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Volumn 417, Issue 3, 2009, Pages 651-666

Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum

Author keywords

Calcium homoeostasis; Calreticulin; Endoplasmic reticulum (ER); Protein folding; Quality control

Indexed keywords

CALRETICULIN; EMBRYONIC DEVELOPMENT; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM (ER); HOMOEOSTASIS; INTRACELLULAR CA; ISOMERASE; PROCESS PROPERTIES;

EID: 59849120392     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081847     Document Type: Review
Times cited : (586)

References (192)
  • 1
    • 0034235397 scopus 로고    scopus 로고
    • Calcium, a signaling molecule in the endoplasmic reticulum?
    • Corbett, E. F. and Michalak, M. (2000) Calcium, a signaling molecule in the endoplasmic reticulum? Trends Biochem. Sci. 25, 307-311
    • (2000) Trends Biochem. Sci , vol.25 , pp. 307-311
    • Corbett, E.F.1    Michalak, M.2
  • 2
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • Hebert, D. N. and Molinari, M. (2007) In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol. Rev. 87, 1377-1408
    • (2007) Physiol. Rev , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 4
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel, L., Burns, K., MacLennan, D. H., Reithmeier, R. A. F. and Michalak, M. (1989) Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 264, 21522-21528
    • (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
  • 5
    • 0024829021 scopus 로고
    • Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein
    • Smith, M. J. and Koch, G. L. E. (1989) Multiple zones in the sequence of calreticulin (CRP55, calregulin, HACBP), a major calcium binding ER/SR protein. EMBO J. 8, 3581-3586
    • (1989) EMBO J , vol.8 , pp. 3581-3586
    • Smith, M.J.1    Koch, G.L.E.2
  • 6
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag, J. D., Bergeron, J. J. M., Li, Y., Borisova, S., Hahn, M., Thomas, D. Y. and Cygler, M. (2001) The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8, 633-644
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.M.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6    Cygler, M.7
  • 7
    • 0036877146 scopus 로고    scopus 로고
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 32, 269-278
    • (2002) Cell Calcium , vol.32 , pp. 269-278
    • Michalak, M.1    Parker, J.M.R.2    Opas, M.3
  • 8
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach, M. R., Cohen-Doyle, M. F., Thomas, D. Y. and Williams, D. B. (2002) Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J. Biol. Chem. 277, 29686-29697
    • (2002) J. Biol. Chem , vol.277 , pp. 29686-29697
    • Leach, M.R.1    Cohen-Doyle, M.F.2    Thomas, D.Y.3    Williams, D.B.4
  • 9
    • 0346727443 scopus 로고    scopus 로고
    • Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: Pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition
    • Kapoor, M., Ellgaard, L., Gopalakrishnapai, J., Schirra, C., Gemma, E., Oscarson, S., Helenius, A. and Surolia, A. (2004) Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition. Biochemistry 43, 97-106
    • (2004) Biochemistry , vol.43 , pp. 97-106
    • Kapoor, M.1    Ellgaard, L.2    Gopalakrishnapai, J.3    Schirra, C.4    Gemma, E.5    Oscarson, S.6    Helenius, A.7    Surolia, A.8
  • 13
    • 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, M. R., Cohen-Doyle, M. F. and Williams, D. B. (1999) Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J. 18, 6718-6729
    • (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
  • 14
    • 25844474620 scopus 로고    scopus 로고
    • Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein
    • Thammavongsa, V., Mancino, L. and Raghavan, M. (2005) Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein. J. Biol. Chem. 280, 33497-33505
    • (2005) J. Biol. Chem , vol.280 , pp. 33497-33505
    • Thammavongsa, V.1    Mancino, L.2    Raghavan, M.3
  • 15
    • 26944462066 scopus 로고    scopus 로고
    • Delineation of the lectin site of the molecular chaperone calreticulin
    • Thomson, S. P. and Williams, D. B. (2005) Delineation of the lectin site of the molecular chaperone calreticulin. Cell Stress Chaperones 10, 242-251
    • (2005) Cell Stress Chaperones , vol.10 , pp. 242-251
    • Thomson, S.P.1    Williams, D.B.2
  • 18
    • 1542305433 scopus 로고    scopus 로고
    • Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation
    • Leach, M. R. and Williams, D. B. (2004) Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation. J. Biol. Chem. 279, 9072-9079
    • (2004) J. Biol. Chem , vol.279 , pp. 9072-9079
    • Leach, M.R.1    Williams, D.B.2
  • 20
    • 48749094772 scopus 로고    scopus 로고
    • Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
    • Ireland, B. S., Brockmeier, U., Howe, C. M., Elliott, T. and Williams, D. B. (2008) Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules. Mol. Biol. Cell 19, 2413-2423
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2413-2423
    • Ireland, B.S.1    Brockmeier, U.2    Howe, C.M.3    Elliott, T.4    Williams, D.B.5
  • 22
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • Vassilakos, A., Michalak, M., Lehrman, M. A. and Williams, D. B. (1998) Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37, 3480-3490
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 23
    • 0035846853 scopus 로고    scopus 로고
    • Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment
    • Ellgaard, L., Riek, R., Braun, D., Herrmann, T., Helenius, A. and Wüthrich, K. (2001) Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment. FEBS Lett. 488, 69-73
    • (2001) FEBS Lett , vol.488 , pp. 69-73
    • Ellgaard, L.1    Riek, R.2    Braun, D.3    Herrmann, T.4    Helenius, A.5    Wüthrich, K.6
  • 27
    • 0028205240 scopus 로고
    • Human, mouse, and rat calnexin cDNA cloning: Identification of potential calcium binding motifs and gene localization to human chromosome 5
    • Tjoelker, L. W., Seyfried, C. E., Eddy, Jr, R. L., Byers, M. G., Shows, T. B., Calderon, J. and Gray, P. W. (1994) Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. Biochemistry 33, 3229-3236
    • (1994) Biochemistry , vol.33 , pp. 3229-3236
    • Tjoelker, L.W.1    Seyfried, C.E.2    Eddy Jr, R.L.3    Byers, M.G.4    Shows, T.B.5    Calderon, J.6    Gray, P.W.7
  • 28
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver, J. D., van der Wal, F. J., Bulleid, N. J. and High, S. (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    van der Wal, F.J.2    Bulleid, N.J.3    High, S.4
  • 30
    • 30944449960 scopus 로고    scopus 로고
    • In vitro mapping of calnexin interaction with ribosomes
    • Delom, F. and Chevet, E. (2006) In vitro mapping of calnexin interaction with ribosomes. Biochem. Biophys. Res. Commun. 341, 39-44
    • (2006) Biochem. Biophys. Res. Commun , vol.341 , pp. 39-44
    • Delom, F.1    Chevet, E.2
  • 32
    • 0027057336 scopus 로고
    • Casein kinase II phosphorylation of signal sequence receptor a and the associated membrane chaperone calnexin
    • Ou, W. J., Thomas, D. Y., Bell, A. W. and Bergeron, J. J. (1992) Casein kinase II phosphorylation of signal sequence receptor a and the associated membrane chaperone calnexin. J. Biol. Chem. 267, 23789-23796
    • (1992) J. Biol. Chem , vol.267 , pp. 23789-23796
    • Ou, W.J.1    Thomas, D.Y.2    Bell, A.W.3    Bergeron, J.J.4
  • 36
    • 23944438373 scopus 로고    scopus 로고
    • Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57
    • Bedard, K., Szabo, E., Michalak, M. and Opas, M. (2005) Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57. Int. Rev. Cytol. 245, 91-121
    • (2005) Int. Rev. Cytol , vol.245 , pp. 91-121
    • Bedard, K.1    Szabo, E.2    Michalak, M.3    Opas, M.4
  • 37
    • 34948853214 scopus 로고    scopus 로고
    • GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion
    • Wanderling, S., Simen, B. B., Ostrovsky, O., Ahmed, N. T., Vogen, S. M., Gidalevitz, T. and Argon, Y. (2007) GRP94 is essential for mesoderm induction and muscle development because it regulates insulin-like growth factor secretion. Mol. Biol. Cell 18, 3764-3775
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3764-3775
    • Wanderling, S.1    Simen, B.B.2    Ostrovsky, O.3    Ahmed, N.T.4    Vogen, S.M.5    Gidalevitz, T.6    Argon, Y.7
  • 41
    • 26244451375 scopus 로고    scopus 로고
    • The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex
    • Elliott, T. and Williams, A. (2005) The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex. Immunol Rev. 207, 89-99
    • (2005) Immunol Rev , vol.207 , pp. 89-99
    • Elliott, T.1    Williams, A.2
  • 42
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • Wearsch, P. A. and Cresswell, P. (2007) Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat. Immunol. 8, 873-881
    • (2007) Nat. Immunol , vol.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 43
    • 33646594461 scopus 로고    scopus 로고
    • Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle
    • Solda, T., Garbi, N., Hammerling, G. J. and Molinari, M. (2006) Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle. J. Biol. Chem. 281, 6219-6126
    • (2006) J. Biol. Chem , vol.281 , pp. 6219-6126
    • Solda, T.1    Garbi, N.2    Hammerling, G.J.3    Molinari, M.4
  • 44
    • 0036169941 scopus 로고    scopus 로고
    • Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
    • Gao, B., Adhikari, R., Howarth, M., Nakamura, K., Gold, M. C., Hill, A. B., Knee, R., Michalak, M. and Elliott, T. (2002) Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16, 99-109
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3    Nakamura, K.4    Gold, M.C.5    Hill, A.B.6    Knee, R.7    Michalak, M.8    Elliott, T.9
  • 45
    • 1342334746 scopus 로고    scopus 로고
    • Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control
    • Molinari, M., Eriksson, K. K., Calanca, V., Galli, C., Cresswell, P., Michalak, M. and Helenius, A. (2004) Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol. Cell 13, 125-135
    • (2004) Mol. Cell , vol.13 , pp. 125-135
    • Molinari, M.1    Eriksson, K.K.2    Calanca, V.3    Galli, C.4    Cresswell, P.5    Michalak, M.6    Helenius, A.7
  • 47
    • 0035133393 scopus 로고    scopus 로고
    • ER calcium and the functions of intracellular organelles
    • Ashby, M. C. and Tepikin, A. V. (2001) ER calcium and the functions of intracellular organelles. Semin. Cell Dev. Biol. 12, 11-17
    • (2001) Semin. Cell Dev. Biol , vol.12 , pp. 11-17
    • Ashby, M.C.1    Tepikin, A.V.2
  • 48
    • 0028851245 scopus 로고
    • Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus
    • Greber, U. F. and Gerace, L. (1995) Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus. J. Cell Biol. 128, 5-14
    • (1995) J. Cell Biol , vol.128 , pp. 5-14
    • Greber, U.F.1    Gerace, L.2
  • 52
    • 0037195869 scopus 로고    scopus 로고
    • Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria
    • Arnaudeau, S., Frieden, M., Nakamura, K., Castelbou, C., Michalak, M. and Demaurex, N. (2002) Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria. J. Biol. Chem. 277, 46696-46705
    • (2002) J. Biol. Chem , vol.277 , pp. 46696-46705
    • Arnaudeau, S.1    Frieden, M.2    Nakamura, K.3    Castelbou, C.4    Michalak, M.5    Demaurex, N.6
  • 56
    • 0037184931 scopus 로고    scopus 로고
    • Cardiac-specific expression of calcineurin reverses embryonic lethality in calreticulin-deficient mouse
    • Guo, L., Nakamura, K., Lynch, J., Opas, M., Olson, E. N., Agellon, L. B. and Michalak, M. (2002) Cardiac-specific expression of calcineurin reverses embryonic lethality in calreticulin-deficient mouse. J. Biol. Chem. 277, 50776-50779
    • (2002) J. Biol. Chem , vol.277 , pp. 50776-50779
    • Guo, L.1    Nakamura, K.2    Lynch, J.3    Opas, M.4    Olson, E.N.5    Agellon, L.B.6    Michalak, M.7
  • 58
    • 0037393115 scopus 로고    scopus 로고
    • Effects of prenatal glucocorticoid exposure on cardiac calreticulin and calsequestrin protein expression during early development and in adulthood
    • Langdown, M. L., Holness, M. J. and Sugden, M. C. (2003) Effects of prenatal glucocorticoid exposure on cardiac calreticulin and calsequestrin protein expression during early development and in adulthood. Biochem. J. 371, 61-69
    • (2003) Biochem. J , vol.371 , pp. 61-69
    • Langdown, M.L.1    Holness, M.J.2    Sugden, M.C.3
  • 59
    • 0030876765 scopus 로고    scopus 로고
    • Regulation of calreticulin gene expression by calcium
    • Waser, M., Mesaeli, N., Spencer, C. and Michalak, M. (1997) Regulation of calreticulin gene expression by calcium. J. Cell Biol. 138, 547-557
    • (1997) J. Cell Biol , vol.138 , pp. 547-557
    • Waser, M.1    Mesaeli, N.2    Spencer, C.3    Michalak, M.4
  • 60
    • 41149086194 scopus 로고    scopus 로고
    • Regulation of the calreticulin gene by GATA6 and Evi-1 transcription factors
    • Qiu, Y., Lynch, J., Guo, L., Yatsula, B., Perkins, A. S. and Michalak, M. (2008) Regulation of the calreticulin gene by GATA6 and Evi-1 transcription factors. Biochemistry 47, 3697-3704
    • (2008) Biochemistry , vol.47 , pp. 3697-3704
    • Qiu, Y.1    Lynch, J.2    Guo, L.3    Yatsula, B.4    Perkins, A.S.5    Michalak, M.6
  • 61
    • 0029090829 scopus 로고
    • Myogenic and morphogenetic defects in the heart tubes of murine embryos lacking the homeobox gene Nkx2-Nkx5
    • Lyons, I., Parsons, L. M., Hartley, L., Li, R., Andrews, J. E., Robb, L. and Harvey, R. P. (1995) Myogenic and morphogenetic defects in the heart tubes of murine embryos lacking the homeobox gene Nkx2-Nkx5. Genes Dev. 9, 1654-1666
    • (1995) Genes Dev , vol.9 , pp. 1654-1666
    • Lyons, I.1    Parsons, L.M.2    Hartley, L.3    Li, R.4    Andrews, J.E.5    Robb, L.6    Harvey, R.P.7
  • 62
    • 47549114853 scopus 로고    scopus 로고
    • Calreticulin modulates commitment to adipocyte differentiation
    • Szabo, E., Qiu, Y., Baksh, S., Michalak, M. and Opas, M. (2008) Calreticulin modulates commitment to adipocyte differentiation. J. Cell Biol. 182, 103-116
    • (2008) J. Cell Biol , vol.182 , pp. 103-116
    • Szabo, E.1    Qiu, Y.2    Baksh, S.3    Michalak, M.4    Opas, M.5
  • 63
    • 0345327702 scopus 로고    scopus 로고
    • Presence of the inositol 1,4,5-triphosphate receptor isoforms in the nucleoplasm
    • Huh, Y. H. and Yoo, S. H. (2003) Presence of the inositol 1,4,5-triphosphate receptor isoforms in the nucleoplasm. FEBS Lett. 555, 411-418
    • (2003) FEBS Lett , vol.555 , pp. 411-418
    • Huh, Y.H.1    Yoo, S.H.2
  • 64
    • 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
  • 65
    • 0026782109 scopus 로고
    • Calreticulin in T-lymphocytes: Identification of calreticulin in T-lymphocytes and demonstration that activation of T cells correlates with increased levels of calreticulin mRNA and protein
    • Burns, K., Helgason, C. D., Bleackley, R. C. and Michalak, M. (1992) Calreticulin in T-lymphocytes: identification of calreticulin in T-lymphocytes and demonstration that activation of T cells correlates with increased levels of calreticulin mRNA and protein. J. Biol. Chem. 267, 19039-19042
    • (1992) J. Biol. Chem , vol.267 , pp. 19039-19042
    • Burns, K.1    Helgason, C.D.2    Bleackley, R.C.3    Michalak, M.4
  • 67
    • 26444571807 scopus 로고    scopus 로고
    • Regulation of protein compartmentalization expands the diversity of protein function
    • Shaffer, K. L., Sharma, A., Snapp, E. L. and Hegde, R. S. (2005) Regulation of protein compartmentalization expands the diversity of protein function. Dev. Cell 9, 545-554
    • (2005) Dev. Cell , vol.9 , pp. 545-554
    • Shaffer, K.L.1    Sharma, A.2    Snapp, E.L.3    Hegde, R.S.4
  • 68
    • 26444575860 scopus 로고    scopus 로고
    • Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol
    • Afshar, N., Black, B. E. and Paschal, B. M. (2005) Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol. Mol. Cell. Biol. 25, 8844-8853
    • (2005) Mol. Cell. Biol , vol.25 , pp. 8844-8853
    • Afshar, N.1    Black, B.E.2    Paschal, B.M.3
  • 69
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause, K.-H. and Michalak, M. (1997) Calreticulin. Cell 88, 439-443
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.-H.1    Michalak, M.2
  • 74
    • 33748489532 scopus 로고    scopus 로고
    • Dendritic cell surface calreticulin is a receptor for NY-ESO-1: Direct interactions between tumor-associated antigen and the innate immune system
    • Zeng, G., Aldridge, M. E., Tian, X., Seiler, D., Zhang, X., Jin, Y., Rao, J., Li, W., Chen, D., Langford, M. P. et al. (2006) Dendritic cell surface calreticulin is a receptor for NY-ESO-1: direct interactions between tumor-associated antigen and the innate immune system. J. Immunol. 177, 3582-3589
    • (2006) J. Immunol , vol.177 , pp. 3582-3589
    • Zeng, G.1    Aldridge, M.E.2    Tian, X.3    Seiler, D.4    Zhang, X.5    Jin, Y.6    Rao, J.7    Li, W.8    Chen, D.9    Langford, M.P.10
  • 75
    • 0037020093 scopus 로고    scopus 로고
    • The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin
    • Goicoechea, S., Pallero, M. A., Eggleton, P., Michalak, M. and Murphy-Ullrich, J. E. (2002) The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin. J. Biol. Chem. 277, 37219-37228
    • (2002) J. Biol. Chem , vol.277 , pp. 37219-37228
    • Goicoechea, S.1    Pallero, M.A.2    Eggleton, P.3    Michalak, M.4    Murphy-Ullrich, J.E.5
  • 77
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden, C. A., deCathelineau, A., Hoffmann, P. R., Bratton, D., Ghebrehiwet, B., Fadok, V. A. and Henson, P. M. (2001) C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med. 194, 781-795
    • (2001) J. Exp. Med , vol.194 , pp. 781-795
    • Ogden, C.A.1    deCathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 79
    • 0036748173 scopus 로고    scopus 로고
    • gC1q-R/p33: Structure-function predictions from the crystal structure
    • Ghebrehiwet, B., Jesty, J. and Peerschke, E. I. (2002) gC1q-R/p33: structure-function predictions from the crystal structure. Immunobiology 205, 421-432
    • (2002) Immunobiology , vol.205 , pp. 421-432
    • Ghebrehiwet, B.1    Jesty, J.2    Peerschke, E.I.3
  • 80
    • 33646477412 scopus 로고    scopus 로고
    • Impaired recognition of apoptotic neutrophils by the C1q/calreticulin and CD91 pathway in systemic lupus erythematosus
    • Donnelly, S., Roake, W., Brown, S., Young, P., Naik, H., Wordsworth, P., Isenberg, D. A., Reid, K. B. and Eggleton, P. (2006) Impaired recognition of apoptotic neutrophils by the C1q/calreticulin and CD91 pathway in systemic lupus erythematosus. Arthritis Rheum. 54, 1543-1556
    • (2006) Arthritis Rheum , vol.54 , pp. 1543-1556
    • Donnelly, S.1    Roake, W.2    Brown, S.3    Young, P.4    Naik, H.5    Wordsworth, P.6    Isenberg, D.A.7    Reid, K.B.8    Eggleton, P.9
  • 81
    • 66949178483 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted
  • 84
    • 0037477628 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly
    • Orr, A. W., Pedraza, C. E., Pallero, M. A., Elzie, C. A., Goicoechea, S., Strickland, D. K. and Murphy-Ullrich, J. E. (2003) Low density lipoprotein receptor-related protein is a calreticulin coreceptor that signals focal adhesion disassembly. J. Cell Biol. 161, 1179-1189
    • (2003) J. Cell Biol , vol.161 , pp. 1179-1189
    • Orr, A.W.1    Pedraza, C.E.2    Pallero, M.A.3    Elzie, C.A.4    Goicoechea, S.5    Strickland, D.K.6    Murphy-Ullrich, J.E.7
  • 85
    • 0042170209 scopus 로고    scopus 로고
    • Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration
    • Orr, A. W., Elzie, C. A., Kucik, D. F. and Murphy-Ullrich, J. E. (2003) Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration. J. Cell Sci. 116, 2917-2927
    • (2003) J. Cell Sci , vol.116 , pp. 2917-2927
    • Orr, A.W.1    Elzie, C.A.2    Kucik, D.F.3    Murphy-Ullrich, J.E.4
  • 87
    • 0036796111 scopus 로고    scopus 로고
    • Physical and functional interaction between cell-surface calreticulin and the collagen receptors integrin α2β1 and glycoprotein VI in human platelets
    • Elton, C. M., Smethurst, P. A., Eggleton, P. and Farndale, R. W. (2002) Physical and functional interaction between cell-surface calreticulin and the collagen receptors integrin α2β1 and glycoprotein VI in human platelets. Thromb. Haemostasis 88, 648-654
    • (2002) Thromb. Haemostasis , vol.88 , pp. 648-654
    • Elton, C.M.1    Smethurst, P.A.2    Eggleton, P.3    Farndale, R.W.4
  • 88
    • 33645721361 scopus 로고    scopus 로고
    • Maturation of human neutrophil phagosomes includes incorporation of molecular chaperones and endoplasmic reticulum quality control machinery
    • Burlak, C., Whitney, A. R., Mead, D. J., Hackstadt, T. and Deleo, F. R. (2006) Maturation of human neutrophil phagosomes includes incorporation of molecular chaperones and endoplasmic reticulum quality control machinery. Mol. Cell. Proteomics 5, 620-634
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 620-634
    • Burlak, C.1    Whitney, A.R.2    Mead, D.J.3    Hackstadt, T.4    Deleo, F.R.5
  • 89
    • 2342513408 scopus 로고    scopus 로고
    • Calreticulin on the mouse egg surface mediates transmembrane signaling linked to cell cycle resumption
    • Tutuncu, L., Stein, P., Ord, T. S., Jorgez, C. J. and Williams, C. J. (2004) Calreticulin on the mouse egg surface mediates transmembrane signaling linked to cell cycle resumption. Dev. Biol. 270, 246-260
    • (2004) Dev. Biol , vol.270 , pp. 246-260
    • Tutuncu, L.1    Stein, P.2    Ord, T.S.3    Jorgez, C.J.4    Williams, C.J.5
  • 90
    • 0038146923 scopus 로고    scopus 로고
    • Calreticulin: An endoplasmic reticulum protein with calcium-binding activity is also found in the extracellular matrix
    • Somogyi, E., Petersson, U., Hultenby, K. and Wendel, M. (2003) Calreticulin: an endoplasmic reticulum protein with calcium-binding activity is also found in the extracellular matrix. Matrix Biol. 22, 179-191
    • (2003) Matrix Biol , vol.22 , pp. 179-191
    • Somogyi, E.1    Petersson, U.2    Hultenby, K.3    Wendel, M.4
  • 91
    • 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 α 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 α 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
  • 92
    • 0001634869 scopus 로고    scopus 로고
    • Calreticulin couples calcium release and calcium influx in integrin-mediated calcium signaling
    • Kwon, M. S., Park, C. S., Choi, K., Ahnn, J., Kim, J. I., Eom, S. H., Kaufman, S. J. and Song, W. K. (2000) Calreticulin couples calcium release and calcium influx in integrin-mediated calcium signaling, Mol. Biol. Cell 11, 1433-1443
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1433-1443
    • Kwon, M.S.1    Park, C.S.2    Choi, K.3    Ahnn, J.4    Kim, J.I.5    Eom, S.H.6    Kaufman, S.J.7    Song, W.K.8
  • 95
    • 0034652696 scopus 로고    scopus 로고
    • Nuclear matrix of calreticulin in hepatocellular carcinoma
    • Yoon, G. S., Lee, H., Jung, Y., Yu, E., Moon, H. B., Song, K. and Lee, I. (2000) Nuclear matrix of calreticulin in hepatocellular carcinoma. Cancer Res. 60, 1117-1120
    • (2000) Cancer Res , vol.60 , pp. 1117-1120
    • Yoon, G.S.1    Lee, H.2    Jung, Y.3    Yu, E.4    Moon, H.B.5    Song, K.6    Lee, I.7
  • 96
    • 0033582436 scopus 로고    scopus 로고
    • Calreticulin enhances the transcriptional activity of thyroid transcription factor-1 by binding to its homeodomain
    • Perrone, L., Tell, G. and Di Lauro, R. (1999) Calreticulin enhances the transcriptional activity of thyroid transcription factor-1 by binding to its homeodomain. J. Biol. Chem. 274, 4640-4645
    • (1999) J. Biol. Chem , vol.274 , pp. 4640-4645
    • Perrone, L.1    Tell, G.2    Di Lauro, R.3
  • 98
    • 0030611105 scopus 로고    scopus 로고
    • The systemic lupus erythematosus (SLE) disease autoantigen-calreticulin can inhibit C1q association with immune complexes
    • Kishore, U., Sontheimer, R. D., Sastry, K. N., Zappi, E. G., Hughes, G. R., Khamashta, M. A. and Eggleton, P. (1997) The systemic lupus erythematosus (SLE) disease autoantigen-calreticulin can inhibit C1q association with immune complexes. Clin. Exp. Immunol. 108, 181-190
    • (1997) Clin. Exp. Immunol , vol.108 , pp. 181-190
    • Kishore, U.1    Sontheimer, R.D.2    Sastry, K.N.3    Zappi, E.G.4    Hughes, G.R.5    Khamashta, M.A.6    Eggleton, P.7
  • 99
    • 0026075634 scopus 로고
    • Molecular characterization of the Ro/SS-A autoimmune response
    • Sontheimer, R. D., Lieu, T. S. and McCauliffe, D. P. (1991) Molecular characterization of the Ro/SS-A autoimmune response. Semin. Dermatol. 10, 199-205
    • (1991) Semin. Dermatol , vol.10 , pp. 199-205
    • Sontheimer, R.D.1    Lieu, T.S.2    McCauliffe, D.P.3
  • 101
    • 38049048232 scopus 로고    scopus 로고
    • Autoantibodies in celiac disease
    • Alaedini, A. and Green, P. H. (2008) Autoantibodies in celiac disease. Autoimmunity 41, 19-26
    • (2008) Autoimmunity , vol.41 , pp. 19-26
    • Alaedini, A.1    Green, P.H.2
  • 105
    • 15044359599 scopus 로고    scopus 로고
    • Does Trypanosoma cruzi calreticulin modulate the complement system and angiogenesis?
    • Ferreira, V., Molina, M. C., Schwaeble, W., Lemus, D. and Ferreira, A. (2005) Does Trypanosoma cruzi calreticulin modulate the complement system and angiogenesis? Trends Parasitol. 21, 169-174
    • (2005) Trends Parasitol , vol.21 , pp. 169-174
    • Ferreira, V.1    Molina, M.C.2    Schwaeble, W.3    Lemus, D.4    Ferreira, A.5
  • 106
    • 0032977771 scopus 로고    scopus 로고
    • Pathophysiological roles of calreticulin in autoimmune disease
    • Eggleton, P. and Llewellyn, D. H. (1999) Pathophysiological roles of calreticulin in autoimmune disease. Scand. J. Immunol. 49, 466-473
    • (1999) Scand. J. Immunol , vol.49 , pp. 466-473
    • Eggleton, P.1    Llewellyn, D.H.2
  • 107
    • 17144427307 scopus 로고    scopus 로고
    • Anti-Ro/SSA and La/SSB antibodies
    • Franceschini, F. and Cavazzana, I. (2005) Anti-Ro/SSA and La/SSB antibodies. Autoimmunity 38, 55-63
    • (2005) Autoimmunity , vol.38 , pp. 55-63
    • Franceschini, F.1    Cavazzana, I.2
  • 111
    • 30444440869 scopus 로고    scopus 로고
    • Immune function of C1q and its modulators CD91 and CD93
    • Tarr, J. and Eggleton, P. (2005) Immune function of C1q and its modulators CD91 and CD93. Crit. Rev. Immunol. 25, 305-330
    • (2005) Crit. Rev. Immunol , vol.25 , pp. 305-330
    • Tarr, J.1    Eggleton, P.2
  • 112
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden, C. A., deCathelineau, A., Hoffmann, P. R., Bratton, D., Ghebrehiwet, B., Fadok, V. A. and Henson, P. M. (2001) C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med. 194, 781-795
    • (2001) J. Exp. Med , vol.194 , pp. 781-795
    • Ogden, C.A.1    deCathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 113
    • 33646477412 scopus 로고    scopus 로고
    • Impaired recognition of apoptotic neutrophils by the C1q/calreticulin and CD91 pathway in systemic lupus erythematosus
    • Donnelly, S., Roake, W., Brown, S., Young, P., Naik, H., Wordsworth, P., Isenberg, D. A., Reid, K. B. and Eggleton, P. (2006) Impaired recognition of apoptotic neutrophils by the C1q/calreticulin and CD91 pathway in systemic lupus erythematosus. Arthritis Rheum. 54, 1543-1556
    • (2006) Arthritis Rheum , vol.54 , pp. 1543-1556
    • Donnelly, S.1    Roake, W.2    Brown, S.3    Young, P.4    Naik, H.5    Wordsworth, P.6    Isenberg, D.A.7    Reid, K.B.8    Eggleton, P.9
  • 115
    • 0034788572 scopus 로고    scopus 로고
    • Tumor-specific immunity and antiangiogenesis generated by a DNA vaccine encoding calreticulin linked to a tumor antigen
    • Cheng, W. F., Hung, C. F., Chai, C. Y., Hsu, K. F., He, L., Ling, M. and Wu, T. C. (2001) Tumor-specific immunity and antiangiogenesis generated by a DNA vaccine encoding calreticulin linked to a tumor antigen. J. Clin. Invest. 108, 669-678
    • (2001) J. Clin. Invest , vol.108 , pp. 669-678
    • Cheng, W.F.1    Hung, C.F.2    Chai, C.Y.3    Hsu, K.F.4    He, L.5    Ling, M.6    Wu, T.C.7
  • 116
    • 18944376330 scopus 로고    scopus 로고
    • Characterization of DNA vaccines encoding the domains of calreticulin for their ability to elicit tumor-specific immunity and antiangiogenesis
    • Cheng, W. F., Hung, C. F., Chen, C. A., Lee, C. N., Su, Y. N., Chai, C. Y., Boyd, D. A., Hsieh, C. Y. and Wu, T. C. (2005) Characterization of DNA vaccines encoding the domains of calreticulin for their ability to elicit tumor-specific immunity and antiangiogenesis. Vaccine 23, 3864-3874
    • (2005) Vaccine , vol.23 , pp. 3864-3874
    • Cheng, W.F.1    Hung, C.F.2    Chen, C.A.3    Lee, C.N.4    Su, Y.N.5    Chai, C.Y.6    Boyd, D.A.7    Hsieh, C.Y.8    Wu, T.C.9
  • 117
    • 42949170542 scopus 로고    scopus 로고
    • Enhancement of antibody responses to Bacillus anthracis protective antigen domain IV by use of calreticulin as a chimeric molecular adjuvant
    • Park, Y. S., Lee, J. H., Hung, C. F., Wu, T. C. and Kim, T. W. (2008) Enhancement of antibody responses to Bacillus anthracis protective antigen domain IV by use of calreticulin as a chimeric molecular adjuvant. Infect. Immun. 76, 1952-1959
    • (2008) Infect. Immun , vol.76 , pp. 1952-1959
    • Park, Y.S.1    Lee, J.H.2    Hung, C.F.3    Wu, T.C.4    Kim, T.W.5
  • 118
    • 14844352487 scopus 로고    scopus 로고
    • Impaired cytolytic activity in calreticulin-deficient CTLs
    • Sipione, S., Ewen, C., Shostak, I., Michalak, M. and Bleackley, R. C. (2005) Impaired cytolytic activity in calreticulin-deficient CTLs. J. Immunol. 174, 3212-3219
    • (2005) J. Immunol , vol.174 , pp. 3212-3219
    • Sipione, S.1    Ewen, C.2    Shostak, I.3    Michalak, M.4    Bleackley, R.C.5
  • 119
    • 0027507325 scopus 로고
    • The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes
    • Dupuis, M., Schaerer, E., Krause, K.-H. and Tschopp, J. (1993) The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes. J. Exp. Med. 177, 1-7
    • (1993) J. Exp. Med , vol.177 , pp. 1-7
    • Dupuis, M.1    Schaerer, E.2    Krause, K.-H.3    Tschopp, J.4
  • 125
    • 84984552535 scopus 로고    scopus 로고
    • Enhancement of vaccinia vaccine potency by linkage of tumor antigen gene to gene encoding calreticulin
    • Hsieh, C. J., Kim, T. W., Hung, C. F., Juang, J., Moniz, M., Boyd, D. A., He, L., Chen, P. J., Chen, C. H. and Wu, T. C. (2004) Enhancement of vaccinia vaccine potency by linkage of tumor antigen gene to gene encoding calreticulin. Vaccine 22, 3993-4001
    • (2004) Vaccine , vol.22 , pp. 3993-4001
    • Hsieh, C.J.1    Kim, T.W.2    Hung, C.F.3    Juang, J.4    Moniz, M.5    Boyd, D.A.6    He, L.7    Chen, P.J.8    Chen, C.H.9    Wu, T.C.10
  • 126
    • 33747280364 scopus 로고    scopus 로고
    • Sindbis virus replicon particles encoding calreticulin linked to a tumor antigen generate long-term tumor-specific immunity
    • Cheng, W. F., Lee, C. N., Su, Y. N., Chai, C. Y., Chang, M. C., Polo, J. M., Hung, C. F., Wu, T. C., Hsieh, C. Y. and Chen, C. A. (2006) Sindbis virus replicon particles encoding calreticulin linked to a tumor antigen generate long-term tumor-specific immunity. Cancer Gene Ther. 13, 873-885
    • (2006) Cancer Gene Ther , vol.13 , pp. 873-885
    • Cheng, W.F.1    Lee, C.N.2    Su, Y.N.3    Chai, C.Y.4    Chang, M.C.5    Polo, J.M.6    Hung, C.F.7    Wu, T.C.8    Hsieh, C.Y.9    Chen, C.A.10
  • 128
    • 42549144606 scopus 로고    scopus 로고
    • Bcl-2 protein family members: Versatile regulators of calcium signaling in cell survival and apoptosis
    • Rong, Y. and Distelhorst, C. W. (2008) Bcl-2 protein family members: versatile regulators of calcium signaling in cell survival and apoptosis. Annu. Rev. Physiol. 70, 73-91
    • (2008) Annu. Rev. Physiol , vol.70 , pp. 73-91
    • Rong, Y.1    Distelhorst, C.W.2
  • 129
    • 45449093954 scopus 로고    scopus 로고
    • Calcium signaling in lymphocytes
    • Oh-Hora, M. and Rao, A. (2008) Calcium signaling in lymphocytes. Curr. Opin. Immunol. 20, 250-258
    • (2008) Curr. Opin. Immunol , vol.20 , pp. 250-258
    • Oh-Hora, M.1    Rao, A.2
  • 131
    • 46149094254 scopus 로고    scopus 로고
    • Enhanced calreticulin expression promotes calcium-dependent apoptosis in postnatal cardiomyocytes
    • Lim, S., Chang, W., Lee, B. K., Song, H., Hong, J. H., Lee, S., Song, B. W., Kim, H. J., Cha, M. J., Jang, Y. et al. (2008) Enhanced calreticulin expression promotes calcium-dependent apoptosis in postnatal cardiomyocytes. Mol. Cells 25, 390-396
    • (2008) Mol. Cells , vol.25 , pp. 390-396
    • Lim, S.1    Chang, W.2    Lee, B.K.3    Song, H.4    Hong, J.H.5    Lee, S.6    Song, B.W.7    Kim, H.J.8    Cha, M.J.9    Jang, Y.10
  • 133
    • 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) EMBO J , vol.20 , pp. 2690-2701
    • Pinton, P.1    Ferrari, D.2    Rapizzi, E.3    Di Virgilio, F.4    Pozzan, T.5    Rizzuto, R.6
  • 134
    • 0034680794 scopus 로고    scopus 로고
    • Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin
    • Goicoechea, S., Orr, A. W., Pallero, M. A., Eggleton, P. and Murphy-Ullrich, J. E. (2000) Thrombospondin mediates focal adhesion disassembly through interactions with cell surface calreticulin. J. Biol. Chem. 275, 36358-36368
    • (2000) J. Biol. Chem , vol.275 , pp. 36358-36368
    • Goicoechea, S.1    Orr, A.W.2    Pallero, M.A.3    Eggleton, P.4    Murphy-Ullrich, J.E.5
  • 135
    • 55549142180 scopus 로고    scopus 로고
    • Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis
    • Pallero, M. A., Elzie, C. A., Chen, J., Mosher, D. F. and Murphy-Ullrich, J. E. (2008) Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis. FASEB J. 22, 3968-3979
    • (2008) FASEB J , vol.22 , pp. 3968-3979
    • Pallero, M.A.1    Elzie, C.A.2    Chen, J.3    Mosher, D.F.4    Murphy-Ullrich, J.E.5
  • 136
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPα or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai, S. J., Xiao, Y. Q., Dickinson, M., Nick, J. A., Voelker, D. R., Greene, K. E. and Henson, P. M. (2003) By binding SIRPα or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell 115, 13-23
    • (2003) Cell , vol.115 , pp. 13-23
    • Gardai, S.J.1    Xiao, Y.Q.2    Dickinson, M.3    Nick, J.A.4    Voelker, D.R.5    Greene, K.E.6    Henson, P.M.7
  • 140
    • 34548293624 scopus 로고    scopus 로고
    • Inhibition of angiogenesis by a novel small peptide consisting of the active fragments of platelet factor-4 and vasostatin
    • Li, X., Jiang, L., Wang, Y., Xiao, Y., Huang, Y., Yao, Q., Yang, Y. and Wu, X. (2007) Inhibition of angiogenesis by a novel small peptide consisting of the active fragments of platelet factor-4 and vasostatin. Cancer Lett. 256, 29-32
    • (2007) Cancer Lett , vol.256 , pp. 29-32
    • Li, X.1    Jiang, L.2    Wang, Y.3    Xiao, Y.4    Huang, Y.5    Yao, Q.6    Yang, Y.7    Wu, X.8
  • 141
    • 0036144369 scopus 로고    scopus 로고
    • Laminin binding to the calreticulin fragment vasostatin regulates endothelial cell function
    • Yao, L., Pike, S. E. and Tosato, G. (2002) Laminin binding to the calreticulin fragment vasostatin regulates endothelial cell function. J. Leukocyte Biol. 71, 47-53
    • (2002) J. Leukocyte Biol , vol.71 , pp. 47-53
    • Yao, L.1    Pike, S.E.2    Tosato, G.3
  • 143
    • 33645235802 scopus 로고    scopus 로고
    • Combination of vasostatin gene therapy with cyclophosphamide inhibits growth of B16(F10) melanoma tumours
    • Jazowiecka-Rakus, J., Jarosz, M. and Szala, S. (2006) Combination of vasostatin gene therapy with cyclophosphamide inhibits growth of B16(F10) melanoma tumours. Acta Biochim. Pol. 53, 199-202
    • (2006) Acta Biochim. Pol , vol.53 , pp. 199-202
    • Jazowiecka-Rakus, J.1    Jarosz, M.2    Szala, S.3
  • 144
    • 33847288085 scopus 로고    scopus 로고
    • Complete eradication of hepatocellular carcinomas by combined vasostatin gene therapy and B7H3-mediated immunotherapy
    • Ma, L., Luo, L., Qiao, H., Dong, X., Pan, S., Jiang, H., Krissansen, G. W. and Sun, X. (2007) Complete eradication of hepatocellular carcinomas by combined vasostatin gene therapy and B7H3-mediated immunotherapy. J. Hepatol. 46, 98-106
    • (2007) J. Hepatol , vol.46 , pp. 98-106
    • Ma, L.1    Luo, L.2    Qiao, H.3    Dong, X.4    Pan, S.5    Jiang, H.6    Krissansen, G.W.7    Sun, X.8
  • 145
    • 39049165759 scopus 로고    scopus 로고
    • Suppression of lung tumor growth and metastasis in mice by adeno-associated virus-mediated expression of vasostatin
    • Cai, K. X., Tse, L. Y., Leung, C., Tam, P. K., Xu, R. and Sham, M. H. (2008) Suppression of lung tumor growth and metastasis in mice by adeno-associated virus-mediated expression of vasostatin. Clin. Cancer Res. 14, 939-949
    • (2008) Clin. Cancer Res , vol.14 , pp. 939-949
    • Cai, K.X.1    Tse, L.Y.2    Leung, C.3    Tam, P.K.4    Xu, R.5    Sham, M.H.6
  • 146
    • 31444448592 scopus 로고    scopus 로고
    • Gene transfer of vasostatin, a calreticulin fragment, into neuroendocrine tumor cells results in enhanced malignant behavior
    • Liu, M., Imam, H., Oberg, K. and Zhou, Y. (2005) Gene transfer of vasostatin, a calreticulin fragment, into neuroendocrine tumor cells results in enhanced malignant behavior. Neuroendocrinology 82, 1-10
    • (2005) Neuroendocrinology , vol.82 , pp. 1-10
    • Liu, M.1    Imam, H.2    Oberg, K.3    Zhou, Y.4
  • 148
    • 34848870970 scopus 로고    scopus 로고
    • db/db mice exhibit severe wound-healing impairments compared with other murine diabetic strains in a silicone-splinted excisional wound model
    • Michaels, J., Churgin, S. S., Blechman, K. M., Greives, M. R., Aarabi, S., Galiano, R. D. and Gurtner, G. C. (2007) db/db mice exhibit severe wound-healing impairments compared with other murine diabetic strains in a silicone-splinted excisional wound model. Wound Repair Regen. 15, 665-670
    • (2007) Wound Repair Regen , vol.15 , pp. 665-670
    • Michaels, J.1    Churgin, S.S.2    Blechman, K.M.3    Greives, M.R.4    Aarabi, S.5    Galiano, R.D.6    Gurtner, G.C.7
  • 149
  • 150
    • 1442277113 scopus 로고    scopus 로고
    • Calreticulin-independent regulation of the platelet integrin αIIbβ3 by the KVGFFKR αIIb-cytoplasmic motif
    • Reilly, D., Larkin, D., Devocelle, M., Fitzgerald, D. J. and Moran, N. (2004) Calreticulin-independent regulation of the platelet integrin αIIbβ3 by the KVGFFKR αIIb-cytoplasmic motif. Platelets 15, 43-54
    • (2004) Platelets , vol.15 , pp. 43-54
    • Reilly, D.1    Larkin, D.2    Devocelle, M.3    Fitzgerald, D.J.4    Moran, N.5
  • 151
    • 15044360781 scopus 로고    scopus 로고
    • The intermediate filament protein vimentin binds specifically to a recombinant integrin α2/β1 cytoplasmic tail complex and co-localizes with native α2/β1 in endothelial cell focal adhesions
    • Kreis, S., Schonfeld, H. J., Melchior, C., Steiner, B. and Kieffer, N. (2005) The intermediate filament protein vimentin binds specifically to
    • (2005) Exp. Cell Res , vol.305 , pp. 110-121
    • Kreis, S.1    Schonfeld, H.J.2    Melchior, C.3    Steiner, B.4    Kieffer, N.5
  • 152
    • 33749147653 scopus 로고    scopus 로고
    • Transforming growth factor-β3 affects plasminogen activator inhibitor-1 expression in fetal mice and modulates fibroblast-mediated collagen gel contraction
    • Li, W. Y., Huang, E. Y., Dudas, M., Kaartinen, V., Warburton, D. and Tuan, T. L. (2006) Transforming growth factor-β3 affects plasminogen activator inhibitor-1 expression in fetal mice and modulates fibroblast-mediated collagen gel contraction. Wound Repair Regen. 14, 516-525
    • (2006) Wound Repair Regen , vol.14 , pp. 516-525
    • Li, W.Y.1    Huang, E.Y.2    Dudas, M.3    Kaartinen, V.4    Warburton, D.5    Tuan, T.L.6
  • 153
    • 0030788353 scopus 로고    scopus 로고
    • Transforming growth factor β3 (TGFβ3) accelerates wound healing without alteration of scar prominence: Histologic and competitive reverse-transcription-polymerase chain reaction studies
    • Wu, L., Siddiqui, A., Morris, D. E., Cox, D. A., Roth, S. I. and Mustoe, T. A. (1997) Transforming growth factor β3 (TGFβ3) accelerates wound healing without alteration of scar prominence: histologic and competitive reverse-transcription-polymerase chain reaction studies. Arch. Surg. 132, 753-760
    • (1997) Arch. Surg , vol.132 , pp. 753-760
    • Wu, L.1    Siddiqui, A.2    Morris, D.E.3    Cox, D.A.4    Roth, S.I.5    Mustoe, T.A.6
  • 154
    • 33646249166 scopus 로고    scopus 로고
    • A novel 'sandwich' assay for quantifying chemo-regulated cell migration within 3-dimensional matrices: Wound healing cytokines exhibit distinct motogenic activities compared to the transmembrane assay
    • Schor, S. L., Ellis, I. R., Harada, K., Motegi, K., Anderson, A. R., Chaplain, M. A., Keatch, R. P. and Schor, A. M. (2006) A novel 'sandwich' assay for quantifying chemo-regulated cell migration within 3-dimensional matrices: wound healing cytokines exhibit distinct motogenic activities compared to the transmembrane assay. Cell Motil. Cytoskeleton 63, 287-300
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 287-300
    • Schor, S.L.1    Ellis, I.R.2    Harada, K.3    Motegi, K.4    Anderson, A.R.5    Chaplain, M.A.6    Keatch, R.P.7    Schor, A.M.8
  • 155
    • 34447283329 scopus 로고    scopus 로고
    • Dissecting focal adhesions in cells differentially expressing calreticulin: A microscopy study
    • Papp, S., Fadel, M. P. and Opas, M. (2007) Dissecting focal adhesions in cells differentially expressing calreticulin: a microscopy study. Biol. Cell 99, 389-402
    • (2007) Biol. Cell , vol.99 , pp. 389-402
    • Papp, S.1    Fadel, M.P.2    Opas, M.3
  • 156
    • 34447550245 scopus 로고    scopus 로고
    • Calreticulin affects fibronectin-based cell-substratum adhesion via the regulation of c-Src activity
    • Papp, S., Fadel, M. P., Kim, H., McCulloch, C. A. and Opas, M. (2007) Calreticulin affects fibronectin-based cell-substratum adhesion via the regulation of c-Src activity. J. Biol. Chem.282, 16585-16598
    • (2007) J. Biol. Chem , vol.282 , pp. 16585-16598
    • Papp, S.1    Fadel, M.P.2    Kim, H.3    McCulloch, C.A.4    Opas, M.5
  • 157
    • 34447637646 scopus 로고    scopus 로고
    • Differential expression and activity of matrix metalloproteinase-2 and -9 in the calreticulin deficient cells
    • Wu, M., Massaeli, H., Durston, M. and Mesaeli, N. (2007) Differential expression and activity of matrix metalloproteinase-2 and -9 in the calreticulin deficient cells. Matrix Biol. 26, 463-472
    • (2007) Matrix Biol , vol.26 , pp. 463-472
    • Wu, M.1    Massaeli, H.2    Durston, M.3    Mesaeli, N.4
  • 159
    • 33947117494 scopus 로고    scopus 로고
    • Extracellular heat shock protein-90α: Linking hypoxia to skin cell motility and wound healing
    • Li, W., Li, Y., Guan, S., Fan, J., Cheng, C. F., Bright, A. M., Chinn, C., Chen, M. and Woodley, D. T. (2007) Extracellular heat shock protein-90α: linking hypoxia to skin cell motility and wound healing. EMBO J. 26, 1221-1233
    • (2007) EMBO J , vol.26 , pp. 1221-1233
    • Li, W.1    Li, Y.2    Guan, S.3    Fan, J.4    Cheng, C.F.5    Bright, A.M.6    Chinn, C.7    Chen, M.8    Woodley, D.T.9
  • 160
    • 34548189523 scopus 로고    scopus 로고
    • Extracellular heat shock protein 90: A role for a molecular chaperone in cell motility and cancer metastasis
    • Tsutsumi, S. and Neckers, L. (2007) Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis. Cancer Sci. 98, 1536-1539
    • (2007) Cancer Sci , vol.98 , pp. 1536-1539
    • Tsutsumi, S.1    Neckers, L.2
  • 161
    • 33645711396 scopus 로고    scopus 로고
    • In vivo delivery of heat shock protein 70 accelerates wound healing by up-regulating macrophage-mediated phagocytosis
    • Kovalchin, J. T., Wang, R., Wagh, M. S., Azoulay, J., Sanders, M. and Chandawarkar, R. Y. (2006) In vivo delivery of heat shock protein 70 accelerates wound healing by up-regulating macrophage-mediated phagocytosis. Wound Repair Regen. 14, 129-137
    • (2006) Wound Repair Regen , vol.14 , pp. 129-137
    • Kovalchin, J.T.1    Wang, R.2    Wagh, M.S.3    Azoulay, J.4    Sanders, M.5    Chandawarkar, R.Y.6
  • 162
    • 35548998775 scopus 로고    scopus 로고
    • Chaperonopathies by defect, excess, or mistake
    • Macario, A. J. and De Macario, E. C. (2007) Chaperonopathies by defect, excess, or mistake. Ann. N.Y. Acad. Sci. 1113, 178-191
    • (2007) Ann. N.Y. Acad. Sci , vol.1113 , pp. 178-191
    • Macario, A.J.1    De Macario, E.C.2
  • 163
    • 43249113945 scopus 로고    scopus 로고
    • Transforming growth factor α (TGFα)-stimulated secretion of HSP90α: Using the receptor LRP-1/CD91 to promote human skin cell migration against a TGFβ-rich environment during wound healing
    • Cheng, C. F., Fan, J., Fedesco, M., Guan, S., Li, Y., Bandyopadhyay, B., Bright, A. M., Yerushalmi, D., Liang, M., Chen, M. et al. (2008) Transforming growth factor α (TGFα)-stimulated secretion of HSP90α: using the receptor LRP-1/CD91 to promote human skin cell migration against a TGFβ-rich environment during wound healing. Mol. Cell. Biol. 28, 3344-335
    • (2008) Mol. Cell. Biol , vol.28 , pp. 3344-4335
    • Cheng, C.F.1    Fan, J.2    Fedesco, M.3    Guan, S.4    Li, Y.5    Bandyopadhyay, B.6    Bright, A.M.7    Yerushalmi, D.8    Liang, M.9    Chen, M.10
  • 165
    • 33751426035 scopus 로고    scopus 로고
    • Ultrastructural analysis of development of myocardium in calreticulin-deficient mice
    • Lozyk, M. D., Papp, S., Zhang, X., Nakamura, K., Michalak, M. and Opas, M. (2006) Ultrastructural analysis of development of myocardium in calreticulin-deficient mice. BMC Dev. Biol. 6, 54
    • (2006) BMC Dev. Biol , vol.6 , pp. 54
    • Lozyk, M.D.1    Papp, S.2    Zhang, X.3    Nakamura, K.4    Michalak, M.5    Opas, M.6
  • 166
    • 0026500977 scopus 로고
    • The involvement of adherens junction components in myofibrillogenesis in cultured cardiac myocytes
    • Goncharova, E. J., Kam, Z. and Geiger, B. (1992) The involvement of adherens junction components in myofibrillogenesis in cultured cardiac myocytes. Development 114, 173-183
    • (1992) Development , vol.114 , pp. 173-183
    • Goncharova, E.J.1    Kam, Z.2    Geiger, B.3
  • 167
    • 0032190429 scopus 로고    scopus 로고
    • N-cadherin/catenin-mediated morphoregulation of somite formation
    • Linask, K. K., Ludwig, C., Han, M. D., Liu, X., Radice, G. L. and Knudsen, K. A. (1998) N-cadherin/catenin-mediated morphoregulation of somite formation. Dev. Biol. 202, 85-102
    • (1998) Dev. Biol , vol.202 , pp. 85-102
    • Linask, K.K.1    Ludwig, C.2    Han, M.D.3    Liu, X.4    Radice, G.L.5    Knudsen, K.A.6
  • 170
    • 34249079726 scopus 로고    scopus 로고
    • Partial reversal of transformed fusiform phenotype by overexpression of calreticulin
    • Opas, M. and Fadel, M. P. (2007) Partial reversal of transformed fusiform phenotype by overexpression of calreticulin. Cell. Mol. Biol. Lett. 12, 294-307
    • (2007) Cell. Mol. Biol. Lett , vol.12 , pp. 294-307
    • Opas, M.1    Fadel, M.P.2
  • 171
    • 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. (1996) 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
  • 172
    • 0033591411 scopus 로고    scopus 로고
    • Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion
    • Fadel, M. P., Dziak, E., Lo, C. M., Ferrier, J., Mesaeli, N., Michalak, M. and Opas, M. (1999) Calreticulin affects focal contact-dependent but not close contact-dependent cell-substratum adhesion. J. Biol. Chem. 274, 15085-15094
    • (1999) J. Biol. Chem , vol.274 , pp. 15085-15094
    • Fadel, M.P.1    Dziak, E.2    Lo, C.M.3    Ferrier, J.4    Mesaeli, N.5    Michalak, M.6    Opas, M.7
  • 174
    • 85056042454 scopus 로고    scopus 로고
    • Expression of endoplasmic reticulum chaperones in cardiac development. Open Cardiovasc
    • Papp, S., Zhang, X., Szabo, E. and Opas, M. (2008) Expression of endoplasmic reticulum chaperones in cardiac development. Open Cardiovasc. Med. J. 2, 31-35
    • (2008) Med. J , vol.2 , pp. 31-35
    • Papp, S.1    Zhang, X.2    Szabo, E.3    Opas, M.4
  • 177
    • 0029885782 scopus 로고    scopus 로고
    • Complete congenital heart block is associated with increased autoantibody titers against calreticulin
    • Orth, T., Dorner, T., Meyer Zum Buschenfelde, K. H. and Mayet, W. J. (1996) Complete congenital heart block is associated with increased autoantibody titers against calreticulin. Eur. J. Clin. Invest. 26, 205-215
    • (1996) Eur. J. Clin. Invest , vol.26 , pp. 205-215
    • Orth, T.1    Dorner, T.2    Meyer Zum Buschenfelde, K.H.3    Mayet, W.J.4
  • 178
    • 0035951849 scopus 로고    scopus 로고
    • Calcium, calcineurin, and the control of transcription
    • Crabtree, G. R. (2001) Calcium, calcineurin, and the control of transcription. J. Biol. Chem. 276, 2313-2316
    • (2001) J. Biol. Chem , vol.276 , pp. 2313-2316
    • Crabtree, G.R.1
  • 179
    • 0030911475 scopus 로고    scopus 로고
    • Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C
    • Lin, Q., Schwarz, J., Bucana, C. and Olson, E. N. (1997) Control of mouse cardiac morphogenesis and myogenesis by transcription factor MEF2C. Science 276, 1404-1407
    • (1997) Science , vol.276 , pp. 1404-1407
    • Lin, Q.1    Schwarz, J.2    Bucana, C.3    Olson, E.N.4
  • 180
    • 0029005816 scopus 로고
    • Calreticulin modulates the in vitro DNA binding but not the in vivo transcriptional activation by peroxisome proliferator-activated receptor/retinoid X receptor heterodimers
    • Winrow, C. J., Miyata, K. S., Marcus, S. L., Burns, K., Michalak, M. and Rachubinski, R. A. (1995) Calreticulin modulates the in vitro DNA binding but not the in vivo transcriptional activation by peroxisome proliferator-activated receptor/retinoid X receptor heterodimers. Mol. Cell. Endocrinol. 111, 175-179
    • (1995) Mol. Cell. Endocrinol , vol.111 , pp. 175-179
    • Winrow, C.J.1    Miyata, K.S.2    Marcus, S.L.3    Burns, K.4    Michalak, M.5    Rachubinski, R.A.6
  • 181
    • 0036787010 scopus 로고    scopus 로고
    • Calreticulin interacts with C/EBPα and C/EBPβ mRNAs and represses translation of C/EBP proteins
    • Timchenko, L. T., Iakova, P., Welm, A. L., Cai, Z. J. and Timchenko, N. A. (2002) Calreticulin interacts with C/EBPα and C/EBPβ mRNAs and represses translation of C/EBP proteins. Mol. Cell. Biol. 22, 7242-7257
    • (2002) Mol. Cell. Biol , vol.22 , pp. 7242-7257
    • Timchenko, L.T.1    Iakova, P.2    Welm, A.L.3    Cai, Z.J.4    Timchenko, N.A.5
  • 182
    • 8644234403 scopus 로고    scopus 로고
    • High extracellular calcium attenuates adipogenesis in 3T3-L1 preadipocytes
    • Jensen, B., Farach-Carson, M. C., Kenaley, E. and Akanbi, K. A. (2004) High extracellular calcium attenuates adipogenesis in 3T3-L1 preadipocytes. Exp. Cell Res. 301, 280-292
    • (2004) Exp. Cell Res , vol.301 , pp. 280-292
    • Jensen, B.1    Farach-Carson, M.C.2    Kenaley, E.3    Akanbi, K.A.4
  • 183
    • 0037147144 scopus 로고    scopus 로고
    • Calcineurin mediates the calcium-dependent inhibition of adipocyte differentiation in 3T3-L1 cells
    • Neal, J. W. and Clipstone, N. A. (2002) Calcineurin mediates the calcium-dependent inhibition of adipocyte differentiation in 3T3-L1 cells. J. Biol. Chem. 277, 49776-49781
    • (2002) J. Biol. Chem , vol.277 , pp. 49776-49781
    • Neal, J.W.1    Clipstone, N.A.2
  • 185
    • 21244481801 scopus 로고    scopus 로고
    • Wnt signaling inhibits adipogenesis through β-catenin-dependent and -independent mechanisms
    • Kennell, J. A. and MacDougald, O. A. (2005) Wnt signaling inhibits adipogenesis through β-catenin-dependent and -independent mechanisms. J. Biol. Chem. 280, 24004-24010
    • (2005) J. Biol. Chem , vol.280 , pp. 24004-24010
    • Kennell, J.A.1    MacDougald, O.A.2
  • 186
    • 0028800964 scopus 로고
    • Constitutive expression of calreticulin in osteoblasts inhibits mineralization
    • St-Arnaud, R., Prud'homme, J., Leung-Hagesteijn, C. and Dedhar, S. (1995) Constitutive expression of calreticulin in osteoblasts inhibits mineralization. J. Cell Biol. 131, 1351-1359
    • (1995) J. Cell Biol , vol.131 , pp. 1351-1359
    • St-Arnaud, R.1    Prud'homme, J.2    Leung-Hagesteijn, C.3    Dedhar, S.4
  • 187
    • 4644269515 scopus 로고    scopus 로고
    • FGF18 represses noggin expression and is induced by calcineurin
    • Reinhold, M. I., Abe, M., Kapadia, R. M., Liao, Z. and Naski, M. C. (2004) FGF18 represses noggin expression and is induced by calcineurin. J. Biol. Chem. 279, 38209-38219
    • (2004) J. Biol. Chem , vol.279 , pp. 38209-38219
    • Reinhold, M.I.1    Abe, M.2    Kapadia, R.M.3    Liao, Z.4    Naski, M.C.5
  • 189
    • 36049023510 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress during the embryonic development of the central nervous system in the mouse
    • Zhang, X., Szabo, E., Michalak, M. and Opas, M. (2007) Endoplasmic reticulum stress during the embryonic development of the central nervous system in the mouse. Int. J. Dev. Neurosci. 25, 455-463
    • (2007) Int. J. Dev. Neurosci , vol.25 , pp. 455-463
    • Zhang, X.1    Szabo, E.2    Michalak, M.3    Opas, M.4
  • 190
    • 0034630347 scopus 로고    scopus 로고
    • Heart, brain, and body wall defects in mice lacking calreticulin
    • Rauch, F., Prud'homme, J., Arabian, A., Dedhar, S. and St-Arnaud, R. (2000) Heart, brain, and body wall defects in mice lacking calreticulin. Exp. Cell Res. 256, 105-111
    • (2000) Exp. Cell Res , vol.256 , pp. 105-111
    • Rauch, F.1    Prud'homme, J.2    Arabian, A.3    Dedhar, S.4    St-Arnaud, R.5
  • 191
    • 0033065724 scopus 로고    scopus 로고
    • Bending of the neural plate during mouse spinal neurulation is independent of actin microfilaments
    • Ybot-Gonzalez, P. and Copp, A. J. (1999) Bending of the neural plate during mouse spinal neurulation is independent of actin microfilaments. Dev. Dyn. 215, 273-283
    • (1999) Dev. Dyn , vol.215 , pp. 273-283
    • Ybot-Gonzalez, P.1    Copp, A.J.2
  • 192
    • 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


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