메뉴 건너뛰기




Volumn 39, Issue 1, 2006, Pages 65-73

Calcium release from ryanodine receptors in the nucleoplasmic reticulum

Author keywords

C2C12; Channel; Nuclear signaling; Nucleoplasmic reticulum; Ryanodine receptor

Indexed keywords

CALCIUM; CELL PROTEIN; DANTROLENE; RYANODINE RECEPTOR;

EID: 29444441912     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2005.09.010     Document Type: Article
Times cited : (83)

References (40)
  • 2
    • 0026009773 scopus 로고
    • Ryanodine receptor protein is expressed during differentiation in the muscle cell lines BC3H1 and C2C12
    • J.A. Airey M.D. Baring J.L. Sutko Ryanodine receptor protein is expressed during differentiation in the muscle cell lines BC3H1 and C2C12 Dev. Biol. 148 1991 365-374
    • (1991) Dev. Biol. , vol.148 , pp. 365-374
    • Airey, J.A.1    Baring, M.D.2    Sutko, J.L.3
  • 4
    • 0014032729 scopus 로고
    • Nuclei from rat liver: Isolation method that combines purity with high yield
    • G. Blobel V.R. Potter Nuclei from rat liver: Isolation method that combines purity with high yield Science 154 1966 1662-1665
    • (1966) Science , vol.154 , pp. 1662-1665
    • Blobel, G.1    Potter, V.R.2
  • 5
    • 0032906554 scopus 로고    scopus 로고
    • Photolysis of caged calcium in femtoliter volumes using two-photon excitation
    • E.B. Brown J.B. Shear S.R. Adams R.Y. Tsien W.W. Webb Photolysis of caged calcium in femtoliter volumes using two-photon excitation Biophys. J. 76 1999 489-499
    • (1999) Biophys. J. , vol.76 , pp. 489-499
    • Brown, E.B.1    Shear, J.B.2    Adams, S.R.3    Tsien, R.Y.4    Webb, W.W.5
  • 6
    • 0028290497 scopus 로고
    • Confocal microscopy to analyze cytosolic and nuclear calcium in cultured vascular cells
    • M. Burnier G. Centeno E. Burki H.R. Brunner Confocal microscopy to analyze cytosolic and nuclear calcium in cultured vascular cells Am. J. Physiol. 266 1994 C1118-C1127
    • (1994) Am. J. Physiol. , vol.266
    • Burnier, M.1    Centeno, G.2    Burki, E.3    Brunner, H.R.4
  • 8
    • 0033956950 scopus 로고    scopus 로고
    • An estimate of rapid cytoplasmic calcium buffering in a single smooth muscle cell
    • B. Daub V. Ganitkevich An estimate of rapid cytoplasmic calcium buffering in a single smooth muscle cell Cell Calcium 27 2000 3-13
    • (2000) Cell Calcium , vol.27 , pp. 3-13
    • Daub, B.1    Ganitkevich, V.2
  • 9
    • 0032510478 scopus 로고    scopus 로고
    • Translocation of calmodulin to the nucleus supports CREB phosphorylation in hippocampal neurons
    • K. Deisseroth E.K. Heist R.W. Tsien Translocation of calmodulin to the nucleus supports CREB phosphorylation in hippocampal neurons Nature 392 1998 198-202
    • (1998) Nature , vol.392 , pp. 198-202
    • Deisseroth, K.1    Heist, E.K.2    Tsien, R.W.3
  • 11
    • 0026040577 scopus 로고
    • The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus
    • N. Divecha H. Banfic R.F. Irvine The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus EMBO J. 10 1991 3207-3214
    • (1991) EMBO J. , vol.10 , pp. 3207-3214
    • Divecha, N.1    Banfic, H.2    Irvine, R.F.3
  • 12
    • 0028883178 scopus 로고
    • Phospholipid signaling
    • N. Divecha R.F. Irvine Phospholipid signaling Cell 80 1995 269-278
    • (1995) Cell , vol.80 , pp. 269-278
    • Divecha, N.1    Irvine, R.F.2
  • 14
    • 0031051629 scopus 로고    scopus 로고
    • Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope
    • M. Fricker M. Hollinshead N. White D. Vaux Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope J. Cell Biol. 136 1997 531-544
    • (1997) J. Cell Biol. , vol.136 , pp. 531-544
    • Fricker, M.1    Hollinshead, M.2    White, N.3    Vaux, D.4
  • 17
    • 0028925223 scopus 로고
    • The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues
    • G. Giannini A. Conti S. Mammarella M. Scrobogna V. Sorrentino The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues J. Cell Biol. 128 1995 893-904
    • (1995) J. Cell Biol. , vol.128 , pp. 893-904
    • Giannini, G.1    Conti, A.2    Mammarella, S.3    Scrobogna, M.4    Sorrentino, V.5
  • 18
    • 0031019855 scopus 로고    scopus 로고
    • Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression
    • G.E. Hardingham S. Chawla C.M. Johnson H. Bading Distinct functions of nuclear and cytoplasmic calcium in the control of gene expression Nature 385 1997 260-265
    • (1997) Nature , vol.385 , pp. 260-265
    • Hardingham, G.E.1    Chawla, S.2    Johnson, C.M.3    Bading, H.4
  • 20
    • 0030067950 scopus 로고    scopus 로고
    • Inositol 1,4,5-trisphosphate receptor is located to the inner nuclear membrane vindicating regulation of nuclear calcium signaling by inositol 1,4,5-trisphosphate. Discrete distribution of inositol phosphate receptors to inner and outer nuclear membranes
    • J.P. Humbert N. Matter J.C. Artault P. Koppler A.N. Malviya Inositol 1,4,5-trisphosphate receptor is located to the inner nuclear membrane vindicating regulation of nuclear calcium signaling by inositol 1,4,5-trisphosphate. Discrete distribution of inositol phosphate receptors to inner and outer nuclear membranes J. Biol. Chem. 271 1996 478-485
    • (1996) J. Biol. Chem. , vol.271 , pp. 478-485
    • Humbert, J.P.1    Matter, N.2    Artault, J.C.3    Koppler, P.4    Malviya, A.N.5
  • 22
    • 0027422372 scopus 로고
    • Evidence for stereospecific inositol 1,3,4,5-[3H]tetrakisphosphate binding sites on rat liver nuclei. Delineating inositol 1,3,4,5-tetrakisphosphate interaction in nuclear calcium signaling process
    • P. Koppler N. Matter A.N. Malviya Evidence for stereospecific inositol 1,3,4,5-[3H]tetrakisphosphate binding sites on rat liver nuclei. Delineating inositol 1,3,4,5-tetrakisphosphate interaction in nuclear calcium signaling process J. Biol. Chem. 268 1993 26248-26252
    • (1993) J. Biol. Chem. , vol.268 , pp. 26248-26252
    • Koppler, P.1    Matter, N.2    Malviya, A.N.3
  • 23
    • 0026665955 scopus 로고
    • The calcium pump of the liver nuclear membrane is identical to that of endoplasmic reticulum
    • L. Lanini O. Bachs E. Carafoli The calcium pump of the liver nuclear membrane is identical to that of endoplasmic reticulum J. Biol. Chem. 267 1992 11548-11552
    • (1992) J. Biol. Chem. , vol.267 , pp. 11548-11552
    • Lanini, L.1    Bachs, O.2    Carafoli, E.3
  • 24
    • 0036007499 scopus 로고    scopus 로고
    • 2+ waves require sequential activation of inositol 1,4,5 trisphosphate receptors, then ryanodine receptors in pancreatic acinar cells
    • 2+ waves require sequential activation of inositol 1,4,5 trisphosphate receptors, then ryanodine receptors in pancreatic acinar cells Gastroenterology 122 2002 415-427
    • (2002) Gastroenterology , vol.122 , pp. 415-427
    • Leite, M.1    Franco, A.2    Burgstahler, A.3    Nathanson, M.4
  • 27
    • 0030702896 scopus 로고    scopus 로고
    • Nuclear calcium signalling by individual cytoplasmic calcium puffs
    • P. Lipp D. Thomas M. Berridge M. Bootman Nuclear calcium signalling by individual cytoplasmic calcium puffs EMBO J. 16 1997 7166-7173
    • (1997) EMBO J. , vol.16 , pp. 7166-7173
    • Lipp, P.1    Thomas, D.2    Berridge, M.3    Bootman, M.4
  • 29
    • 0036812239 scopus 로고    scopus 로고
    • Roles of two ryanodine receptor isoforms coexisting in skeletal muscle
    • T. Murayama Y. Ogawa Roles of two ryanodine receptor isoforms coexisting in skeletal muscle Trends Cardiovasc. Med. 12 2002 305-311
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 305-311
    • Murayama, T.1    Ogawa, Y.2
  • 30
    • 0028170056 scopus 로고
    • 2+: Physiological regulation and role in apoptosis
    • 2+: Physiological regulation and role in apoptosis Mol. Cell Biochem. 135 1994 89-98
    • (1994) Mol. Cell Biochem. , vol.135 , pp. 89-98
    • Nicotera, P.1    Rossi, A.D.2
  • 31
    • 0028107008 scopus 로고
    • Calcium permeability of the neuronal nuclear envelope: Evaluation using confocal volumes and intracellular perfusion
    • D.M. O'Malley Calcium permeability of the neuronal nuclear envelope: Evaluation using confocal volumes and intracellular perfusion J. Neurosci. 14 1994 5741-5758
    • (1994) J. Neurosci. , vol.14 , pp. 5741-5758
    • O'Malley, D.M.1
  • 33
    • 0030860031 scopus 로고    scopus 로고
    • Effects of 1-methyladenine on nuclear Ca2+ transients and meiosis resumption in starfish oocytes are mimicked by the nuclear injection of inositol 1,4,5-trisphosphate and cADP-ribose
    • L. Santella K. Kyozuka Effects of 1-methyladenine on nuclear Ca2+ transients and meiosis resumption in starfish oocytes are mimicked by the nuclear injection of inositol 1,4,5-trisphosphate and cADP-ribose Cell Calcium 22 1997 11-20
    • (1997) Cell Calcium , vol.22 , pp. 11-20
    • Santella, L.1    Kyozuka, K.2
  • 36
    • 0030780576 scopus 로고    scopus 로고
    • Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores
    • K. Subramanian T. Meyer Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores Cell 89 1997 963-971
    • (1997) Cell , vol.89 , pp. 963-971
    • Subramanian, K.1    Meyer, T.2
  • 37
    • 0025800065 scopus 로고
    • Foot protein isoforms are expressed at different times during embryonic chick skeletal muscle development
    • J.L. Sutko J.A. Airey K. Murakami M. Takeda C. Beck T. Deerinck M.H. Ellisman Foot protein isoforms are expressed at different times during embryonic chick skeletal muscle development J. Cell Biol. 113 1991 793-803
    • (1991) J. Cell Biol. , vol.113 , pp. 793-803
    • Sutko, J.L.1    Airey, J.A.2    Murakami, K.3    Takeda, M.4    Beck, C.5    Deerinck, T.6    Ellisman, M.H.7
  • 40
    • 0033639075 scopus 로고    scopus 로고
    • Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration
    • A. Tomilin A. Remenyi K. Lins H. Bak S. Leidel G. Vriend M. Wilmanns H.R. Scholer Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration Cell 103 2000 853-864
    • (2000) Cell , vol.103 , pp. 853-864
    • Tomilin, A.1    Remenyi, A.2    Lins, K.3    Bak, H.4    Leidel, S.5    Vriend, G.6    Wilmanns, M.7    Scholer, H.R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.