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Volumn 7, Issue 1, 1996, Pages 114-121

Purification and partial molecular characterization of GRP94, an ER resident chaperone

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; SUIDAE; SUS SCROFA;

EID: 0030087534     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0015     Document Type: Article
Times cited : (53)

References (35)
  • 1
    • 0023660180 scopus 로고
    • Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum
    • 1. Smith, M. J., and Koch, G. L. E. (1987) Isolation and identification of partial cDNA clones for endoplasmin, the major glycoprotein of mammalian endoplasmic reticulum. J. Mol. Biol. 194, 345-347.
    • (1987) J. Mol. Biol. , vol.194 , pp. 345-347
    • Smith, M.J.1    Koch, G.L.E.2
  • 2
    • 0023228980 scopus 로고
    • Structural analysis of genes encoding polymorphic antigens of chemically induced tumors
    • 2. Srivastava, P. K., Chen, Y. T., and Old, L. J. (1987) Structural analysis of genes encoding polymorphic antigens of chemically induced tumors. Proc. Natl. Acad. Sci. USA 84, 3804-3807.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3804-3807
    • Srivastava, P.K.1    Chen, Y.T.2    Old, L.J.3
  • 3
    • 0023664518 scopus 로고
    • ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94)
    • 3. Mazzarella, R. A., and Green, M. (1987) ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). J. Biol. Chem. 262, 8875-8883.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8875-8883
    • Mazzarella, R.A.1    Green, M.2
  • 4
    • 0023019562 scopus 로고
    • hsp108, a novel heat shock inducible protein of chicken
    • 4. Sargan, D. R., Tsai, M. J., and 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
  • 7
    • 0021910786 scopus 로고
    • Structure and assembly of the endoplasmic reticulum: The synthesis of three major ER proteins during lipopolysaccharide-induced differentiation of murine lymphocytes
    • 7. Lewis, M. J., Mazzarella, R. A., and Green, M. (1985) Structure and assembly of the endoplasmic reticulum: The synthesis of three major ER proteins during lipopolysaccharide-induced differentiation of murine lymphocytes. J. Biol. Chem. 260, 3050-3057.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3050-3057
    • Lewis, M.J.1    Mazzarella, R.A.2    Green, M.3
  • 8
    • 0027571389 scopus 로고
    • A pathogen-induced gene of barley encodes a HSP90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum
    • 8. Walther-Larsen, H., Brandt, J., Collinge, D. B., and Thordal-Christensen, H. (1993) A pathogen-induced gene of barley encodes a HSP90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum. Plant Mol. Biol. 21, 1097-1108.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 1097-1108
    • Walther-Larsen, H.1    Brandt, J.2    Collinge, D.B.3    Thordal-Christensen, H.4
  • 9
    • 0023660117 scopus 로고
    • The glucose-regulated protein grp94 is related to heat shock protein hsp90
    • 9. Sorger, P. K., and Pelham, H. R. (1987) The glucose-regulated protein grp94 is related to heat shock protein hsp90. J. Mol. Biol. 194, 341-344.
    • (1987) J. Mol. Biol. , vol.194 , pp. 341-344
    • Sorger, P.K.1    Pelham, H.R.2
  • 10
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • 10. Blobel, G. (1980) Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77, 1496-1500.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 11
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • 11. Munro, S., and Pelham, H. R. B. (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell 48, 899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 12
    • 0021821853 scopus 로고
    • Structure and assembly of the endoplasmic reticulum: Biosynthetic sorting of endoplasmic reticulum proteins
    • 12. Lewis, M. J., Turco, S. J., and Green, M. (1985) Structure and assembly of the endoplasmic reticulum: Biosynthetic sorting of endoplasmic reticulum proteins. J. Biol. Chem. 260, 6926-6931.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6926-6931
    • Lewis, M.J.1    Turco, S.J.2    Green, M.3
  • 14
    • 0026077464 scopus 로고
    • Characterization and purification of the 94-kDa glucose-regulated protein
    • 14. Kang, H. S., and Welch, W. J. (1991) Characterization and purification of the 94-kDa glucose-regulated protein. J. Biol. Chem. 266, 5643-5649.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5643-5649
    • Kang, H.S.1    Welch, W.J.2
  • 15
    • 0010625474 scopus 로고
    • Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts
    • 15. Shiu, R. P. C., Pouyssegur, J., and Pastan, I. (1977) Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts. Proc. Natl. Acad. Sci. USA 74, 3840-3844.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3840-3844
    • Shiu, R.P.C.1    Pouyssegur, J.2    Pastan, I.3
  • 16
    • 0023133224 scopus 로고
    • Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells
    • 16. Lee, A. S. (1987) Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem. Sci. 12, 20-23.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 20-23
    • Lee, A.S.1
  • 17
    • 0023546204 scopus 로고
    • Regulation of the glucose-regulated protein genes by β-mercaptoethanol requires de novo protein synthesis and correlates with inhibition of protein glycosylation
    • 17. Kim, Y. K., Kim, K. S., and Lee, A. S. (1986) Regulation of the glucose-regulated protein genes by β-mercaptoethanol requires de novo protein synthesis and correlates with inhibition of protein glycosylation. J. Cell. Physiol. 133, 533-559.
    • (1986) J. Cell. Physiol. , vol.133 , pp. 533-559
    • Kim, Y.K.1    Kim, K.S.2    Lee, A.S.3
  • 18
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • 18. Kozutsumi, Y., Segal, M., Normington, K., Gething, M. J., and Sambrook, J. (1988) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature (London) 332, 462-464.
    • (1988) Nature (London) , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 19
    • 0026742999 scopus 로고
    • HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
    • 19. Schaiff, W. T., Hruska, K. A., McCourt, D. W., Green, M., and Schwartz, B. D. (1992) HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J. Exp. Med. 176, 657-666.
    • (1992) J. Exp. Med. , vol.176 , pp. 657-666
    • Schaiff, W.T.1    Hruska, K.A.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 20
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains
    • 20. Melnick, J., Aviel, S., and Argon, Y. (1992) The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains. J. Biol. Chem. 267, 21303-21306.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21303-21306
    • Melnick, J.1    Aviel, S.2    Argon, Y.3
  • 21
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • 21. Melnick, J., Dul, J. L., and Argon, Y. (1994) Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature (London) 370, 373-375.
    • (1994) Nature (London) , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 22
    • 0028999264 scopus 로고
    • Conformation-defective herpes simplex virus-1 glycoprotein B activates the promoter of the grp94 gene that codes for the 94-kD stress protein in the endoplasmic reticulum
    • 22. Ramakrishnan, M., Tugizov, S., Pereira, L., and Lee, A. S. (1995) Conformation-defective herpes simplex virus-1 glycoprotein B activates the promoter of the grp94 gene that codes for the 94-kD stress protein in the endoplasmic reticulum. DNA Cell Biol. 14, 373-384.
    • (1995) DNA Cell Biol. , vol.14 , pp. 373-384
    • Ramakrishnan, M.1    Tugizov, S.2    Pereira, L.3    Lee, A.S.4
  • 23
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • 23. Jakob, U., and Buchner, J. (1994) Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci. 19, 205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 24
    • 0021253007 scopus 로고
    • Biochemical characterization of the 94-and 78-kilodalton glucose-regulated proteins in hamster fibroblasts
    • 24. Lee, A. S., Bell, J., and Ting, J. (1984) Biochemical characterization of the 94-and 78-kilodalton glucose-regulated proteins in hamster fibroblasts. J. Biol. Chem. 259, 4616-4621.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4616-4621
    • Lee, A.S.1    Bell, J.2    Ting, J.3
  • 26
    • 0028024312 scopus 로고
    • Analysis of the structure and synthesis of GRP94, an abundant stress protein of the endoplasmic reticulum
    • 26. Qu, D., Mazzarella, R. A., and Green, M. (1994) Analysis of the structure and synthesis of GRP94, an abundant stress protein of the endoplasmic reticulum. DNA Cell Biol. 13, 117-124.
    • (1994) DNA Cell Biol. , vol.13 , pp. 117-124
    • Qu, D.1    Mazzarella, R.A.2    Green, M.3
  • 27
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • 27. Walter, P., and Blobel, G. (1983) Preparation of microsomal membranes for cotranslational protein translocation. Meth. Enzymol. 96, 84-93.
    • (1983) Meth. Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 28
    • 0027238583 scopus 로고
    • Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation
    • 28. Nicchitta, C. V., and 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
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 29. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 259, 680-685.
    • (1970) Nature (London) , vol.259 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0022833371 scopus 로고
    • Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin
    • 30. Koch, G., Smith, M., Macer, D., Webster, P., and Mortara, R. (1986) Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin. J. Cell Sci. 86, 217-232.
    • (1986) J. Cell Sci. , vol.86 , pp. 217-232
    • Koch, G.1    Smith, M.2    Macer, D.3    Webster, P.4    Mortara, R.5
  • 31
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • 31. Palade, G. (1975) Intracellular aspects of the process of protein synthesis. Science 189, 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 32
    • 0026716017 scopus 로고
    • Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kD protein
    • 32. Kelleher, D. J., Kreibich, G., and Gilmore, R. (1992) Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kD protein. Cell 69, 55-65.
    • (1992) Cell , vol.69 , pp. 55-65
    • Kelleher, D.J.1    Kreibich, G.2    Gilmore, R.3
  • 33
    • 0021956575 scopus 로고
    • Isolation and characterization of CAB-63, a novel calcium-binding protein
    • 33. Waisman, D. M., Salimath, B. P., and Anderson, M. J. (1985) Isolation and characterization of CAB-63, a novel calcium-binding protein. J. Biol. Chem. 260, 1652-1660.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1652-1660
    • Waisman, D.M.1    Salimath, B.P.2    Anderson, M.J.3
  • 34
    • 0028486023 scopus 로고
    • A single purification procedure for the major resident proteins of the ER lumen; endoplasmin, BiP, calreticulin and protein disulfide isomerase
    • 34. Rowling, P. J. E., McLaughlin, S. H., Pollock, G. S., and Freedman, R. B. (1994) A single purification procedure for the major resident proteins of the ER lumen; endoplasmin, BiP, calreticulin and protein disulfide isomerase. Protein Expression Purif. 5, 331-336.
    • (1994) Protein Expression Purif. , vol.5 , pp. 331-336
    • Rowling, P.J.E.1    McLaughlin, S.H.2    Pollock, G.S.3    Freedman, R.B.4
  • 35
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • 35. Fujiki, Y., Hubbard, A. L., Fowler, S., and 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.