Biol 186: 185-201.
    • (1997) Dev Biol , vol.186 , pp. 185-201
    • Stricker, S.A.1
  • 35
    • 0026639854 scopus 로고
    • Pregnancies after intracytoplasmic injection of single spermatozoon into an oocyte
    • Palermo G, Joris H, Devroey P, Van Steirteghem AC. 1992. Pregnancies after intracytoplasmic injection of single spermatozoon into an oocyte. Lancet 340: 17-8.
    • (1992) Lancet , vol.340 , pp. 17-18
    • Palermo, G.1    Joris, H.2    Devroey, P.3    Van Steirteghem, A.C.4
  • 36
    • 0028267269 scopus 로고
    • Human oocyte activation after intracytoplasmic sperm injection
    • Tesarik J, Sousa M, Testart J. 1994. Human oocyte activation after intracytoplasmic sperm injection. Hum Reprod 9: 511-8.
    • (1994) Hum Reprod , vol.9 , pp. 511-518
    • Tesarik, J.1    Sousa, M.2    Testart, J.3
  • 37
    • 0031309795 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of intracellular calcium in the mouse egg injected with a spermatozoon
    • Nakano Y, Shirakawa H, Mitsuhashi N, Kuwabara Y, et al. 1997. Spatiotemporal dynamics of intracellular calcium in the mouse egg injected with a spermatozoon. Mol Hum Reprod 3: 1087-93.
    • (1997) Mol Hum Reprod , vol.3 , pp. 1087-1093
    • Nakano, Y.1    Shirakawa, H.2    Mitsuhashi, N.3    Kuwabara, Y.4
  • 38
    • 0027174040 scopus 로고
    • Inositol tri-phosphate in human and ascidian spermatozoa
    • Tosti E, Palumbo A, Dale B. 1993. Inositol tri-phosphate in human and ascidian spermatozoa. Mol Reprod Dev 35: 52-6.
    • (1993) Mol Reprod Dev , vol.35 , pp. 52-56
    • Tosti, E.1    Palumbo, A.2    Dale, B.3
  • 39
    • 0034632895 scopus 로고    scopus 로고
    • NO is necessary and sufficient for egg activation at fertilization
    • Kuo RC, Baxter GT, Thompson SH, Stricker SA, et al. 2000. NO is necessary and sufficient for egg activation at fertilization. Nature 406: 633-6.
    • (2000) Nature , vol.406 , pp. 633-636
    • Kuo, R.C.1    Baxter, G.T.2    Thompson, S.H.3    Stricker, S.A.4
  • 41
    • 0030021886 scopus 로고    scopus 로고
    • 2+ release in eggs at fertilization
    • 2+ release in eggs at fertilization. Rev Reprod 1: 33-9.
    • (1996) Rev Reprod , vol.1 , pp. 33-39
    • Swann, K.1
  • 42
    • 0032533313 scopus 로고    scopus 로고
    • Partial characterization of the calcium-releasing activity of porcine sperm cytosolic extracts
    • Wu H, He CL, Jehn B, Black SJ, et al. 1998. Partial characterization of the calcium-releasing activity of porcine sperm cytosolic extracts. Dev Biol 203: 369-81.
    • (1998) Dev Biol , vol.203 , pp. 369-381
    • Wu, H.1    He, C.L.2    Jehn, B.3    Black, S.J.4
  • 45
    • 0030035074 scopus 로고    scopus 로고
    • Calcium oscillations in mammalian eggs triggered by a soluble sperm protein
    • Parrington J, Swann K, Shevchenko VI, Sesay AK, et al. 1996. Calcium oscillations in mammalian eggs triggered by a soluble sperm protein. Nature 379: 364-8.
    • (1996) Nature , vol.379 , pp. 364-368
    • Parrington, J.1    Swann, K.2    Shevchenko, V.I.3    Sesay, A.K.4
  • 46
    • 0030739524 scopus 로고    scopus 로고
    • Parthenogenetic activation of mouse eggs by microinjection of a truncated c-kit tyrosine kinase present in spermatozoa
    • Sette C, Bevilacqua A, Bianchini A, Mangia F, et al. 1997. Parthenogenetic activation of mouse eggs by microinjection of a truncated c-kit tyrosine kinase present in spermatozoa. Development 124: 2267-74.
    • (1997) Development , vol.124 , pp. 2267-2274
    • Sette, C.1    Bevilacqua, A.2    Bianchini, A.3    Mangia, F.4
  • 47
    • 34249652438 scopus 로고    scopus 로고
    • PAWP, a sperm-specific WW domain-binding protein, promotes meiotic resumption and pronuclear development during fertilization
    • Wu AT, Sutovsky P, Manandhar G, Xu W, et al. 2007. PAWP, a sperm-specific WW domain-binding protein, promotes meiotic resumption and pronuclear development during fertilization. J Biol Chem 282: 12164-75.
    • (2007) J Biol Chem , vol.282 , pp. 12164-12175
    • Wu, A.T.1    Sutovsky, P.2    Manandhar, G.3    Xu, W.4
  • 48
    • 0031965267 scopus 로고    scopus 로고
    • Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity
    • Wolosker H, Kline D, Bian Y, Blackshaw S, et al. 1998. Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity. FASEB J 12: 91-9.
    • (1998) FASEB J , vol.12 , pp. 91-99
    • Wolosker, H.1    Kline, D.2    Bian, Y.3    Blackshaw, S.4
  • 50
    • 0036217935 scopus 로고    scopus 로고
    • Structure, regulation, and function of phospholipase C isozymes
    • Fukami K. 2002. Structure, regulation, and function of phospholipase C isozymes. J Biochem 131: 293-9.
    • (2002) J Biochem , vol.131 , pp. 293-299
    • Fukami, K.1
  • 51
    • 0034653539 scopus 로고    scopus 로고
    • 2+-releasing abilities of sperm extracts compared with tissue extracts and phospholipase C isoforms in sea urchin egg homogenate and mouse eggs
    • 2+-releasing abilities of sperm extracts compared with tissue extracts and phospholipase C isoforms in sea urchin egg homogenate and mouse eggs. Biochem J 346: 743-9.
    • (2000) Biochem J , vol.346 , pp. 743-749
    • Jones, K.T.1    Matsuda, M.2    Parrington, J.3    Katan, M.4
  • 55
    • 33749507370 scopus 로고    scopus 로고
    • Molecular cloning, testicular postnatal expression, and oocyte-activating potential of porcine phospholipase Czeta
    • Yoneda A, Kashima M, Yoshida S, Terada K, et al. 2006. Molecular cloning, testicular postnatal expression, and oocyte-activating potential of porcine phospholipase Czeta. Reproduction 132: 393-401.
    • (2006) Reproduction , vol.132 , pp. 393-401
    • Yoneda, A.1    Kashima, M.2    Yoshida, S.3    Terada, K.4
  • 58
    • 65049089507 scopus 로고    scopus 로고
    • Phospholipase C zeta undergoes dynamic changes in its pattern of localization in sperm during capacitation and the acrosome reaction
    • Young C, Grasa P, Coward K, Davis LC, et al. 2009. Phospholipase C zeta undergoes dynamic changes in its pattern of localization in sperm during capacitation and the acrosome reaction. Fertil Steril 91: 2230-42.
    • (2009) Fertil Steril , vol.91 , pp. 2230-2242
    • Young, C.1    Grasa, P.2    Coward, K.3    Davis, L.C.4
  • 60
    • 70349443589 scopus 로고    scopus 로고
    • Reduced amounts and abnormal forms of phospholipase C zeta (PLCζ) in spermatozoa from infertile men
    • Heytens E, Parrington J, Coward K, Young C, et al. 2009. Reduced amounts and abnormal forms of phospholipase C zeta (PLCζ) in spermatozoa from infertile men. Hum Reprod 24: 2417-28.
    • (2009) Hum Reprod , vol.24 , pp. 2417-2428
    • Heytens, E.1    Parrington, J.2    Coward, K.3    Young, C.4
  • 63
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen LO, Perisic O, Cheung R, Katan M, et al. 1996. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature 380: 595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4
  • 64
    • 20444388673 scopus 로고    scopus 로고
    • The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta
    • Kouchi Z, Shikano T, Nakamura Y, Shirakawa H, et al. 2005. The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta. J Biol Chem 280: 21015-21.
    • (2005) J Biol Chem , vol.280 , pp. 21015-21021
    • Kouchi, Z.1    Shikano, T.2    Nakamura, Y.3    Shirakawa, H.4
  • 66
    • 33748767655 scopus 로고    scopus 로고
    • 2+ oscillation-inducing activities of phospholipase Czeta, a mammalian egg-activating factor
    • 2+ oscillation-inducing activities of phospholipase Czeta, a mammalian egg-activating factor. J Biol Chem 281: 27794-805.
    • (2006) J Biol Chem , vol.281 , pp. 27794-27805
    • Kuroda, K.1    Ito, M.2    Shikano, T.3    Awaji, T.4
  • 67
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon MA, Ferguson KM, O'Brien R, Sigler PB, et al. 1995. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc Natl Acad Sci USA 92: 10472-6.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4
  • 68
    • 0032547744 scopus 로고    scopus 로고
    • Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools
    • Varnai P, Balla T. 1998. Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H]inositol-labeled phosphoinositide pools. J Cell Biol 143: 501-10.
    • (1998) J Cell Biol , vol.143 , pp. 501-510
    • Varnai, P.1    Balla, T.2
  • 69
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler S, Currie RA, Campbell DG, Deak M, et al. 2000. Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem J 351: 19-31.
    • (2000) Biochem J , vol.351 , pp. 19-31
    • Dowler, S.1    Currie, R.A.2    Campbell, D.G.3    Deak, M.4
  • 70
    • 1942422232 scopus 로고    scopus 로고
    • 2+ oscillation-inducing phospholipase C zeta expressed in mouse eggs is accumulated to the pronucleus during egg activation
    • 2+ oscillation-inducing phospholipase C zeta expressed in mouse eggs is accumulated to the pronucleus during egg activation. Dev Biol 268: 245-57.
    • (2004) Dev Biol , vol.268 , pp. 245-257
    • Yoda, A.1    Oda, S.2    Shikano, T.3    Kouchi, Z.4
  • 71
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: structural and functional diversity
    • Nalefski EA, Falke JJ. 1996. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci 5: 2375-90.
    • (1996) Protein Sci , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 72
    • 0032728220 scopus 로고    scopus 로고
    • Mammalian phosphoinositide-specific phospholipase C
    • Williams RL. 1999. Mammalian phosphoinositide-specific phospholipase C. Biochim Biophys Acta 1441: 255-67.
    • (1999) Biochim Biophys Acta , vol.1441 , pp. 255-267
    • Williams, R.L.1
  • 75
    • 0033887478 scopus 로고    scopus 로고
    • Signaling and subcellular targeting by membrane-binding domains
    • Hurley JH, Misra S. 2000. Signaling and subcellular targeting by membrane-binding domains. Annu Rev Biophys Biomol Struct 29: 49-79.
    • (2000) Annu Rev Biophys Biomol Struct , vol.29 , pp. 49-79
    • Hurley, J.H.1    Misra, S.2
  • 76
    • 79961164207 scopus 로고    scopus 로고
    • Phospholipase Czeta binding to PtdIns(4,5)P2 requires the XY-linker region
    • Nomikos M, Elgmati K, Theodoridou M, Calver BL, et al. 2011. Phospholipase Czeta binding to PtdIns(4, 5)P2 requires the XY-linker region. J Cell Sci 124: 2582-90.
    • (2011) J Cell Sci , vol.124 , pp. 2582-2590
    • Nomikos, M.1    Elgmati, K.2    Theodoridou, M.3    Calver, B.L.4
  • 77
    • 34547095244 scopus 로고    scopus 로고
    • PLCzeta, a sperm-specific PLC and its potential role in fertilization
    • Saunders CM, Swann K, Lai FA. 2007. PLCzeta, a sperm-specific PLC and its potential role in fertilization. Biochem Soc Symp 74: 23-36.
    • (2007) Biochem Soc Symp , vol.74 , pp. 23-36
    • Saunders, C.M.1    Swann, K.2    Lai, F.A.3
  • 78
    • 34447521411 scopus 로고    scopus 로고
    • Binding of phosphoinositide-specific phospholipase C-zeta (PLC-zeta) to phospholipid membranes: potential role of an unstructured cluster of basic residues
    • Nomikos M, Mulgrew-Nesbitt A, Pallavi P, Mihalyne G, et al. 2007. Binding of phosphoinositide-specific phospholipase C-zeta (PLC-zeta) to phospholipid membranes: potential role of an unstructured cluster of basic residues. J Biol Chem 282: 16644-53.
    • (2007) J Biol Chem , vol.282 , pp. 16644-16653
    • Nomikos, M.1    Mulgrew-Nesbitt, A.2    Pallavi, P.3    Mihalyne, G.4
  • 79
    • 48349120928 scopus 로고    scopus 로고
    • General and versatile autoinhibition of PLC isozymes
    • Hicks SN, Jezyk MR, Gershburg S, Seifert JP, et al. 2008. General and versatile autoinhibition of PLC isozymes. Mol Cell 31: 383-94.
    • (2008) Mol Cell , vol.31 , pp. 383-394
    • Hicks, S.N.1    Jezyk, M.R.2    Gershburg, S.3    Seifert, J.P.4
  • 80
    • 78149268559 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes
    • Gresset A, Hicks SN, Harden TK, Sondek J. 2010. Mechanism of phosphorylation-induced activation of phospholipase C-gamma isozymes. J Biol Chem 285: 35836-47.
    • (2010) J Biol Chem , vol.285 , pp. 35836-35847
    • Gresset, A.1    Hicks, S.N.2    Harden, T.K.3    Sondek, J.4
  • 81
    • 80052164183 scopus 로고    scopus 로고
    • Novel regulation of PLCζ activity via its XY-linker
    • Nomikos M, Elgmati K, Theodoridou M, Georgilis A, et al. 2011. Novel regulation of PLCζ activity via its XY-linker. Biochem J 438: 427-32.
    • (2011) Biochem J , vol.438 , pp. 427-432
    • Nomikos, M.1    Elgmati, K.2    Theodoridou, M.3    Georgilis, A.4
  • 82
    • 36549037283 scopus 로고    scopus 로고
    • Proteolytic processing of phospholipase Czeta and [Ca2+]i oscillations during mammalian fertilization
    • Kurokawa M, Yoon SY, Alfandari D, Fukami K, et al. 2007. Proteolytic processing of phospholipase Czeta and [Ca2+]i oscillations during mammalian fertilization. Dev Biol 312: 407-18.
    • (2007) Dev Biol , vol.312 , pp. 407-418
    • Kurokawa, M.1    Yoon, S.Y.2    Alfandari, D.3    Fukami, K.4
  • 83
    • 3042818381 scopus 로고    scopus 로고
    • 2+ oscillations in mouse embryos are regulated by nuclear targeting of PLCzeta
    • 2+ oscillations in mouse embryos are regulated by nuclear targeting of PLCzeta. J Cell Sci 117: 2513-21.
    • (2004) J Cell Sci , vol.117 , pp. 2513-2521
    • Larman, M.G.1    Saunders, C.M.2    Carroll, J.3    Lai, F.A.4
  • 85
    • 44349150442 scopus 로고    scopus 로고
    • 2+ oscillation-inducing activity and nuclear translocation ability of PLCZ1, an egg-activating sperm factor candidate, between mouse, rat, human, and medaka fish
    • 2+ oscillation-inducing activity and nuclear translocation ability of PLCZ1, an egg-activating sperm factor candidate, between mouse, rat, human, and medaka fish. Biol Reprod 78: 1081-90.
    • (2008) Biol Reprod , vol.78 , pp. 1081-1090
    • Ito, M.1    Shikano, T.2    Oda, S.3    Horiguchi, T.4
  • 86
    • 56749161915 scopus 로고    scopus 로고
    • Efficiency of assisted oocyte activation as a solution for failed intracytoplasmic sperm injection
    • Heindryckx B, De Gheselle S, Gerris J, Dhont M, et al. 2008. Efficiency of assisted oocyte activation as a solution for failed intracytoplasmic sperm injection. Reprod Biomed Online 17: 662-8.
    • (2008) Reprod Biomed Online , vol.17 , pp. 662-668
    • Heindryckx, B.1    De Gheselle, S.2    Gerris, J.3    Dhont, M.4
  • 87
    • 33845440956 scopus 로고    scopus 로고
    • 2+ oscillatory pattern in fertilized mouse eggs affects gene expression and development to term
    • 2+ oscillatory pattern in fertilized mouse eggs affects gene expression and development to term. Dev Biol 300: 534-44.
    • (2006) Dev Biol , vol.300 , pp. 534-544
    • Ozil, J.P.1    Banrezes, B.2    Toth, S.3    Pan, H.4
  • 88
    • 33644849262 scopus 로고    scopus 로고
    • Expression of a fluorescent recombinant form of sperm protein phospholipase C zeta in mouse epididymal sperm by in vivo gene transfer into the testis
    • Coward K, Kubota H, Hibbitt O, McIlhinney J, et al. 2006. Expression of a fluorescent recombinant form of sperm protein phospholipase C zeta in mouse epididymal sperm by in vivo gene transfer into the testis. Fertil Steril 85: 1281-9.
    • (2006) Fertil Steril , vol.85 , pp. 1281-1289
    • Coward, K.1    Kubota, H.2    Hibbitt, O.3    McIlhinney, J.4


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