메뉴 건너뛰기




Volumn 76, Issue 5, 1998, Pages 779-785

Calreticulin, a multifunctional Ca2+ binding chaperone of the endoplasmic reticulum

Author keywords

Ca2+ binding protein; Calreticulin; Chaperone; Endoplasmic reticulum

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; CALNEXIN; CALRETICULIN; CHAPERONE; CALCIUM BINDING PROTEIN; RIBONUCLEOPROTEIN;

EID: 0032216661     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/bcb-76-5-779     Document Type: Conference Paper
Times cited : (96)

References (57)
  • 1
    • 0013624349 scopus 로고
    • Localization of calreticulin, a major calcium binding protein, in plant cells
    • Allen, N.S., and Tiwari, S.C. 1991. Localization of calreticulin, a major calcium binding protein, in plant cells. Plant Physiol. 96: 42.
    • (1991) Plant Physiol. , vol.96 , pp. 42
    • Allen, N.S.1    Tiwari, S.C.2
  • 3
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh, S., Burns, K., Andrin, C., and Michalak, M. 1995. Interaction of calreticulin with protein disulfide isomerase. J. Biol. Chem. 270: 31338-31344.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31338-31344
    • Baksh, S.1    Burns, K.2    Andrin, C.3    Michalak, M.4
  • 4
    • 0029989731 scopus 로고    scopus 로고
    • Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2
    • Baldan, B., Navazio, L., Friso, A., Mariani, P., and Meggio, F. 1996. Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2. Biochem. Biophys. Res. Commun. 221: 498-502.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 498-502
    • Baldan, B.1    Navazio, L.2    Friso, A.3    Mariani, P.4    Meggio, F.5
  • 7
    • 0032127595 scopus 로고    scopus 로고
    • Neuronal calcium signaling
    • Berridge, M.J. 1998. Neuronal calcium signaling. Neuron, 21: 13-26.
    • (1998) Neuron , vol.21 , pp. 13-26
    • Berridge, M.J.1
  • 10
    • 0028831997 scopus 로고
    • Calcium signaling
    • Clapham, D.E. 1995. Calcium signaling. Cell, 80: 259-268.
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 11
    • 0030978516 scopus 로고    scopus 로고
    • Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion
    • London
    • Coppolino, M., Woodside, M.J., Demaurex, N., Grinstein, S., St-Arnaud, R., and Dedhar, S. 1997. Calreticulin is essential for integrin-mediated calcium signalling and cell adhesion. Nature (London), 386: 843-847.
    • (1997) Nature , vol.386 , pp. 843-847
    • Coppolino, M.1    Woodside, M.J.2    Demaurex, N.3    Grinstein, S.4    St-Arnaud, R.5    Dedhar, S.6
  • 13
    • 0031214672 scopus 로고    scopus 로고
    • Cloning and characterization of the calreticulin gene from Ricinus comunis L
    • Coughlan, S.J., Craig, H., and Winfrey, R. 1997. Cloning and characterization of the calreticulin gene from Ricinus comunis L. Plant Mol. Biol. 34: 897-911.
    • (1997) Plant Mol. Biol. , vol.34 , pp. 897-911
    • Coughlan, S.J.1    Craig, H.2    Winfrey, R.3
  • 14
    • 0031774263 scopus 로고    scopus 로고
    • BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress
    • Crofts, A.J., Leborgne-Castel, N., Pesca, M., Vitale, A., and Denecke, J. 1998. BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress. Plant Cell, 10: 813-823.
    • (1998) Plant Cell , vol.10 , pp. 813-823
    • Crofts, A.J.1    Leborgne-Castel, N.2    Pesca, M.3    Vitale, A.4    Denecke, J.5
  • 15
    • 0028240392 scopus 로고
    • Novel functions for calreticulin: Interaction with integrins and modulation of gene expression
    • Dedhar, S. 1994. Novel functions for calreticulin: interaction with integrins and modulation of gene expression. Trends Biochem. Sci. 19: 269-271.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 269-271
    • Dedhar, S.1
  • 16
    • 0000531516 scopus 로고
    • Analysis of sorting signals responsible for the accumulation of soluble reticuloplasmins in the plant endoplasmic reticulum
    • Denecke, J., Ek, B., Caspers, M., Sinjorgo, K.M.C., and Palva, E.T. 1993. Analysis of sorting signals responsible for the accumulation of soluble reticuloplasmins in the plant endoplasmic reticulum. J. Exp. Bot. 44: 213-221.
    • (1993) J. Exp. Bot. , vol.44 , pp. 213-221
    • Denecke, J.1    Ek, B.2    Caspers, M.3    Sinjorgo, K.M.C.4    Palva, E.T.5
  • 18
    • 0030130430 scopus 로고    scopus 로고
    • Isolation of full length cDNA encoding calreticulin from a PCR library of in vitro zygotes of maize
    • Dresselhaus, T., Hagel, C., Lörz, H., and Kranz, E. 1996. Isolation of full length cDNA encoding calreticulin from a PCR library of in vitro zygotes of maize. Plant Mol. Biol. 31: 23-34.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 23-34
    • Dresselhaus, T.1    Hagel, C.2    Lörz, H.3    Kranz, E.4
  • 19
    • 0030834284 scopus 로고    scopus 로고
    • Identification of calreticulin-like protein as one of the phosphoproteins modulated in response to oligogalacturonides in tobacco cells
    • Droillard, M.-J., Güclü, J., Le Caer, J.-P., Mathieu, Y., Guern, J., and Laurière, C. 1997. Identification of calreticulin-like protein as one of the phosphoproteins modulated in response to oligogalacturonides in tobacco cells. Planta, 202: 341-348.
    • (1997) Planta , vol.202 , pp. 341-348
    • Droillard, M.-J.1    Güclü, J.2    Le Caer, J.-P.3    Mathieu, Y.4    Guern, J.L.C.5
  • 20
    • 0031843044 scopus 로고    scopus 로고
    • Delayed activation of the store-operated calcium current induced by calreticulin overexpression in RBL-1 cells
    • Fasolato, C., Pizzo, P., and Pozzan, T. 1998. Delayed activation of the store-operated calcium current induced by calreticulin overexpression in RBL-1 cells. Mol. Biol. Cell, 9: 1513-1522.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1513-1522
    • Fasolato, C.1    Pizzo, P.2    Pozzan, T.3
  • 23
    • 0032563599 scopus 로고    scopus 로고
    • Differential modulation of SERCA2 isoforms by calretriculin
    • John, L.M., Lechleiter, J.D., and Camacho, P. 1998. Differential modulation of SERCA2 isoforms by calretriculin. J. Cell Biol. 142: 963-973.
    • (1998) J. Cell Biol. , vol.142 , pp. 963-973
    • John, L.M.1    Lechleiter, J.D.2    Camacho, P.3
  • 24
    • 0030096580 scopus 로고    scopus 로고
    • Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation
    • Knight, H., Trewavas, A.J., and Knight, M.R. 1996. Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation. Plant Cell, 8: 489-503.
    • (1996) Plant Cell , vol.8 , pp. 489-503
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 25
    • 0031279985 scopus 로고    scopus 로고
    • Calcium signalling in Arabidopsis thaliana responding to drought and salinity
    • Knight, H., Trewavas, A.J., and Knight, M.R. 1997. Calcium signalling in Arabidopsis thaliana responding to drought and salinity. Plant. J. 12: 1067-1078.
    • (1997) Plant. J. , vol.12 , pp. 1067-1078
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 26
    • 0030897340 scopus 로고    scopus 로고
    • Cabeticulin
    • Krause, K.-H., and Michalak, M. 1997. Cabeticulin. Cell, 88: 439-443.
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.-H.1    Michalak, M.2
  • 27
    • 0028020123 scopus 로고
    • 2+ response to bradykinin and increases sensitivity to ionomycin in NG-108-15 cells
    • 2+ response to bradykinin and increases sensitivity to ionomycin in NG-108-15 cells. J. Biol. Chem. 269: 28635-28639.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28635-28639
    • Liu, N.1    Fine, R.E.2    Simons, E.3    Johnson, R.J.4
  • 28
    • 0032540349 scopus 로고    scopus 로고
    • ERcalcistorin/protein-disulfide isomerase acts as a calcium storage protein in the endoplasmic reticulum of a living cell
    • Lucero, H., Lebeche, D., and Kaminer, B. 1998. ERcalcistorin/protein-disulfide isomerase acts as a calcium storage protein in the endoplasmic reticulum of a living cell. J. Biol. Chem. 273: 9857-9863.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9857-9863
    • Lucero, H.1    Lebeche, D.2    Kaminer, B.3
  • 34
    • 0004118576 scopus 로고    scopus 로고
    • R.G. Landes Company, Biomedical Publishers, Austin, Tex.
    • Michalak, M. (Editor). 1996. Calreticulin. R.G. Landes Company, Biomedical Publishers, Austin, Tex.
    • (1996) Calreticulin
    • Michalak, M.E.1
  • 36
    • 0029828912 scopus 로고    scopus 로고
    • Endoplasmic reticulum form of calreticulin modulates glucocorticoid-sensitive gene expression
    • Michalak, M., Burns, K., Mesaeli, N., Andrin, C., Jass, G.H., Busaan, J.L., and Opas, M. 1996. Endoplasmic reticulum form of calreticulin modulates glucocorticoid-sensitive gene expression. J. Biol. Chem. 271: 29436-29445.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29436-29445
    • Michalak, M.1    Burns, K.2    Mesaeli, N.3    Andrin, C.4    Jass, G.H.5    Busaan, J.L.6    Opas, M.7
  • 39
    • 0027982729 scopus 로고
    • Calreticulin, not just another calcium-binding protein
    • Nash, P.D., Opas, M., and Michalak, M. 1994. Calreticulin, not just another calcium-binding protein. Mol. Cell. Biochem. 135: 71-78.
    • (1994) Mol. Cell. Biochem. , vol.135 , pp. 71-78
    • Nash, P.D.1    Opas, M.2    Michalak, M.3
  • 40
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef, W.M., McCormick, S.J., and Clark, R.A. 1995. Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem. 270: 4741-4747.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4741-4747
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 41
    • 0032549522 scopus 로고    scopus 로고
    • Coordinated participation of calreticulin and calnexin in the biosynthesis of myeloperoxidase
    • Nauseef, W.M., McCormick, S.J., and Goedken, M. 1998. Coordinated participation of calreticulin and calnexin in the biosynthesis of myeloperoxidase. J. Biol. Chem. 273: 7107-7111.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7107-7111
    • Nauseef, W.M.1    McCormick, S.J.2    Goedken, M.3
  • 43
    • 0029751274 scopus 로고    scopus 로고
    • Primary structure of the N-linked carbohydrate chains of calreticulin from spinach leaves
    • Navazio, L., Baldan, B., Mariani, P., Gerwig, G.J., and Vliegenthart, J.F.G. 1996. Primary structure of the N-linked carbohydrate chains of calreticulin from spinach leaves. Glycoconj. J. 13: 977-983.
    • (1996) Glycoconj. J. , vol.13 , pp. 977-983
    • Navazio, L.1    Baldan, B.2    Mariani, P.3    Gerwig, G.J.4    Vliegenthart, J.F.G.5
  • 45
    • 0031131643 scopus 로고    scopus 로고
    • Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana
    • Nelson, D.E., Glausinger, B., and Bonhert, H.J. 1997. Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana. Plant Physiol. 114: 29-37.
    • (1997) Plant Physiol. , vol.114 , pp. 29-37
    • Nelson, D.E.1    Glausinger, B.2    Bonhert, H.J.3
  • 47
    • 0001116042 scopus 로고    scopus 로고
    • Calreticulin in plant cells
    • Opas, M., Milner, R.E., and Michalak, M. 1996a. Calreticulin in plant cells. Protoplasma, 191: 164-171.
    • (1996) Protoplasma , vol.191 , pp. 164-171
    • Opas, M.1    Milner, R.E.2    Michalak, M.3
  • 48
    • 0030459614 scopus 로고    scopus 로고
    • Calreticulin modulates cell adhesiveness via regulation of vinculin expression
    • Opas, M., Szewczenko-Pawlikowski, M., Jass, G.K., Mesaeli, N., and Michalak, M. 1996b. Calreticulin modulates cell adhesiveness via regulation of vinculin expression. J. Cell Biol. 135: 1913-1923.
    • (1996) J. Cell Biol. , vol.135 , pp. 1913-1923
    • Opas, M.1    Szewczenko-Pawlikowski, M.2    Jass, G.K.3    Mesaeli, N.4    Michalak, M.5
  • 49
    • 0015955240 scopus 로고
    • Isolation of a high affinity calcium binding protein from sarcoplasmic reticulum
    • Ostwald, T.J., and MacLennan, D.H. 1974. Isolation of a high affinity calcium binding protein from sarcoplasmic reticulum. J. Biol. Chem. 249: 974-979.
    • (1974) J. Biol. Chem. , vol.249 , pp. 974-979
    • Ostwald, T.J.1    Maclennan, D.H.2
  • 51
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan, T., Rizzuto, R., Volpe, P., and Meldolesi, J. 1994. Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev. 74: 595-636.
    • (1994) Physiol. Rev. , vol.74 , pp. 595-636
    • Pozzan, T.1    Rizzuto, R.2    Volpe, P.3    Meldolesi, J.4
  • 52
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin a subunits
    • Rojiani, M.V., Finlay, B.B., Gray, V., and Dedhar, S. 1991. In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin a subunits. Biochemistry, 30: 9859-9866.
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 53
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstruction of phylogenetic trees
    • Saitou, N., and Nei, M. 1987. The neighbor-joining method: a new method for reconstruction of phylogenetic trees. Mol. Biol. Evol. 4: 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 54
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Sapiro, R.G., Zhu, Q., Bhoyroo, V., and Söling, H.D. 1996. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem. 271: 11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Sapiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Söling, H.D.4
  • 55
    • 0000673326 scopus 로고
    • Calreticulin: The diverse functional repertoire of a new human autoantigen
    • Sontheimer, R.D., Lieu, T.-S., and Capra, J.D. 1993. Calreticulin: the diverse functional repertoire of a new human autoantigen. Immunologist, 1: 155-160.
    • (1993) Immunologist , vol.1 , pp. 155-160
    • Sontheimer, R.D.1    Lieu, T.-S.2    Capra, J.D.3
  • 56
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperone, calnexin and calreticulin
    • Vassilakos, A., Michalak, M., Lehrman, M.A. and Williams, D.B. 1998. Oligosaccharide binding characteristics of the molecular chaperone, calnexin and calreticulin. Biochemistry, 36: 3480-3490.
    • (1998) Biochemistry , vol.36 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 57
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun, A., Darby, N.J., Tessier, D.C., Michalak, M., Bergeron, J.J.M., and Thomas, D.Y. 1998. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273: 6009-6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.M.5    Thomas, D.Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.