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Volumn 30, Issue 7, 2012, Pages 558-562

Release of the glucose-regulated protein 94 by baby hamster kidney cells

Author keywords

Glucose regulated protein 94; Heat shock protein; Lipid rafts; Release; Secretion

Indexed keywords

BREFELDIN A; GLUCOSE REGULATED PROTEIN 94; MONENSIN;

EID: 84867020107     PISSN: 02636484     EISSN: 10990844     Source Type: Journal    
DOI: 10.1002/cbf.2831     Document Type: Article
Times cited : (8)

References (29)
  • 1
    • 0037409604 scopus 로고    scopus 로고
    • Evolution of heat shock protein and immunity
    • Robert J. Evolution of heat shock protein and immunity. Dev Comp Immunol 2003; 27: 449-464.
    • (2003) Dev Comp Immunol , vol.27 , pp. 449-464
    • Robert, J.1
  • 2
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S, Pelham HR. A C-terminal signal prevents secretion of luminal ER proteins. Cell 1987; 48: 899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 3
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick J, Dul JL, Argon Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 1994; 370: 373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 4
    • 0036785611 scopus 로고    scopus 로고
    • Evidence that glycoprotein 96 (B2), a stress protein, functions as a Th2-specific costimulatory molecule
    • Banerjee PP, Vinay DS, Mathew A, et al. Evidence that glycoprotein 96 (B2), a stress protein, functions as a Th2-specific costimulatory molecule. J Immunol 2002; 169: 3507-3518.
    • (2002) J Immunol , vol.169 , pp. 3507-3518
    • Banerjee, P.P.1    Vinay, D.S.2    Mathew, A.3
  • 5
    • 0033747044 scopus 로고    scopus 로고
    • Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway
    • Basu S, Binder RJ, Suto R, et al. Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int Immunol 2000; 12: 1539-1546.
    • (2000) Int Immunol , vol.12 , pp. 1539-1546
    • Basu, S.1    Binder, R.J.2    Suto, R.3
  • 6
    • 0030905479 scopus 로고    scopus 로고
    • The endoplasmic reticulum-resident stress protein gp96 binds peptides translocated by TAP
    • Lammert E, Arnold D, Nijenhuis M, et al. The endoplasmic reticulum-resident stress protein gp96 binds peptides translocated by TAP. Eur J Immunol 1997; 2: 923-927.
    • (1997) Eur J Immunol , vol.2 , pp. 923-927
    • Lammert, E.1    Arnold, D.2    Nijenhuis, M.3
  • 7
    • 0030805217 scopus 로고    scopus 로고
    • TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin
    • Spee P, Neefjes J. TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin. Eur J Immunol 1997; 27: 2441-2449.
    • (1997) Eur J Immunol , vol.27 , pp. 2441-2449
    • Spee, P.1    Neefjes, J.2
  • 8
    • 0033839045 scopus 로고    scopus 로고
    • The heat shock protein gp96 induces maturation of dendritic cells and down-regulation of its receptor
    • Singh-Jasuja H, Scherer HU, Hilf N, et al. The heat shock protein gp96 induces maturation of dendritic cells and down-regulation of its receptor. Eur J Immunol 2000; 30: 2211-2215.
    • (2000) Eur J Immunol , vol.30 , pp. 2211-2215
    • Singh-Jasuja, H.1    Scherer, H.U.2    Hilf, N.3
  • 9
    • 0035893009 scopus 로고    scopus 로고
    • Cell surface targeting of heat shock protein gp96 induces dendritic cell maturation and antitumor immunity
    • Zheng H, Dai J, Stoilova D, Li Z. Cell surface targeting of heat shock protein gp96 induces dendritic cell maturation and antitumor immunity. J Immunol 2001; 167: 6731-6735.
    • (2001) J Immunol , vol.167 , pp. 6731-6735
    • Zheng, H.1    Dai, J.2    Stoilova, D.3    Li, Z.4
  • 10
    • 0035877850 scopus 로고    scopus 로고
    • Virally induced lytic cell death elicits the release of immunogenic GRP94/gp96
    • Berwin B, Reed RC, Nicchitta CV. Virally induced lytic cell death elicits the release of immunogenic GRP94/gp96. J Biol Chem 2001; 276: 21083-21088.
    • (2001) J Biol Chem , vol.276 , pp. 21083-21088
    • Berwin, B.1    Reed, R.C.2    Nicchitta, C.V.3
  • 11
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth C, Koch GL. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 1989; 59: 729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.2
  • 12
    • 0029838338 scopus 로고    scopus 로고
    • Tumor-specific cell surface expression of KDEL-containing, endoplasmic reticular heat shock protein gp96
    • Altmeyer A, Maki RG, Feldweg AM, et al. Tumor-specific cell surface expression of KDEL-containing, endoplasmic reticular heat shock protein gp96. Int J Cancer 1996; 69: 340-349.
    • (1996) Int J Cancer , vol.69 , pp. 340-349
    • Altmeyer, A.1    Maki, R.G.2    Feldweg, A.M.3
  • 13
    • 77949263080 scopus 로고    scopus 로고
    • Glucose-regulated protein 78 (Grp78/BiP) is secreted by human oviduct epithelial cells and the recombinant protein modulates sperm-zona pellucida binding
    • Briggiler CI, González-Echeverría MF, Munuce MJ, et al. Glucose-regulated protein 78 (Grp78/BiP) is secreted by human oviduct epithelial cells and the recombinant protein modulates sperm-zona pellucida binding. Fertil Steril 2010; 93: 1574-1584.
    • (2010) Fertil Steril , vol.93 , pp. 1574-1584
    • Briggiler, C.I.1    González-Echeverría, M.F.2    Munuce, M.J.3
  • 14
    • 0345035504 scopus 로고    scopus 로고
    • Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved
    • Robert J, Ménoret A, Cohen N. Cell surface expression of the endoplasmic reticular heat shock protein gp96 is phylogenetically conserved. J Immunol 1999; 163: 4133-4139.
    • (1999) J Immunol , vol.163 , pp. 4133-4139
    • Robert, J.1    Ménoret, A.2    Cohen, N.3
  • 15
    • 0022534393 scopus 로고
    • Tumor rejection antigens of chemically induced sarcomas of inbred mice
    • Srivastava PK, DeLeo AB, Old LJ. Tumor rejection antigens of chemically induced sarcomas of inbred mice. Proc Natl Acad Sci U S A 1986; 83: 3407-3411.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 3407-3411
    • Srivastava, P.K.1    DeLeo, A.B.2    Old, L.J.3
  • 16
    • 0031055601 scopus 로고    scopus 로고
    • Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones
    • Wiest DL, Bhandoola A, Punt J, et al. Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones. Proc Natl Acad Sci U S A 1997; 94: 1884-1889.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 1884-1889
    • Wiest, D.L.1    Bhandoola, A.2    Punt, J.3
  • 17
    • 77957344304 scopus 로고    scopus 로고
    • Secretion of the heat shock proteins HSP70 and HSC70 by baby hamster kidney (BHK-21) cells
    • Evdokimovskaya Y, Skarga Y, Vrublevskaya V, Morenkov O. Secretion of the heat shock proteins HSP70 and HSC70 by baby hamster kidney (BHK-21) cells. Cell Biol Int 2010; 34: 985-990.
    • (2010) Cell Biol Int , vol.34 , pp. 985-990
    • Evdokimovskaya, Y.1    Skarga, Y.2    Vrublevskaya, V.3    Morenkov, O.4
  • 19
    • 70449713654 scopus 로고    scopus 로고
    • GRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib
    • Kern J, Untergasser G, Zenzmaier C, et al. GRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib. Blood 2009; 114: 3960-3967.
    • (2009) Blood , vol.114 , pp. 3960-3967
    • Kern, J.1    Untergasser, G.2    Zenzmaier, C.3
  • 20
    • 20744436655 scopus 로고    scopus 로고
    • Exosome-dependent trafficking of hsp70: a novel secretory pathway for cellular stress proteins
    • Lancaster GI, Febbraio MA. Exosome-dependent trafficking of hsp70: a novel secretory pathway for cellular stress proteins. J Biol Chem 2005; 280: 23349-23355.
    • (2005) J Biol Chem , vol.280 , pp. 23349-23355
    • Lancaster, G.I.1    Febbraio, M.A.2
  • 21
    • 33750570923 scopus 로고    scopus 로고
    • Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosome
    • Mambula SS, Calderwood SK. Heat shock protein 70 is secreted from tumor cells by a nonclassical pathway involving lysosomal endosome. J Immunol 2006; 177: 7849-7857.
    • (2006) J Immunol , vol.177 , pp. 7849-7857
    • Mambula, S.S.1    Calderwood, S.K.2
  • 22
    • 0037096162 scopus 로고    scopus 로고
    • The exosome pathway in K562 cells is regulated by Rab11
    • Savina A, Vidal M, Colombo MI. The exosome pathway in K562 cells is regulated by Rab11. J Cell Sci 2002; 115: 2505-2515.
    • (2002) J Cell Sci , vol.115 , pp. 2505-2515
    • Savina, A.1    Vidal, M.2    Colombo, M.I.3
  • 23
    • 0026024416 scopus 로고
    • Brefeldin A, a drug that blocks secretion, prevents the assembly of nonclathrin-coated buds on Golgi cisternae
    • Orci L, Tagaya M, Amherdt M, et al. Brefeldin A, a drug that blocks secretion, prevents the assembly of nonclathrin-coated buds on Golgi cisternae. Cell 1991; 64: 1183-1195.
    • (1991) Cell , vol.64 , pp. 1183-1195
    • Orci, L.1    Tagaya, M.2    Amherdt, M.3
  • 24
    • 0025240867 scopus 로고
    • Alteration of intracellular traffic by monensin; mechanism, specificity and relationship to toxicity
    • Mollenhauer HH, Morré DJ, Rowe LD. Alteration of intracellular traffic by monensin; mechanism, specificity and relationship to toxicity. Biochim Biophys Acta 1990; 1031: 225-246.
    • (1990) Biochim Biophys Acta , vol.1031 , pp. 225-246
    • Mollenhauer, H.H.1    Morré, D.J.2    Rowe, L.D.3
  • 25
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterolrich membrane rafts
    • Brown DA, London E. Structure and function of sphingolipid- and cholesterolrich membrane rafts. J Biol Chem 2000; 275: 17221-17224.
    • (2000) J Biol Chem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 27
    • 1842484428 scopus 로고    scopus 로고
    • Lipid rafts and the regulation of exocytosis
    • Salaün C, James DJ, Chamberlain LH. Lipid rafts and the regulation of exocytosis. Traffic 2004; 5: 255-264.
    • (2004) Traffic , vol.5 , pp. 255-264
    • Salaün, C.1    James, D.J.2    Chamberlain, L.H.3
  • 29
    • 0031793127 scopus 로고    scopus 로고
    • Heat shock protein 70kDa: molecular biology, biochemistry, and physiology
    • Kiang JG, Tsokos GC. Heat shock protein 70kDa: molecular biology, biochemistry, and physiology. Pharmacol Ther 1998; 80: 183-201.
    • (1998) Pharmacol Ther , vol.80 , pp. 183-201
    • Kiang, J.G.1    Tsokos, G.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.