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Volumn 267, Issue 7, 2000, Pages 1945-1957

Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells. Evidence for a unique role in secretory-protein synthesis

Author keywords

Enamel cells; Endoplasmic reticulum; ERp29; Reticuloplasmin

Indexed keywords

CELL PROTEIN; COMPLEMENTARY DNA;

EID: 0034108939     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01193.x     Document Type: Article
Times cited : (60)

References (60)
  • 1
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J. & Sambrook, J. (1992) Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 2
    • 0028283948 scopus 로고
    • Molecular and cellular physiology of intracellular calcium stores
    • Pozzan, T., Rizzuto, R., Volpe, P. & 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
  • 3
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasome-mediated protein degradation: How two topographically restricted events came together
    • Brodsky, J.L. & McCracken, A.A. (1997) ER-associated and proteasome-mediated protein degradation: how two topographically restricted events came together. Trends Cell Biol. 7, 151-156.
    • (1997) Trends Cell Biol. , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 4
    • 0025630758 scopus 로고
    • The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion
    • Dorner, A.J., Wasley, L.C., Raney, P., Haugejorden, S., Green, M. & Kaufman, R.J. (1990) The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion. J. Biol. Chem. 265, 22029-22034.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22029-22034
    • Dorner, A.J.1    Wasley, L.C.2    Raney, P.3    Haugejorden, S.4    Green, M.5    Kaufman, R.J.6
  • 5
    • 0028967755 scopus 로고
    • Transduction of calcium stress through interaction of the human transcription factor CBF with the proximal CCAAT regulatory element of the grp78/BiP promoter
    • Roy, B. & Lee, A.S. (1995) Transduction of calcium stress through interaction of the human transcription factor CBF with the proximal CCAAT regulatory element of the grp78/BiP promoter. Mol. Cell. Biol. 15, 2263-2274.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2263-2274
    • Roy, B.1    Lee, A.S.2
  • 6
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • Thomas, P.J., Qu, B.H. & Pedersen, P.L. (1995) Defective protein folding as a basis of human disease. Trends Biochem. Sci. 20, 456-459.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.H.2    Pedersen, P.L.3
  • 7
    • 0030918842 scopus 로고    scopus 로고
    • Protein processing. A role in the pathophysiology of genetic disease
    • Brooks, D.A. (1997) Protein processing. A role in the pathophysiology of genetic disease. FEBS Lett. 409, 115-120.
    • (1997) FEBS Lett. , vol.409 , pp. 115-120
    • Brooks, D.A.1
  • 9
    • 0032101239 scopus 로고    scopus 로고
    • The unfolded protein response: An intracellular signalling pathway with many surprising features
    • Sidrauski, C., Chapman, R. & Walter, P. (1998) The unfolded protein response: an intracellular signalling pathway with many surprising features. Trends Cell Biol. 8, 245-249.
    • (1998) Trends Cell Biol. , vol.8 , pp. 245-249
    • Sidrauski, C.1    Chapman, R.2    Walter, P.3
  • 11
    • 0025225456 scopus 로고
    • The retention signal for soluble proteins of the endoplasmic reticulum
    • Pelham, H.R.B. (1990) The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem. Sci. 15, 483-486.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 483-486
    • Pelham, H.R.B.1
  • 12
    • 0029781385 scopus 로고    scopus 로고
    • Purification and characterization of the human KDEL receptor
    • Scheel, A.A. & Pelham, H.R.B. (1996) Purification and characterization of the human KDEL receptor. Biochemistry 35, 10203-10209.
    • (1996) Biochemistry , vol.35 , pp. 10203-10209
    • Scheel, A.A.1    Pelham, H.R.B.2
  • 13
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman, R.B., Hirst, T.R. & Tuite, M.F. (1994) Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19, 331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 14
    • 0033028924 scopus 로고    scopus 로고
    • Identifying and characterizing a second structural domain of protein disulfide isomerase
    • Darby, N.J., van straten, M., Penka, E., Vincentelli, R. & Kemmink, J. (1999) Identifying and characterizing a second structural domain of protein disulfide isomerase. FEBS Lett. 448, 167-172.
    • (1999) FEBS Lett. , vol.448 , pp. 167-172
    • Darby, N.J.1    Van Straten, M.2    Penka, E.3    Vincentelli, R.4    Kemmink, J.5
  • 15
    • 0033545187 scopus 로고    scopus 로고
    • The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
    • Hellman, R., Vanhow, M., Lejeune, A., Stevens, F.J. & Hendershot, L.M. (1999) The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP. J. Cell Biol. 144, 21-30.
    • (1999) J. Cell Biol. , vol.144 , pp. 21-30
    • Hellman, R.1    Vanhow, M.2    Lejeune, A.3    Stevens, F.J.4    Hendershot, L.M.5
  • 16
    • 0023749218 scopus 로고
    • Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum
    • Macer, D.RJ. & Koch, G.L.E. (1988) Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum. J. Cell Sci. 91, 61-70.
    • (1988) J. Cell Sci. , vol.91 , pp. 61-70
    • Macer, D.R.J.1    Koch, G.L.E.2
  • 18
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi, T., Helakosik, T., Tasanen, K., Myllyla, R., Huhtala, M.L., Koivu, J. & Kivirikko, K.I. (1987) Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J. 6, 643-649.
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helakosik, T.2    Tasanen, K.3    Myllyla, R.4    Huhtala, M.L.5    Koivu, J.6    Kivirikko, K.I.7
  • 19
    • 0029058132 scopus 로고
    • Microsomal triglyceride transfer protein: A protein complex required for the assembly of lipoprotein particles
    • Gordon, D.A., Wetterau, J.R. & Gregg, R.E. (1995) Microsomal triglyceride transfer protein: a protein complex required for the assembly of lipoprotein particles. Trends Cell Biol. 5, 317-325.
    • (1995) Trends Cell Biol. , vol.5 , pp. 317-325
    • Gordon, D.A.1    Wetterau, J.R.2    Gregg, R.E.3
  • 20
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu, U. & Helenius, A. (1997) Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol. 136, 555-565.
    • (1997) J. Cell Biol. , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 21
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth, C. & Koch, G.L.E. (1989) Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 59, 729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.E.2
  • 23
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause, K.H. & Michalak, M. (1997) Calreticulin. Cell 88, 439-443.
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.H.1    Michalak, M.2
  • 25
    • 0000395667 scopus 로고
    • Stereological analysis of organelle distribution within rat incisor enamel organ at successive stages of amelogenesis
    • Smith, C.E. (1984) Stereological analysis of organelle distribution within rat incisor enamel organ at successive stages of amelogenesis. INSERM 125, 273-282.
    • (1984) INSERM , vol.125 , pp. 273-282
    • Smith, C.E.1
  • 26
    • 0029957742 scopus 로고    scopus 로고
    • Abundant calcium homeostasis machinery in rat dental enamel cells. Up-regulation of calcium store proteins during enamel hypermineralization implicates the endoplasmic reticulum in calcium transcytosis
    • Hubbard, M.J. (1996) Abundant calcium homeostasis machinery in rat dental enamel cells. Up-regulation of calcium store proteins during enamel hypermineralization implicates the endoplasmic reticulum in calcium transcytosis. Eur. J. Biochem. 239, 611-623.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 611-623
    • Hubbard, M.J.1
  • 27
    • 0031848228 scopus 로고    scopus 로고
    • Proteomic analysis of enamel cells from developing rat teeth. Big returns from a small tissue
    • Hubbard, M.J. (1998) Proteomic analysis of enamel cells from developing rat teeth. Big returns from a small tissue. Electrophoresis 19, 1891-1900.
    • (1998) Electrophoresis , vol.19 , pp. 1891-1900
    • Hubbard, M.J.1
  • 28
    • 0032457014 scopus 로고    scopus 로고
    • Enamel cell biology. Towards a comprehensive biochemical understanding
    • Hubbard, M.J. (1998) Enamel cell biology. Towards a comprehensive biochemical understanding. Connect. Tissue Res. 38, 17-32.
    • (1998) Connect. Tissue Res. , vol.38 , pp. 17-32
    • Hubbard, M.J.1
  • 29
    • 0034534065 scopus 로고    scopus 로고
    • Calcium transport across the dental enamel epithelium
    • in press
    • Hubbard, M.J. (2000) Calcium transport across the dental enamel epithelium. Crit. Rev. Oral Biol. Med. in press.
    • (2000) Crit. Rev. Oral Biol. Med.
    • Hubbard, M.J.1
  • 30
    • 0031054441 scopus 로고    scopus 로고
    • Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum
    • Demmer, J., Zhou, C.M. & Hubbard, M.J. (1997) Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum. FEBS Lett. 402, 145-150.
    • (1997) FEBS Lett. , vol.402 , pp. 145-150
    • Demmer, J.1    Zhou, C.M.2    Hubbard, M.J.3
  • 33
    • 0032146759 scopus 로고    scopus 로고
    • ERp28, a human endoplasmic reticulum lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif
    • Ferrari, D.M., Van Nguyen, P., Kratzin, H. & Soling, H.D. (1998) ERp28, a human endoplasmic reticulum lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif. Eur. J. Biochem. 255, 570-579.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 570-579
    • Ferrari, D.M.1    Van Nguyen, P.2    Kratzin, H.3    Soling, H.D.4
  • 34
  • 36
    • 0031882304 scopus 로고    scopus 로고
    • Windbeutel, a gene required for dorsoventral patterning in Drosophila, encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulum
    • Konsolaki, M. & Schupbach, T. (1998) Windbeutel, a gene required for dorsoventral patterning in Drosophila, encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulum. Genes Dev. 12, 120-131.
    • (1998) Genes Dev. , vol.12 , pp. 120-131
    • Konsolaki, M.1    Schupbach, T.2
  • 38
    • 0028972028 scopus 로고
    • 30kDa (calretinin) are substantially localised in the particulate fraction of rat brain
    • 30kDa (calretinin) are substantially localised in the particulate fraction of rat brain. FEBS Lett. 374, 333-337.
    • (1995) FEBS Lett. , vol.374 , pp. 333-337
    • Hubbard, M.J.1    McHugh, N.J.2
  • 39
    • 0033662286 scopus 로고    scopus 로고
    • Human ERp29: Isolation, primary structural characterisation and two-dimensional gel mapping
    • in press
    • Hubbard, M.J. & McHugh, N.J. (2000) Human ERp29: Isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis in press.
    • (2000) Electrophoresis
    • Hubbard, M.J.1    McHugh, N.J.2
  • 40
    • 0030581291 scopus 로고    scopus 로고
    • 1-β-subunit is a calcium-binding protein
    • 1-β-subunit is a calcium-binding protein. FEBS Lett. 391, 323-329.
    • (1996) FEBS Lett. , vol.391 , pp. 323-329
    • Hubbard, M.J.1    McHugh, N.J.2
  • 41
    • 0028824080 scopus 로고
    • Mass spectrometric approaches for the identification of gel-separated proteins
    • Patterson, S.D. & Aebersold, R. (1995) Mass spectrometric approaches for the identification of gel-separated proteins. Electrophoresis 16, 1791-1814.
    • (1995) Electrophoresis , vol.16 , pp. 1791-1814
    • Patterson, S.D.1    Aebersold, R.2
  • 42
    • 0016261378 scopus 로고
    • Analytical study of microsomes and isolated subcellular membranes from rat liver: IV. Biochemical, physical and morphological modifications of microsomal components induced by digitonin, EDTA and pyrophosphate
    • Amar-Costesec, A., Wibo, M., Thines-Sempoux, D., Beaufay, H. & Berthet, J. (1974) Analytical study of microsomes and isolated subcellular membranes from rat liver: IV. Biochemical, physical and morphological modifications of microsomal components induced by digitonin, EDTA and pyrophosphate. J. Cell Biol. 62, 717-745.
    • (1974) J. Cell Biol. , vol.62 , pp. 717-745
    • Amar-Costesec, A.1    Wibo, M.2    Thines-Sempoux, D.3    Beaufay, H.4    Berthet, J.5
  • 43
    • 0019537774 scopus 로고
    • Intracellular and intramembranous localization of a protein disulfide isomerase in rat liver
    • Ohba, H., Harano, T. & Omura, T. (1981) Intracellular and intramembranous localization of a protein disulfide isomerase in rat liver. J. Biochem. (Tokyo) 89, 889-900.
    • (1981) J. Biochem. (Tokyo) , vol.89 , pp. 889-900
    • Ohba, H.1    Harano, T.2    Omura, T.3
  • 44
    • 0024586112 scopus 로고
    • Preparation and characterization of dog pancreas microsomal membranes specifically depleted of protein disulphide-isomerase
    • Paver, J.L., Hawkins, H.C. & Freedman, R.B. (1989) Preparation and characterization of dog pancreas microsomal membranes specifically depleted of protein disulphide-isomerase. Biochem. J. 257, 657-663.
    • (1989) Biochem. J. , vol.257 , pp. 657-663
    • Paver, J.L.1    Hawkins, H.C.2    Freedman, R.B.3
  • 45
    • 0024999921 scopus 로고
    • Cotranslational glycosylation of proteins in systems depleted of protein disulphide isomerase
    • Bulleid, N.J. & Freedman, R.B. (1990) Cotranslational glycosylation of proteins in systems depleted of protein disulphide isomerase. EMBO J. 9, 3527-3532.
    • (1990) EMBO J. , vol.9 , pp. 3527-3532
    • Bulleid, N.J.1    Freedman, R.B.2
  • 46
    • 0027238583 scopus 로고
    • Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation
    • Nicchitta, C.V. & Blobel, G. (1993) Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation. Cell 73, 989-998.
    • (1993) Cell , vol.73 , pp. 989-998
    • Nicchitta, C.V.1    Blobel, G.2
  • 47
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment. Application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A.L., Fowler, S. & Lazarow, P.B. (1982) Isolation of intracellular membranes by means of sodium carbonate treatment. Application to endoplasmic reticulum. J. Cell Biol. 93, 97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 48
    • 0026573487 scopus 로고
    • Characterization of endoplasmic reticulum by co-localization of BiP and dicarbocyanine dyes
    • Terasaki, M. & Reese, T.S. (1992) Characterization of endoplasmic reticulum by co-localization of BiP and dicarbocyanine dyes. J. Cell Sci. 101, 315-322.
    • (1992) J. Cell Sci. , vol.101 , pp. 315-322
    • Terasaki, M.1    Reese, T.S.2
  • 49
    • 0032555788 scopus 로고    scopus 로고
    • 2+ stores has a key role in nonmuscle cell signaling and function
    • 2+ stores has a key role in nonmuscle cell signaling and function. J. Cell Biol. 142, 1395-1398.
    • (1998) J. Cell Biol. , vol.142 , pp. 1395-1398
    • Meldolesi, J.1    Pozzan, T.2
  • 51
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman, J.C., Ellis, L., Blacher, R.W., Roth, R.A. & Rutter, W.J. (1985) Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317, 267-270.
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 52
    • 0024603788 scopus 로고
    • Role of protein disulphide-isomerase in the expression of native proteins
    • Freedman, R.B., Bulleid, N.J., Hawkins, H.C. & Paver, J.L. (1989) Role of protein disulphide-isomerase in the expression of native proteins. Biochem. Soc. Symp. 55, 167-192.
    • (1989) Biochem. Soc. Symp. , vol.55 , pp. 167-192
    • Freedman, R.B.1    Bulleid, N.J.2    Hawkins, H.C.3    Paver, J.L.4
  • 53
    • 0030668358 scopus 로고    scopus 로고
    • Lactation-associated and prolactin-responsive changes in protein synthesis in mouse mammary cells
    • Beaton, A., Wilkins, R.J. & Wheeler, T.T. (1997) Lactation-associated and prolactin-responsive changes in protein synthesis in mouse mammary cells. Tissue Cell 29, 509-516.
    • (1997) Tissue Cell , vol.29 , pp. 509-516
    • Beaton, A.1    Wilkins, R.J.2    Wheeler, T.T.3
  • 54
    • 0022606290 scopus 로고
    • Development of a radio-immunoassay for quantitation of calregulin in bovine tissues
    • Khanna, N.C. & Waisman, D.M. (1986) Development of a radio-immunoassay for quantitation of calregulin in bovine tissues. Biochemistry 25, 1078-1082.
    • (1986) Biochemistry , vol.25 , pp. 1078-1082
    • Khanna, N.C.1    Waisman, D.M.2
  • 55
    • 0000540826 scopus 로고
    • The distribution of protein disulphide-isomerase activity in mammalian tissue
    • Brockway, B.E., Foster, S.J., Freedman, R.B. & Hillson, D.A. (1982) The distribution of protein disulphide-isomerase activity in mammalian tissue. Biochem. Soc. Trans. 10, 115-116.
    • (1982) Biochem. Soc. Trans. , vol.10 , pp. 115-116
    • Brockway, B.E.1    Foster, S.J.2    Freedman, R.B.3    Hillson, D.A.4
  • 56
    • 0023019562 scopus 로고
    • Hsp108, a novel heat shock inducible protein of chicken
    • Sargan, D.R., Tsai, M.J. & O'Malley, B.W. (1986) Hsp108, a novel heat shock inducible protein of chicken. Biochemistry 25, 6252-6258.
    • (1986) Biochemistry , vol.25 , pp. 6252-6258
    • Sargan, D.R.1    Tsai, M.J.2    O'Malley, B.W.3
  • 57
    • 0015912802 scopus 로고
    • Metabolism of insulin and glucagon. Glutathione-insulin transhydrogenase from microsomes of rat liver
    • Ansorge, S., Bohley, P., Kirschke, H., Langner, J., Wiederanders, B. & Hanson, H. (1973) Metabolism of insulin and glucagon. Glutathione-insulin transhydrogenase from microsomes of rat liver. Eur. J. Biochem. 32, 27-35.
    • (1973) Eur. J. Biochem. , vol.32 , pp. 27-35
    • Ansorge, S.1    Bohley, P.2    Kirschke, H.3    Langner, J.4    Wiederanders, B.5    Hanson, H.6
  • 58
    • 0020787176 scopus 로고
    • Structural properties of homogeneous protein disulphide isomerase from bovine liver purified by a rapid high-yielding procedure
    • Lambert, N. & Freedman, R.B. (1983) Structural properties of homogeneous protein disulphide isomerase from bovine liver purified by a rapid high-yielding procedure. Biochem. J. 213, 225-234.
    • (1983) Biochem. J. , vol.213 , pp. 225-234
    • Lambert, N.1    Freedman, R.B.2
  • 59
    • 0030765707 scopus 로고    scopus 로고
    • Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER
    • Carelli, S., Ceriotti, A., Cabibbo, A., Fassina, G., Ruvo, M. & Sitia, R. (1997) Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER. Science 277, 1681-1684.
    • (1997) Science , vol.277 , pp. 1681-1684
    • Carelli, S.1    Ceriotti, A.2    Cabibbo, A.3    Fassina, G.4    Ruvo, M.5    Sitia, R.6


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