메뉴 건너뛰기




Volumn 28, Issue 3, 1996, Pages 455-465

The presence and partitioning of calcium binding proteins in hepatic and cardiac nuclei

Author keywords

Calcium binding protein; Calnexin; Calsequestrin; Electrophoresis; Nucleus; Stains All; Western blotting

Indexed keywords

CALCIUM BINDING PROTEIN; CALNEXIN; CALSEQUESTRIN; NUCLEAR PROTEIN; SODIUM CHLORIDE;

EID: 0029914561     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmcc.1996.0042     Document Type: Article
Times cited : (17)

References (42)
  • 1
  • 2
    • 0026951318 scopus 로고
    • Calcium channels in the heart: An overview
    • BALKE CW, GOLD MR, 1992. Calcium channels in the heart: An overview. Heart Dis Stroke 1: 398-403.
    • (1992) Heart Dis Stroke , vol.1 , pp. 398-403
    • Balke, C.W.1    Gold, M.R.2
  • 4
    • 0021100150 scopus 로고
    • 2+-dependent elution from phenyl-sepharose
    • 2+-dependent elution from phenyl-sepharose. J Biol Chem 258: 11932-11936.
    • (1983) J Biol Chem , vol.258 , pp. 11932-11936
    • Cala, S.E.1    Jones, L.R.2
  • 5
    • 0027398879 scopus 로고
    • Purification of a 90-kDa protein (Band VII) from cardiac sarcoplasmic reticulum. Identification as calnexin and localization of casein kinase II phosphorylation sites
    • CALA SE, ULBRIGHT C, KELLEY JS, JONES LR, 1993. Purification of a 90-kDa protein (Band VII) from cardiac sarcoplasmic reticulum. Identification as calnexin and localization of casein kinase II phosphorylation sites. J Biol Chem 268: 2969-2975.
    • (1993) J Biol Chem , vol.268 , pp. 2969-2975
    • Cala, S.E.1    Ulbright, C.2    Kelley, J.S.3    Jones, L.R.4
  • 6
    • 0020643575 scopus 로고
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye "Stains-all."
    • 2+-binding proteins, calsequestrin, calmodulin, troponin C, and S-100, with the cationic carbocyanine dye "Stains-all." J Biol Chem 258: 11267-11273.
    • (1983) J Biol Chem , vol.258 , pp. 11267-11273
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3
  • 7
    • 0021111582 scopus 로고
    • Purification and characterization of calsequestrin from canine cardiac sarcoplasmic reticulum and identification of the 53,000 dalton glycoprotein
    • CAMPBELL KP, MACLENNAN DH, JORGENSEN AO, MINTZER MC, 1983b. Purification and characterization of calsequestrin from canine cardiac sarcoplasmic reticulum and identification of the 53,000 dalton glycoprotein. J Biol Chem 258: 1197-1204.
    • (1983) J Biol Chem , vol.258 , pp. 1197-1204
    • Campbell, K.P.1    MacLennan, D.H.2    Jorgensen, A.O.3    Mintzer, M.C.4
  • 8
    • 0023160147 scopus 로고
    • DNA repair in human cells: Methods for the determination of calmodulin involvement
    • CHARP PA, 1987. DNA repair in human cells: methods for the determination of calmodulin involvement. Methods Enzymol 139: 715-730.
    • (1987) Methods Enzymol , vol.139 , pp. 715-730
    • Charp, P.A.1
  • 13
    • 0027415086 scopus 로고
    • Identification and purification of a calcium-binding protein in hepatic nuclear membranes
    • GILCHRIST JSC, PIERCE GN, 1993. Identification and purification of a calcium-binding protein in hepatic nuclear membranes. J Biol Chem 268: 4291-4299.
    • (1993) J Biol Chem , vol.268 , pp. 4291-4299
    • Gilchrist, J.S.C.1    Pierce, G.N.2
  • 14
    • 0025014719 scopus 로고
    • Subcellular calcium transients visualized by confocal microscopy in a voltage-clamped vertebrate neuron
    • HERNANDEZ-CRUZ A, SALA F, ADAMS PR, 1990. Subcellular calcium transients visualized by confocal microscopy in a voltage-clamped vertebrate neuron. Science 247: 858-862.
    • (1990) Science , vol.247 , pp. 858-862
    • Hernandez-Cruz, A.1    Sala, F.2    Adams, P.R.3
  • 16
    • 0025933191 scopus 로고
    • Calcium-induced release of calcium regulates differentiation of cultured spinal neurons
    • HOLLIDAY J, ADAMS RJ, SEJNOWSKI TJ, SPITZER NC, 1991. Calcium-induced release of calcium regulates differentiation of cultured spinal neurons. Neuron 7: 787-796.
    • (1991) Neuron , vol.7 , pp. 787-796
    • Holliday, J.1    Adams, R.J.2    Sejnowski, T.J.3    Spitzer, N.C.4
  • 17
    • 0019325282 scopus 로고
    • Fractionation of rat ventricular nuclei
    • JACKOWSKI G, LIEW CC, 1980. Fractionation of rat ventricular nuclei. Biochem J 188: 363-373.
    • (1980) Biochem J , vol.188 , pp. 363-373
    • Jackowski, G.1    Liew, C.C.2
  • 18
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • JACKSON MR, COHEN-DOYLE MF, PETERSON PA, WILLIAMS DB, 1994. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 263: 384-387.
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 19
  • 20
    • 0019471221 scopus 로고
    • Considerations in the isolation of rat liver nuclear matrix, nuclear envelope, and pore complex lamina
    • KAUFMANN SH, COFFEY DS, SHAPER JH, 1981. Considerations in the isolation of rat liver nuclear matrix, nuclear envelope, and pore complex lamina. Exp Cell Res 132: 105-123.
    • (1981) Exp Cell Res , vol.132 , pp. 105-123
    • Kaufmann, S.H.1    Coffey, D.S.2    Shaper, J.H.3
  • 21
    • 0024478377 scopus 로고
    • 2+ regulates hormone secretion and proopiomelanocortin gene expression in melanotrope cells via the calmodulin and the protein kinase C pathways
    • 2+ regulates hormone secretion and proopiomelanocortin gene expression in melanotrope cells via the calmodulin and the protein kinase C pathways. J Neurochem 52: 1279-1283.
    • (1989) J Neurochem , vol.52 , pp. 1279-1283
    • Loeffler, J.P.1    Kley, N.2    Louis, J.C.3    Demeneix, B.A.4
  • 23
    • 0342423455 scopus 로고
    • Structure, function and biosynthesis of sarcoplasmic reticulum proteins
    • MACLENNAN DH, CAMPBELL KP, 1979. Structure, function and biosynthesis of sarcoplasmic reticulum proteins. Trends Biochem Sci 4: 148-151.
    • (1979) Trends Biochem Sci , vol.4 , pp. 148-151
    • MacLennan, D.H.1    Campbell, K.P.2
  • 24
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J Biochem 95: 511-519.
    • (1984) J Biochem , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 25
    • 0027530629 scopus 로고
    • Stimulation of nuclear protein kinase C leads to phosphorylation of nuclear inositol 1,4,5-trisphosphate receptor and accelerated calcium release by inositol 1,4,5-trisphosphate from isolated rat liver nuclei
    • MATTER N, RITZ MF, FREYERMUTH S, ROGUE P, MALVIYA AN, 1993. Stimulation of nuclear protein kinase C leads to phosphorylation of nuclear inositol 1,4,5-trisphosphate receptor and accelerated calcium release by inositol 1,4,5-trisphosphate from isolated rat liver nuclei. J Biol Chem 268: 732-736.
    • (1993) J Biol Chem , vol.268 , pp. 732-736
    • Matter, N.1    Ritz, M.F.2    Freyermuth, S.3    Rogue, P.4    Malviya, A.N.5
  • 28
    • 0024477528 scopus 로고
    • Cardiac contractile protein ATPase activity in a diet induced model of noninsulin dependent diabetes mellitus
    • PIERCE GN, LOCKWOOD MK, ECKHERT CD, 1989a. Cardiac contractile protein ATPase activity in a diet induced model of noninsulin dependent diabetes mellitus. Can J Cardiol 5: 117-120.
    • (1989) Can J Cardiol , vol.5 , pp. 117-120
    • Pierce, G.N.1    Lockwood, M.K.2    Eckhert, C.D.3
  • 29
    • 0024598302 scopus 로고
    • Effects of chronic swimming training on cardiac sarcolemmal function and composition
    • PIERCE GN, SEKHON PS, MENG H, MADDAFORD TG, 1989b. Effects of chronic swimming training on cardiac sarcolemmal function and composition. J Appl Physiol 66: 1715-1721.
    • (1989) J Appl Physiol , vol.66 , pp. 1715-1721
    • Pierce, G.N.1    Sekhon, P.S.2    Meng, H.3    Maddaford, T.G.4
  • 30
    • 0021840109 scopus 로고
    • Changes of free calcium levels with stages of the cell division cycle
    • POENIE M, ALDERTON J, TSIEN RY, STEINHARDT RA, 1985. Changes of free calcium levels with stages of the cell division cycle. Nature 315: 147-150.
    • (1985) Nature , vol.315 , pp. 147-150
    • Poenie, M.1    Alderton, J.2    Tsien, R.Y.3    Steinhardt, R.A.4
  • 31
    • 0025971503 scopus 로고
    • Stimulated rise in neuronal calcium is faster and greater in the nucleus than the cytosol
    • PRZYWARA DA, BHAVE SV, BHAVE A, WAKADE TD, WAKADE AR, 1991. Stimulated rise in neuronal calcium is faster and greater in the nucleus than the cytosol. FASEB J 5: 217-222.
    • (1991) FASEB J , vol.5 , pp. 217-222
    • Przywara, D.A.1    Bhave, S.V.2    Bhave, A.3    Wakade, T.D.4    Wakade, A.R.5
  • 33
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • RAJAGOPALAN S, XU Y BRENNER MB, 1994. Retention of unassembled components of integral membrane proteins by calnexin. Science 263: 387-390.
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 35
    • 0025270328 scopus 로고
    • Membrane depolarization and calcium induce c-fos transcription via phosphorylation of transcription factor CREB
    • SHENG M, MCFADDEN G, GREENBERG ME, 1990. Membrane depolarization and calcium induce c-fos transcription via phosphorylation of transcription factor CREB. Neuron 4: 571-582.
    • (1990) Neuron , vol.4 , pp. 571-582
    • Sheng, M.1    McFadden, G.2    Greenberg, M.E.3
  • 36
    • 0025807509 scopus 로고
    • 2+-regulated transcription factor phosphorylated by calmodulin-dependent kinases
    • 2+-regulated transcription factor phosphorylated by calmodulin-dependent kinases. Science 252: 1427-1430.
    • (1991) Science , vol.252 , pp. 1427-1430
    • Sheng, M.1    Thompson, M.A.2    Greenberg, M.E.3
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitro-cellulose sheets: Procedure and some applications
    • TOWBIN H, STAEHLIN T, GORDON J, 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitro-cellulose 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    Staehlin, T.2    Gordon, J.3
  • 40
    • 0024326031 scopus 로고
    • Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium
    • VAN PN, PETER F, SOLING HD, 1989. Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium. J Biol Chem 264: 17494-17501.
    • (1989) J Biol Chem , vol.264 , pp. 17494-17501
    • Van, P.N.1    Peter, F.2    Soling, H.D.3
  • 41
    • 0342423441 scopus 로고
    • Cheung WY, ed. Academic Press: New York
    • WHITE BA, BANCROFT C, 1987. In: Cheung WY, ed. Calcium and Cell Function Vol. 7, Academic Press: New York, 109-132.
    • (1987) Calcium and Cell Function , vol.7 , pp. 109-132
    • White, B.A.1    Bancroft, C.2
  • 42
    • 0022351039 scopus 로고
    • Calcium gradients in single smooth muscle cells revealed by the digital imaging microscope using Fura-2
    • WILLIAMS DA, FOGARTY KE, TSIEN RY, FAY FS, 1985. Calcium gradients in single smooth muscle cells revealed by the digital imaging microscope using Fura-2. Nature 318: 558-561.
    • (1985) Nature , vol.318 , pp. 558-561
    • Williams, D.A.1    Fogarty, K.E.2    Tsien, R.Y.3    Fay, F.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.