메뉴 건너뛰기




Volumn 263, Issue 1, 2004, Pages 137-142

Calreticulin in the heart

Author keywords

Calcium binding proteins; Cardiac arrhythmia; Cardiac development; Chaperone; Endoplasmic reticulum

Indexed keywords

BINDING PROTEIN; CALNEXIN; CALRETICULIN; CHAPERONE;

EID: 4544307105     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MCBI.0000041855.10149.5f     Document Type: Article
Times cited : (26)

References (60)
  • 1
    • 0033209269 scopus 로고    scopus 로고
    • Introduction: Molecular chaperones of the ER: Their role in protein folding and genetic disease
    • Brooks DA: Introduction: Molecular chaperones of the ER: Their role in protein folding and genetic disease. Semin Cell Dev Biol 10: 441-442, 1999
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 441-442
    • Brooks, D.A.1
  • 7
    • 0035355341 scopus 로고    scopus 로고
    • 2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: Significance for the molecular mechanism of Bcl-2 action
    • 2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: Significance for the molecular mechanism of Bcl-2 action. EMBO J 20: 2690-2701, 2001
    • (2001) EMBO J. , vol.20 , pp. 2690-2701
    • Pinton, P.1    Ferrari, D.2    Rapizzi, E.3    Virgilio, F.D.4    Pozzan, T.5    Rizzuto, R.6
  • 9
    • 0036182380 scopus 로고    scopus 로고
    • Calcium and oxidative stress: From cell signaling to cell death
    • Ermak G, Davies KJ: Calcium and oxidative stress: from cell signaling to cell death. Mol Immunol 38: 713-721, 2002
    • (2002) Mol. Immunol. , vol.38 , pp. 713-721
    • Ermak, G.1    Davies, K.J.2
  • 15
    • 0028916152 scopus 로고
    • Death before birth: Clues from gene knockouts and mutations
    • Copp AJ: Death before birth: Clues from gene knockouts and mutations. Trends Genet 1: 87-93, 1995
    • (1995) Trends Genet. , vol.1 , pp. 87-93
    • Copp, A.J.1
  • 16
    • 0030046595 scopus 로고    scopus 로고
    • Mouse mutants and cardiac development: New molecular insights into cardiogenesis
    • Rossant J: Mouse mutants and cardiac development: New molecular insights into cardiogenesis. Circ Res 78: 349-353, 1996
    • (1996) Circ. Res. , vol.78 , pp. 349-353
    • Rossant, J.1
  • 19
    • 0033485263 scopus 로고    scopus 로고
    • Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins
    • Saito Y, Ihara Y, Leach MR, Cohen-Doyle MF, Williams DB: Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J 18: 6718-6729, 1999
    • (1999) EMBO J. , vol.18 , pp. 6718-6729
    • Saito, Y.1    Ihara, Y.2    Leach, M.R.3    Cohen-Doyle, M.F.4    Williams, D.B.5
  • 20
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A: Setting the standards: Quality control in the secretory pathway. Science 286: 1882-1888, 1999
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 24
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RAF, Michalak M: Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 264: 21522-21528, 1989
    • (1989) J. Biol. Chem. , vol.264 , pp. 21522-21528
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.F.4    Michalak, M.5
  • 25
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein
    • Smith MJ, Koch GLE: Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J 8: 3581-3586, 1989
    • (1989) EMBO J. , vol.8 , pp. 3581-3586
    • Smith, M.J.1    Koch, G.E.2
  • 27
    • 0023037907 scopus 로고
    • Conformational changes induced by binding of divalent cations to calregulin
    • Khanna NC, Tokuda M, Waisman DM: Conformational changes induced by binding of divalent cations to calregulin. J Biol Chem 261: 8883-8887, 1986
    • (1986) J. Biol. Chem. , vol.261 , pp. 8883-8887
    • Khanna, N.C.1    Tokuda, M.2    Waisman, D.M.3
  • 36
    • 0032563599 scopus 로고    scopus 로고
    • Differential modulation of SERCA2 isoforms by calreticulin
    • John LM, Lechleiter JD, Camacho P: Differential modulation of SERCA2 isoforms by calreticulin. J Cell Biol 142: 963-973, 1998
    • (1998) J. Cell Biol. , vol.142 , pp. 963-973
    • John, L.M.1    Lechleiter, J.D.2    Camacho, P.3
  • 38
    • 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, Pozzan T: Delayed activation of the store-operated calcium current induced by calreticulin overexpression in RBL-1 cells. Mol Biol Cell 9: 1513-1522, 1998
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1513-1522
    • Fasolato, C.1    Pizzo, P.2    Pozzan, T.3
  • 40
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth C, Koch GLE: Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 59: 729-737, 1989
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.E.2
  • 41
    • 0025313861 scopus 로고
    • Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum
    • Lodish HF, Kong N: Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum. J Biol Chem 265: 10893-10899, 1990
    • (1990) J. Biol. Chem. , vol.265 , pp. 10893-10899
    • Lodish, H.F.1    Kong, N.2
  • 42
    • 0026654505 scopus 로고
    • Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum
    • Lodish HF, Kong N, Wikstrom L: Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum. J Biol Chem 267: 12753-12760, 1992
    • (1992) J. Biol. Chem. , vol.267 , pp. 12753-12760
    • Lodish, H.F.1    Kong, N.2    Wikstrom, L.3
  • 43
    • 0034235397 scopus 로고    scopus 로고
    • Calcium, a signaling molecule in the endoplasmic reticulum?
    • Corbett EF, Michalak M: Calcium, a signaling molecule in the endoplasmic reticulum? Trends Biochem Sci 25: 307-311, 2000
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 307-311
    • Corbett, E.F.1    Michalak, M.2
  • 45
    • 0025834610 scopus 로고
    • Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum
    • Milner RE, Baksh S, Shemanko C, Carpenter MR, Smillie L, Vance JE, Opas M, Michalak M: Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum. J Biol Chem 266: 7155-7165, 1991
    • (1991) J. Biol. Chem. , vol.266 , pp. 7155-7165
    • Milner, R.E.1    Baksh, S.2    Shemanko, C.3    Carpenter, M.R.4    Smillie, L.5    Vance, J.E.6    Opas, M.7    Michalak, M.8
  • 46
    • 0026637858 scopus 로고
    • Widespread tissue distribution of rabbit calreticulin, a non-muscle functional analogue of calsequestrin
    • Tharin S, Dziak E, Michalak M, Opas M: Widespread tissue distribution of rabbit calreticulin, a non-muscle functional analogue of calsequestrin. Cell Tissue Res 269: 29-37, 1992
    • (1992) Cell Tissue Res. , vol.269 , pp. 29-37
    • Tharin, S.1    Dziak, E.2    Michalak, M.3    Opas, M.4
  • 51
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao A, Luo C, Hogan PG: Transcription factors of the NFAT family: regulation and function. Annu Rev Immunol 15: 707-747, 1997
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 55
    • 0030248881 scopus 로고    scopus 로고
    • Connexins in mammalian heart function
    • Gros DB, Jongsma HJ: Connexins in mammalian heart function. Bioessays 18: 719-730, 1996
    • (1996) Bioessays , vol.18 , pp. 719-730
    • Gros, D.B.1    Jongsma, H.J.2
  • 56
    • 0032076163 scopus 로고    scopus 로고
    • Cardiomyocyte gap junctions: A target for growth factor signaling
    • Kardami E, Doble BW: Cardiomyocyte gap junctions: A target for growth factor signaling. Trends Cardiovasc Med 8: 180-187, 1998
    • (1998) Trends Cardiovasc. Med. , vol.8 , pp. 180-187
    • Kardami, E.1    Doble, B.W.2
  • 57
    • 0037205465 scopus 로고    scopus 로고
    • Overexpression of calreticulin modulates protein kinase B/Akt signaling to pomote apoptosis during cardiac differentiation of cardiomyoblast H9c2 cells
    • Kageyama K, Ihara Y, Goto S, Urata Y, Toda G, Yano K, Kondo T: Overexpression of calreticulin modulates protein kinase B/Akt signaling to pomote apoptosis during cardiac differentiation of cardiomyoblast H9c2 cells. J Biol Chem 277: 19255-19264, 2002
    • (2002) J. Biol. Chem. , vol.277 , pp. 19255-19264
    • Kageyama, K.1    Ihara, Y.2    Goto, S.3    Urata, Y.4    Toda, G.5    Yano, K.6    Kondo, T.7
  • 58
    • 0000645482 scopus 로고
    • Sur une maladie infantile et familial characterisee par des modifications permanents du pouls des attaques syncopales et epileptiforms et la mort subite
    • Morquio L: Sur une maladie infantile et familial characterisee par des modifications permanents du pouls des attaques syncopales et epileptiforms et la mort subite. Arch Med Inf 4: 467-469, 1901
    • (1901) Arch. Med. Inf. , vol.4 , pp. 467-469
    • Morquio, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.