메뉴 건너뛰기




Volumn 229, Issue 11, 2014, Pages 1842-1854

Role of Caspase-3 Cleaved IP3R1 on Ca2+ Homeostasis and Developmental Competence of Mouse Oocytes and Eggs

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR;

EID: 84904892288     PISSN: 00219541     EISSN: 10974652     Source Type: Journal    
DOI: 10.1002/jcp.24638     Document Type: Article
Times cited : (8)

References (79)
  • 1
    • 0031794032 scopus 로고    scopus 로고
    • In vitro culture retards spontaneous activation of cell cycle progression and cortical granule exocytosis that normally occur in in vivo unfertilized mouse eggs
    • Abbott AL, Xu Z, Kopf GS, Ducibella T, Schultz RM. 1998. In vitro culture retards spontaneous activation of cell cycle progression and cortical granule exocytosis that normally occur in in vivo unfertilized mouse eggs. Biol Reprod 59:1515-1521.
    • (1998) Biol Reprod , vol.59 , pp. 1515-1521
    • Abbott, A.L.1    Xu, Z.2    Kopf, G.S.3    Ducibella, T.4    Schultz, R.M.5
  • 3
    • 0037518204 scopus 로고    scopus 로고
    • IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor
    • Ando H, Mizutani A, Matsu-ura T, Mikoshiba K. 2003. IRBIT, a novel inositol 1, 4, 5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor. J Biol Chem 278:10602-10612.
    • (2003) J Biol Chem , vol.278 , pp. 10602-10612
    • Ando, H.1    Mizutani, A.2    Matsu-ura, T.3    Mikoshiba, K.4
  • 4
    • 5644261222 scopus 로고    scopus 로고
    • Caspase-3-induced truncation of type 1 inositol trisphosphate receptor accelerates apoptotic cell death and induces inositol trisphosphate-independent calcium release during apoptosis
    • Assefa Z, Bultynck G, Szlufcik K, Nadif Kasri N, Vermassen E, Goris J, Missiaen L, Callewaert G, Parys JB, De Smedt H. 2004. Caspase-3-induced truncation of type 1 inositol trisphosphate receptor accelerates apoptotic cell death and induces inositol trisphosphate-independent calcium release during apoptosis. J Biol Chem 279:43227-43236.
    • (2004) J Biol Chem , vol.279 , pp. 43227-43236
    • Assefa, Z.1    Bultynck, G.2    Szlufcik, K.3    Nadif Kasri, N.4    Vermassen, E.5    Goris, J.6    Missiaen, L.7    Callewaert, G.8    Parys, J.B.9    De Smedt, H.10
  • 5
    • 58149389098 scopus 로고    scopus 로고
    • Actin filaments: Key players in the control of asymmetric divisions in mouse oocytes
    • Azoury J, Verlhac MH, Dumont J. 2009. Actin filaments: Key players in the control of asymmetric divisions in mouse oocytes. Biol Cell 101:69-76.
    • (2009) Biol Cell , vol.101 , pp. 69-76
    • Azoury, J.1    Verlhac, M.H.2    Dumont, J.3
  • 6
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge MJ. 1993. Inositol trisphosphate and calcium signalling. Nature 361:315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 8
    • 0034675855 scopus 로고    scopus 로고
    • Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors
    • Boehning D, Joseph SK. 2000. Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1, 4, 5-trisphosphate receptors. EMBO J 19:5450-5459.
    • (2000) EMBO J , vol.19 , pp. 5450-5459
    • Boehning, D.1    Joseph, S.K.2
  • 9
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • Boehning D, Patterson RL, Sedaghat L, Glebova NO, Kurosaki T, Snyder SH. 2003. Cytochrome c binds to inositol (1, 4, 5) trisphosphate receptors, amplifying calcium-dependent apoptosis. Nat Cell Biol 5:1051-1061.
    • (2003) Nat Cell Biol , vol.5 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 10
    • 0024242097 scopus 로고
    • Protein phosphorylation in meiotically competent and incompetent mouse oocytes
    • Bornslaeger EA, Mattei PM, Schultz RM. 1988. Protein phosphorylation in meiotically competent and incompetent mouse oocytes. Mol Reprod Dev 1:19-25.
    • (1988) Mol Reprod Dev , vol.1 , pp. 19-25
    • Bornslaeger, E.A.1    Mattei, P.M.2    Schultz, R.M.3
  • 12
  • 13
    • 0034661998 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptors are downregulated in mouse oocytes in response to sperm or adenophostin A but not to increases in intracellular Ca(2+) or egg activation
    • Brind S, Swann K, Carroll J. 2000. Inositol 1, 4, 5-trisphosphate receptors are downregulated in mouse oocytes in response to sperm or adenophostin A but not to increases in intracellular Ca(2+) or egg activation. Dev Biol 223:251-265.
    • (2000) Dev Biol , vol.223 , pp. 251-265
    • Brind, S.1    Swann, K.2    Carroll, J.3
  • 14
    • 0024407119 scopus 로고
    • An improved culture medium supports development of random-bred 1-cell mouse embryos in vitro
    • Chatot CL, Ziomek CA, Bavister BD, Lewis JL, Torres I. 1989. An improved culture medium supports development of random-bred 1-cell mouse embryos in vitro. J Reprod Fertil 86:679-688.
    • (1989) J Reprod Fertil , vol.86 , pp. 679-688
    • Chatot, C.L.1    Ziomek, C.A.2    Bavister, B.D.3    Lewis, J.L.4    Torres, I.5
  • 15
    • 0034063069 scopus 로고    scopus 로고
    • A specific inhibitor of p34(cdc2)/cyclin B suppresses fertilization-induced calcium oscillations in mouse eggs
    • Deng MQ, Shen SS. 2000. A specific inhibitor of p34(cdc2)/cyclin B suppresses fertilization-induced calcium oscillations in mouse eggs. Biol Reprod 62:873-878.
    • (2000) Biol Reprod , vol.62 , pp. 873-878
    • Deng, M.Q.1    Shen, S.S.2
  • 16
    • 37849008710 scopus 로고    scopus 로고
    • The complex regulatory function of the ligand-binding domain of the inositol 1,4,5-trisphosphate receptor
    • Devogelaere B, Verbert L, Parys JB, Missiaen L, De Smedt H. 2008. The complex regulatory function of the ligand-binding domain of the inositol 1, 4, 5-trisphosphate receptor. Cell Calcium 43:17-27.
    • (2008) Cell Calcium , vol.43 , pp. 17-27
    • Devogelaere, B.1    Verbert, L.2    Parys, J.B.3    Missiaen, L.4    De Smedt, H.5
  • 17
    • 0033859015 scopus 로고    scopus 로고
    • Selective down-regulation of IP(3)receptor subtypes by caspases and calpain during TNF alpha -induced apoptosis of human T-lymphoma cells
    • Diaz F, Bourguignon LY. 2000. Selective down-regulation of IP(3)receptor subtypes by caspases and calpain during TNF alpha -induced apoptosis of human T-lymphoma cells. Cell Calcium 27:315-328.
    • (2000) Cell Calcium , vol.27 , pp. 315-328
    • Diaz, F.1    Bourguignon, L.Y.2
  • 18
    • 73649091477 scopus 로고    scopus 로고
    • Mammalian oocyte development: Checkpoints for competence
    • Fair T. 2010. Mammalian oocyte development: Checkpoints for competence. Reprod Fertil Dev 22:13-20.
    • (2010) Reprod Fertil Dev , vol.22 , pp. 13-20
    • Fair, T.1
  • 19
    • 0030880187 scopus 로고    scopus 로고
    • A member of the Ste20/PAK family of protein kinases is involved in both arrest of Xenopus oocytes at G2/prophase of the first meiotic cell cycle and in prevention of apoptosis
    • Faure S, Vigneron S, Doree M, Morin N. 1997. A member of the Ste20/PAK family of protein kinases is involved in both arrest of Xenopus oocytes at G2/prophase of the first meiotic cell cycle and in prevention of apoptosis. EMBO J 16:5550-5561.
    • (1997) EMBO J , vol.16 , pp. 5550-5561
    • Faure, S.1    Vigneron, S.2    Doree, M.3    Morin, N.4
  • 20
    • 0032896381 scopus 로고    scopus 로고
    • Differential distribution of inositol trisphosphate receptor isoforms in mouse oocytes
    • Fissore RA, Longo FJ, Anderson E, Parys JB, Ducibella T. 1999. Differential distribution of inositol trisphosphate receptor isoforms in mouse oocytes. Biol Reprod 60:49-57.
    • (1999) Biol Reprod , vol.60 , pp. 49-57
    • Fissore, R.A.1    Longo, F.J.2    Anderson, E.3    Parys, J.B.4    Ducibella, T.5
  • 21
    • 0036948437 scopus 로고    scopus 로고
    • Mechanisms underlying oocyte activation and postovulatory ageing
    • Fissore RA, Kurokawa M, Knott J, Zhang M, Smyth J. 2002. Mechanisms underlying oocyte activation and postovulatory ageing. Reproduction 124:745-754.
    • (2002) Reproduction , vol.124 , pp. 745-754
    • Fissore, R.A.1    Kurokawa, M.2    Knott, J.3    Zhang, M.4    Smyth, J.5
  • 22
    • 0027511771 scopus 로고
    • Development of inositol trisphosphate-induced calcium release mechanism during maturation of hamster oocytes
    • Fujiwara T, Nakada K, Shirakawa H, Miyazaki S. 1993. Development of inositol trisphosphate-induced calcium release mechanism during maturation of hamster oocytes. Dev Biol 156:69-79.
    • (1993) Dev Biol , vol.156 , pp. 69-79
    • Fujiwara, T.1    Nakada, K.2    Shirakawa, H.3    Miyazaki, S.4
  • 23
    • 0032870931 scopus 로고    scopus 로고
    • Subunit oligomerization, and topology of the inositol 1,4,5-trisphosphate receptor
    • Galvan DL, Borrego-Diaz E, Perez PJ, Mignery GA. 1999. Subunit oligomerization, and topology of the inositol 1, 4, 5-trisphosphate receptor. J Biol Chem 274:29483-29492.
    • (1999) J Biol Chem , vol.274 , pp. 29483-29492
    • Galvan, D.L.1    Borrego-Diaz, E.2    Perez, P.J.3    Mignery, G.A.4
  • 25
    • 0034090870 scopus 로고    scopus 로고
    • Injection of sperm cytosolic factor into mouse metaphase II oocytes induces different developmental fates according to the frequency of [Ca(2+)](i) oscillations and oocyte age
    • Gordo AC, Wu H, He CL, Fissore RA. 2000. Injection of sperm cytosolic factor into mouse metaphase II oocytes induces different developmental fates according to the frequency of [Ca(2+)](i) oscillations and oocyte age. Biol Reprod 62:1370-1379.
    • (2000) Biol Reprod , vol.62 , pp. 1370-1379
    • Gordo, A.C.1    Wu, H.2    He, C.L.3    Fissore, R.A.4
  • 26
  • 27
    • 0033793115 scopus 로고    scopus 로고
    • Degradation of the type I inositol 1,4,5-trisphosphate receptor by caspase-3 in SH-SY5Y neuroblastoma cells undergoing apoptosis
    • Haug LS, Walaas SI, Ostvold AC. 2000. Degradation of the type I inositol 1, 4, 5-trisphosphate receptor by caspase-3 in SH-SY5Y neuroblastoma cells undergoing apoptosis. J Neurochem 75:1852-1861.
    • (2000) J Neurochem , vol.75 , pp. 1852-1861
    • Haug, L.S.1    Walaas, S.I.2    Ostvold, A.C.3
  • 28
    • 0033607673 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor type 1 is a substrate for caspase-3 and is cleaved during apoptosis in a caspase-3-dependent manner
    • Hirota J, Furuichi T, Mikoshiba K. 1999. Inositol 1, 4, 5-trisphosphate receptor type 1 is a substrate for caspase-3 and is cleaved during apoptosis in a caspase-3-dependent manner. J Biol Chem 274:34433-34437.
    • (1999) J Biol Chem , vol.274 , pp. 34433-34437
    • Hirota, J.1    Furuichi, T.2    Mikoshiba, K.3
  • 30
    • 0030973158 scopus 로고    scopus 로고
    • T cells deficient in inositol 1,4,5-trisphosphate receptor are resistant to apoptosis
    • Jayaraman T, Marks AR. 1997. T cells deficient in inositol 1, 4, 5-trisphosphate receptor are resistant to apoptosis. Mol Cell Biol 17:3005-3012.
    • (1997) Mol Cell Biol , vol.17 , pp. 3005-3012
    • Jayaraman, T.1    Marks, A.R.2
  • 31
    • 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, Fissore RA. 2000. Down-regulation of the inositol 1, 4, 5-trisphosphate receptor in mouse eggs following fertilization or parthenogenetic activation. Dev Biol 223:238-250.
    • (2000) Dev Biol , vol.223 , pp. 238-250
    • Jellerette, T.1    He, C.L.2    Wu, H.3    Parys, J.B.4    Fissore, R.A.5
  • 35
    • 36348987603 scopus 로고    scopus 로고
    • Role of inositol 1,4,5-trisphosphate receptors in apoptosis in DT40 lymphocytes
    • Khan MT, Bhanumathy CD, Schug ZT, Joseph SK. 2007. Role of inositol 1, 4, 5-trisphosphate receptors in apoptosis in DT40 lymphocytes. J Biol Chem 282:32983-32990.
    • (2007) J Biol Chem , vol.282 , pp. 32983-32990
    • Khan, M.T.1    Bhanumathy, C.D.2    Schug, Z.T.3    Joseph, S.K.4
  • 36
    • 0033642385 scopus 로고    scopus 로고
    • Attributes and dynamics of the endoplasmic reticulum in mammalian eggs
    • Kline D. 2000. Attributes and dynamics of the endoplasmic reticulum in mammalian eggs. Curr Top Dev Biol 50:125-154.
    • (2000) Curr Top Dev Biol , vol.50 , pp. 125-154
    • Kline, D.1
  • 37
    • 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 149:80-89.
    • (1992) Dev Biol , vol.149 , pp. 80-89
    • Kline, D.1    Kline, J.T.2
  • 38
    • 0033571596 scopus 로고    scopus 로고
    • The cortical endoplasmic reticulum (ER) of the mouse egg: Localization of ER clusters in relation to the generation of repetitive calcium waves
    • Kline D, Mehlmann L, Fox C, Terasaki M. 1999. The cortical endoplasmic reticulum (ER) of the mouse egg: Localization of ER clusters in relation to the generation of repetitive calcium waves. Dev Biol 215:431-442.
    • (1999) Dev Biol , vol.215 , pp. 431-442
    • Kline, D.1    Mehlmann, L.2    Fox, C.3    Terasaki, M.4
  • 40
    • 0141839695 scopus 로고    scopus 로고
    • ICSI-generated mouse zygotes exhibit altered calcium oscillations, inositol 1,4,5-trisphosphate receptor-1 down-regulation, and embryo development
    • Kurokawa M, Fissore RA. 2003. ICSI-generated mouse zygotes exhibit altered calcium oscillations, inositol 1, 4, 5-trisphosphate receptor-1 down-regulation, and embryo development. Mol Hum Reprod 9:523-533.
    • (2003) Mol Hum Reprod , vol.9 , pp. 523-533
    • Kurokawa, M.1    Fissore, R.A.2
  • 41
    • 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
  • 43
    • 0031673789 scopus 로고    scopus 로고
    • Sperm-triggered calcium oscillations during meiosis in ascidian oocytes first pause, restart, then stop: Correlations with cell cycle kinase activity
    • McDougall A, Levasseur M. 1998. Sperm-triggered calcium oscillations during meiosis in ascidian oocytes first pause, restart, then stop: Correlations with cell cycle kinase activity. Development 125:4451-4459.
    • (1998) Development , vol.125 , pp. 4451-4459
    • McDougall, A.1    Levasseur, M.2
  • 44
    • 27544472085 scopus 로고    scopus 로고
    • Stops and starts in mammalian oocytes: Recent advances in understanding the regulation of meiotic arrest and oocyte maturation
    • Mehlmann LM. 2005. Stops and starts in mammalian oocytes: Recent advances in understanding the regulation of meiotic arrest and oocyte maturation. Reproduction 130:791-799.
    • (2005) Reproduction , vol.130 , pp. 791-799
    • Mehlmann, L.M.1
  • 45
    • 0029113964 scopus 로고
    • Reorganization of the endoplasmic reticulum during meiotic maturation of the mouse oocyte
    • Mehlmann LM, Terasaki M, Jaffe LA, Kline D. 1995. Reorganization of the endoplasmic reticulum during meiotic maturation of the mouse oocyte. Dev Biol 170:607-615.
    • (1995) Dev Biol , vol.170 , pp. 607-615
    • Mehlmann, L.M.1    Terasaki, M.2    Jaffe, L.A.3    Kline, D.4
  • 46
    • 0030589721 scopus 로고    scopus 로고
    • Redistribution and increase in cortical inositol 1,4,5-trisphosphate receptors after meiotic maturation of the mouse oocyte
    • Mehlmann LM, Mikoshiba K, Kline D. 1996. Redistribution and increase in cortical inositol 1, 4, 5-trisphosphate receptors after meiotic maturation of the mouse oocyte. Dev Biol 180:489-498.
    • (1996) Dev Biol , vol.180 , pp. 489-498
    • Mehlmann, L.M.1    Mikoshiba, K.2    Kline, D.3
  • 48
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai T, Ibata K, Park ES, Kubota M, Mikoshiba K, Miyawaki A. 2002. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat Biotechnol 20:87-90.
    • (2002) Nat Biotechnol , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 49
    • 9144262298 scopus 로고    scopus 로고
    • The regulatory domain of the inositol 1,4,5-trisphosphate receptor is necessary to keep the channel domain closed: Possible physiological significance of specific cleavage by caspase 3
    • Nakayama T, Hattori M, Uchida K, Nakamura T, Tateishi Y, Bannai H, Iwai M, Michikawa T, Inoue T, Mikoshiba K. 2004. The regulatory domain of the inositol 1, 4, 5-trisphosphate receptor is necessary to keep the channel domain closed: Possible physiological significance of specific cleavage by caspase 3. Biochem J 377:299-307.
    • (2004) Biochem J , vol.377 , pp. 299-307
    • Nakayama, T.1    Hattori, M.2    Uchida, K.3    Nakamura, T.4    Tateishi, Y.5    Bannai, H.6    Iwai, M.7    Michikawa, T.8    Inoue, T.9    Mikoshiba, K.10
  • 50
    • 0032533943 scopus 로고    scopus 로고
    • Expression of inositol 1,4,5-trisphosphate receptors in mouse oocytes and early embryos: The type I isoform is upregulated in oocytes and downregulated after fertilization
    • Parrington J, Brind S, De Smedt H, Gangeswaran R, Lai FA, Wojcikiewicz R, Carroll J. 1998. Expression of inositol 1, 4, 5-trisphosphate receptors in mouse oocytes and early embryos: The type I isoform is upregulated in oocytes and downregulated after fertilization. Dev Biol 203:451-461.
    • (1998) Dev Biol , vol.203 , pp. 451-461
    • Parrington, J.1    Brind, S.2    De Smedt, H.3    Gangeswaran, R.4    Lai, F.A.5    Wojcikiewicz, R.6    Carroll, J.7
  • 51
    • 0029011313 scopus 로고
    • Rat basophilic leukemia cells as model system for inositol 1,4,5-trisphosphate receptor IV, a receptor of the type II family: Functional comparison and immunological detection
    • Parys JB, de-Smedt H, Missiaen L, Bootman MD, Sienaert I, Casteels R. 1995. Rat basophilic leukemia cells as model system for inositol 1, 4, 5-trisphosphate receptor IV, a receptor of the type II family: Functional comparison and immunological detection. Cell Calcium 17:239-249.
    • (1995) Cell Calcium , vol.17 , pp. 239-249
    • Parys, J.B.1    de-Smedt, H.2    Missiaen, L.3    Bootman, M.D.4    Sienaert, I.5    Casteels, R.6
  • 52
    • 0032935519 scopus 로고    scopus 로고
    • Fragmentation and death (a.k.a. apoptosis) of ovulated oocytes
    • Perez GI, Tao XJ, Tilly JL. 1999. Fragmentation and death (a.k.a. apoptosis) of ovulated oocytes. Mol Hum Reprod 5:414-420.
    • (1999) Mol Hum Reprod , vol.5 , pp. 414-420
    • Perez, G.I.1    Tao, X.J.2    Tilly, J.L.3
  • 53
    • 0036079989 scopus 로고    scopus 로고
    • Inhibition of MEK or cdc2 kinase parthenogenetically activates mouse eggs and yields the same phenotypes as Mos(-/-) parthenogenotes
    • Phillips KP, Petrunewich MA, Collins JL, Booth RA, Liu XJ, Baltz JM. 2002. Inhibition of MEK or cdc2 kinase parthenogenetically activates mouse eggs and yields the same phenotypes as Mos(-/-) parthenogenotes. Dev Biol 247:210-223.
    • (2002) Dev Biol , vol.247 , pp. 210-223
    • Phillips, K.P.1    Petrunewich, M.A.2    Collins, J.L.3    Booth, R.A.4    Liu, X.J.5    Baltz, J.M.6
  • 54
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M, Rogers SW. 1996. PEST sequences and regulation by proteolysis. Trends Biochem Sci 21:267-271.
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 55
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers S, Wells R, Rechsteiner M. 1986. Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis. Science 234:364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 57
    • 0035931854 scopus 로고    scopus 로고
    • P53 activation in response to microtubule disruption is mediated by integrin-Erk signaling
    • Sablina AA, Chumakov PM, Levine AJ, Kopnin BP. 2001. P53 activation in response to microtubule disruption is mediated by integrin-Erk signaling. Oncogene 20:899-909.
    • (2001) Oncogene , vol.20 , pp. 899-909
    • Sablina, A.A.1    Chumakov, P.M.2    Levine, A.J.3    Kopnin, B.P.4
  • 58
    • 0031932444 scopus 로고    scopus 로고
    • Adenophostin, a potent agonist of the inositol 1,4,5-trisphosphate receptor, is useful for fertilization of mouse oocytes injected with round spermatids leading to normal offspring
    • Sato Y, Miyazaki S, Shikano T, Mitsuhashi N, Takeuchi H, Mikoshiba K, Kuwabara Y. 1998. Adenophostin, a potent agonist of the inositol 1, 4, 5-trisphosphate receptor, is useful for fertilization of mouse oocytes injected with round spermatids leading to normal offspring. Biol Reprod 58:867-873.
    • (1998) Biol Reprod , vol.58 , pp. 867-873
    • Sato, Y.1    Miyazaki, S.2    Shikano, T.3    Mitsuhashi, N.4    Takeuchi, H.5    Mikoshiba, K.6    Kuwabara, Y.7
  • 60
    • 0030911979 scopus 로고    scopus 로고
    • Intracellular targeting and homotetramer formation of a truncated inositol 1,4,5-trisphosphate receptor-green fluorescent protein chimera in Xenopus laevis oocytes: Evidence for the involvement of the transmembrane spanning domain in endoplasmic reticulum targeting and homotetramer complex formation
    • Sayers LG, Miyawaki A, Muto A, Takeshita H, Yamamoto A, Michikawa T, Furuichi T, Mikoshiba K. 1997. Intracellular targeting and homotetramer formation of a truncated inositol 1, 4, 5-trisphosphate receptor-green fluorescent protein chimera in Xenopus laevis oocytes: Evidence for the involvement of the transmembrane spanning domain in endoplasmic reticulum targeting and homotetramer complex formation. Biochem J 323:273-280.
    • (1997) Biochem J , vol.323 , pp. 273-280
    • Sayers, L.G.1    Miyawaki, A.2    Muto, A.3    Takeshita, H.4    Yamamoto, A.5    Michikawa, T.6    Furuichi, T.7    Mikoshiba, K.8
  • 62
    • 0020771377 scopus 로고
    • Regulation of mouse oocyte meiotic maturation: Implication of a decrease in oocyte cAMP and protein dephosphorylation in commitment to resume meiosis
    • Schultz RM, Montgomery RR, Belanoff JR. 1983. Regulation of mouse oocyte meiotic maturation: Implication of a decrease in oocyte cAMP and protein dephosphorylation in commitment to resume meiosis. Dev Biol 97:264-273.
    • (1983) Dev Biol , vol.97 , pp. 264-273
    • Schultz, R.M.1    Montgomery, R.R.2    Belanoff, J.R.3
  • 64
    • 0020019986 scopus 로고
    • In vitro maturation of mammalian oocytes. II. Structural and biochemical transformations and the capacity for fertilization
    • Skoblina MN. 1982. In vitro maturation of mammalian oocytes. II. Structural and biochemical transformations and the capacity for fertilization. Ontogenez 13:18-27.
    • (1982) Ontogenez , vol.13 , pp. 18-27
    • Skoblina, M.N.1
  • 65
    • 0023163246 scopus 로고
    • Interactions of aged gametes: In vitro fertilization using in vitro-aged sperm and in vivo-aged ova in the mouse
    • Smith AL, Lodge JR. 1987. Interactions of aged gametes: In vitro fertilization using in vitro-aged sperm and in vivo-aged ova in the mouse. Gamete Res 16:47-56.
    • (1987) Gamete Res , vol.16 , pp. 47-56
    • Smith, A.L.1    Lodge, J.R.2
  • 66
    • 0026802940 scopus 로고
    • Different triggers for calcium oscillations in mouse eggs involve a ryanodine-sensitive calcium store
    • Swann K. 1992. Different triggers for calcium oscillations in mouse eggs involve a ryanodine-sensitive calcium store. Biochem J 287:79-84.
    • (1992) Biochem J , vol.287 , pp. 79-84
    • Swann, K.1
  • 67
    • 0033974683 scopus 로고    scopus 로고
    • Effects of aging on inositol 1,4,5-triphosphate-induced Ca(2+) release in unfertilized mouse oocytes
    • Takahashi T, Saito H, Hiroi M, Doi K, Takahashi E. 2000. Effects of aging on inositol 1, 4, 5-triphosphate-induced Ca(2+) release in unfertilized mouse oocytes. Mol Reprod Dev 55:299-306.
    • (2000) Mol Reprod Dev , vol.55 , pp. 299-306
    • Takahashi, T.1    Saito, H.2    Hiroi, M.3    Doi, K.4    Takahashi, E.5
  • 68
    • 62149122199 scopus 로고    scopus 로고
    • Poor embryo development in mouse oocytes aged in vitro is associated with impaired calcium homeostasis
    • Takahashi T, Igarashi H, Kawagoe J, Amita M, Hara S, Kurachi H. 2009. Poor embryo development in mouse oocytes aged in vitro is associated with impaired calcium homeostasis. Biol Reprod 80:493-502.
    • (2009) Biol Reprod , vol.80 , pp. 493-502
    • Takahashi, T.1    Igarashi, H.2    Kawagoe, J.3    Amita, M.4    Hara, S.5    Kurachi, H.6
  • 69
    • 0028348910 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor causes formation of ER cisternal stacks in transfected fibroblasts and in cerebellar Purkinje cells
    • Takei K, Mignery GA, Mugnaini E, Sudhof TC, De Camilli P. 1994. Inositol 1, 4, 5-trisphosphate receptor causes formation of ER cisternal stacks in transfected fibroblasts and in cerebellar Purkinje cells. Neuron 12:327-342.
    • (1994) Neuron , vol.12 , pp. 327-342
    • Takei, K.1    Mignery, G.A.2    Mugnaini, E.3    Sudhof, T.C.4    De Camilli, P.5
  • 70
    • 0344132619 scopus 로고    scopus 로고
    • Long-term effects of postovulatory aging of mouse oocytes on offspring: A two-generational study
    • Tarin JJ, Perez-Albala S, Aguilar A, Minarro J, Hermenegildo C, Cano A. 1999. Long-term effects of postovulatory aging of mouse oocytes on offspring: A two-generational study. Biol Reprod 61:1347-1355.
    • (1999) Biol Reprod , vol.61 , pp. 1347-1355
    • Tarin, J.J.1    Perez-Albala, S.2    Aguilar, A.3    Minarro, J.4    Hermenegildo, C.5    Cano, A.6
  • 71
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • Thastrup O, Cullen PJ, Drobak BK, Hanley MR, Dawson AP. 1990. Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase. Proc Natl Acad Sci USA 87:2466-2470.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 72
    • 0020024768 scopus 로고
    • Effect of delayed insemination on in-vitro fertilization, culture and transfer of human embryos
    • Trounson AO, Mohr LR, Wood C, Leeton JF. 1982. Effect of delayed insemination on in-vitro fertilization, culture and transfer of human embryos. J Reprod Fertil 64:285-294.
    • (1982) J Reprod Fertil , vol.64 , pp. 285-294
    • Trounson, A.O.1    Mohr, L.R.2    Wood, C.3    Leeton, J.F.4
  • 75
    • 33646833093 scopus 로고    scopus 로고
    • Post-ovulatory ageing of the human oocyte and embryo failure
    • Wilcox AJ, Weinberg CR, Baird DD. 1998. Post-ovulatory ageing of the human oocyte and embryo failure. Hum Reprod 13:394-397.
    • (1998) Hum Reprod , vol.13 , pp. 394-397
    • Wilcox, A.J.1    Weinberg, C.R.2    Baird, D.D.3
  • 76
    • 0030922886 scopus 로고    scopus 로고
    • Spontaneous activation of ovulated mouse eggs: Time-dependent effects on M-phase exit, cortical granule exocytosis, maternal messenger ribonucleic acid recruitment, and inositol 1,4,5-trisphosphate sensitivity
    • Xu Z, Abbott A, Kopf GS, Schultz RM, Ducibella T. 1997. Spontaneous activation of ovulated mouse eggs: Time-dependent effects on M-phase exit, cortical granule exocytosis, maternal messenger ribonucleic acid recruitment, and inositol 1, 4, 5-trisphosphate sensitivity. Biol Reprod 57:743-750.
    • (1997) Biol Reprod , vol.57 , pp. 743-750
    • Xu, Z.1    Abbott, A.2    Kopf, G.S.3    Schultz, R.M.4    Ducibella, T.5
  • 78
    • 0023894787 scopus 로고
    • Second meiotic nondisjunction is not increased in postovulatory aged murine oocytes fertilized in vitro
    • Zackowski JL, Leon PAM-D. 1988. Second meiotic nondisjunction is not increased in postovulatory aged murine oocytes fertilized in vitro. In Vitro Cell Dev Biol 24:133-137.
    • (1988) In Vitro Cell Dev Biol , vol.24 , pp. 133-137
    • Zackowski, J.L.1    Leon, P.-D.2
  • 79
    • 80052745621 scopus 로고    scopus 로고
    • Caffeine alleviates the deterioration of Ca2+ release mechanisms and fragmentation of in vitro-aged mouse eggs
    • Zhang N, Wakai T, Fissore RA. 2011. Caffeine alleviates the deterioration of Ca2+ release mechanisms and fragmentation of in vitro-aged mouse eggs. Mol Reprod Dev 78:684-701.
    • (2011) Mol Reprod Dev , vol.78 , pp. 684-701
    • Zhang, N.1    Wakai, T.2    Fissore, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.