메뉴 건너뛰기




Volumn 172, Issue 8, 2004, Pages 5110-5119

HLA-B27 in Transgenic Rats Forms Disulfide-Linked Heavy Chain Oligomers and Multimers That Bind to the Chaperone BiP

Author keywords

[No Author keywords available]

Indexed keywords

CONCANAVALIN A; CYSTEINE; DISULFIDE; GLUCOSE REGULATED PROTEIN 78; HLA B27 ANTIGEN; IMMUNOGLOBULIN HEAVY CHAIN; IODINE 125; OLIGOMER; POLYMER; SERINE;

EID: 1842476244     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.172.8.5110     Document Type: Article
Times cited : (86)

References (51)
  • 1
    • 0034853747 scopus 로고    scopus 로고
    • HLA-B27 and genetic predisposing factors in spondyloarthropathies
    • Reveille, J. D., E. J. Ball, and M. A. Khan. 2001. HLA-B27 and genetic predisposing factors in spondyloarthropathies. Curr. Opin. Rheumatol. 13:265.
    • (2001) Curr. Opin. Rheumatol. , vol.13 , pp. 265
    • Reveille, J.D.1    Ball, E.J.2    Khan, M.A.3
  • 3
    • 0037053328 scopus 로고    scopus 로고
    • The peptide repertoires of HLA-B27 subtypes differentially associated to spondyloarthropathy (B*2704 and B*2706) differ by specific changes at three anchor positions
    • Sesma, L., V. Montserrat, J. R. Lamas, A. Marina, J. Vazquez, and J. A. Lopez de Castro. 2002. The peptide repertoires of HLA-B27 subtypes differentially associated to spondyloarthropathy (B*2704 and B*2706) differ by specific changes at three anchor positions. J. Biol. Chem. 277:16744.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16744
    • Sesma, L.1    Montserrat, V.2    Lamas, J.R.3    Marina, A.4    Vazquez, J.5    Lopez De Castro, J.A.6
  • 4
    • 0035966070 scopus 로고    scopus 로고
    • The Cys-67 residue of HLA-B27 influences cell surface stability, peptide specificity, and T-cell antigen presentation
    • Alvarez, I., M. Marti, J. Vazquez, E. Camafeita, S. Ogueta, and J. A. Lopez de Castro. 2001. The Cys-67 residue of HLA-B27 influences cell surface stability, peptide specificity, and T-cell antigen presentation. J. Biol. Chem. 276:48740.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48740
    • Alvarez, I.1    Marti, M.2    Vazquez, J.3    Camafeita, E.4    Ogueta, S.5    Lopez De Castro, J.A.6
  • 5
    • 0022533999 scopus 로고
    • Monoclonal antibodies raised against denatured HLA-B locus heavy chains permit biochemical characterization of certain HLA-C locus products
    • Stam, N. J., H. Spits, and H. L. Ploegh. 1986. Monoclonal antibodies raised against denatured HLA-B locus heavy chains permit biochemical characterization of certain HLA-C locus products. J. Immunol. 137:2299.
    • (1986) J. Immunol. , vol.137 , pp. 2299
    • Stam, N.J.1    Spits, H.2    Ploegh, H.L.3
  • 9
    • 0037438486 scopus 로고    scopus 로고
    • CD8αβ T cells are not essential to the pathogenesis of arthritis or colitis in HLA-B27 transgenic rats
    • May, E., M. L. Dorris, N. Satumtira, I. Iqbal, M. I. Rehman, E. Lightfoot, and J. D. Taurog. 2003. CD8αβ T cells are not essential to the pathogenesis of arthritis or colitis in HLA-B27 transgenic rats. J. Immunol. 170:1099.
    • (2003) J. Immunol. , vol.170 , pp. 1099
    • May, E.1    Dorris, M.L.2    Satumtira, N.3    Iqbal, I.4    Rehman, M.I.5    Lightfoot, E.6    Taurog, J.D.7
  • 10
    • 0035253721 scopus 로고    scopus 로고
    • A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum
    • Diedrich, G., N. Bangia, M. Pan, and P. Cresswell. 2001. A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum. J. Immunol. 166:1703.
    • (2001) J. Immunol. , vol.166 , pp. 1703
    • Diedrich, G.1    Bangia, N.2    Pan, M.3    Cresswell, P.4
  • 11
    • 0037015624 scopus 로고    scopus 로고
    • ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum
    • Serwold, T., F. Gonzalez, J. Kim, R. Jacob, and N. Shastri. 2002. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 419:480.
    • (2002) Nature , vol.419 , pp. 480
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 12
    • 0038697962 scopus 로고    scopus 로고
    • Chaperones and folding of MHC class I molecules in the endoplasmic reticulum
    • Paulsson, K., and P. Wang, 2003. Chaperones and folding of MHC class I molecules in the endoplasmic reticulum. Biochim. Biophys. Acta 1641:1.
    • (2003) Biochim. Biophys. Acta , vol.1641 , pp. 1
    • Paulsson, K.1    Wang, P.2
  • 13
    • 0032742012 scopus 로고    scopus 로고
    • Misfolding of HLA-B27 as a result of its B pocket suggests a novel mechanism for its role in susceptibility to spondyloarthropathies
    • Mear, J. P., K. L. Schreiber, C. Munz, X. Zhu, S. Stevanovic, H. G. Rammensee, S. L. Rowland-Jones, and R. A. Colbert. 1999. Misfolding of HLA-B27 as a result of its B pocket suggests a novel mechanism for its role in susceptibility to spondyloarthropathies. J. Immunol. 163:6665.
    • (1999) J. Immunol. , vol.163 , pp. 6665
    • Mear, J.P.1    Schreiber, K.L.2    Munz, C.3    Zhu, X.4    Stevanovic, S.5    Rammensee, H.G.6    Rowland-Jones, S.L.7    Colbert, R.A.8
  • 14
    • 0037189545 scopus 로고    scopus 로고
    • HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum
    • Dangoria, N. S., M. L. DeLay, D. J. Kingsbury, J. P. Mear, B. Uchanska-Ziegler, A. Ziegler, and R. A. Colbert. 2002. HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum. J. Biol. Chem. 277:23459.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23459
    • Dangoria, N.S.1    DeLay, M.L.2    Kingsbury, D.J.3    Mear, J.P.4    Uchanska-Ziegler, B.5    Ziegler, A.6    Colbert, R.A.7
  • 16
    • 0035889905 scopus 로고    scopus 로고
    • Leukocyte receptor complex-encoded immunomodulatory receptors show differing specificity for alternative HLA-B27 structures
    • Allen, R. L., T. Raine, A. Haude, J. Trowsdale, and M. J. Wilson. 2001. Leukocyte receptor complex-encoded immunomodulatory receptors show differing specificity for alternative HLA-B27 structures. J. Immunol. 167:5543.
    • (2001) J. Immunol. , vol.167 , pp. 5543
    • Allen, R.L.1    Raine, T.2    Haude, A.3    Trowsdale, J.4    Wilson, M.J.5
  • 20
    • 0037352755 scopus 로고    scopus 로고
    • Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling
    • Bird, L. A., C. A. Peh, S. Kollnberger, T. Elliott, A. J. McMichael, and P. Bowness. 2003. Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling. Eur. J. Immunol. 33:748.
    • (2003) Eur. J. Immunol. , vol.33 , pp. 748
    • Bird, L.A.1    Peh, C.A.2    Kollnberger, S.3    Elliott, T.4    McMichael, A.J.5    Bowness, P.6
  • 22
    • 0027300353 scopus 로고
    • Susceptibility to inflammatory disease in HLA-B27 transgenic rat lines correlates with the level of B27 expression
    • Taurog, J. D., S. D. Maika, W. A. Simmons, M. Breban, and R. E. Hammer. 1993. Susceptibility to inflammatory disease in HLA-B27 transgenic rat lines correlates with the level of B27 expression. J. Immunol. 150:4168.
    • (1993) J. Immunol. , vol.150 , pp. 4168
    • Taurog, J.D.1    Maika, S.D.2    Simmons, W.A.3    Breban, M.4    Hammer, R.E.5
  • 23
    • 0020507231 scopus 로고
    • Structural and genetic analyses of HLA class I molecules using monoclonal xenoantibodies
    • Rebai, N., and B. Malissen. 1983. Structural and genetic analyses of HLA class I molecules using monoclonal xenoantibodies. Tissue Antigens 22:107.
    • (1983) Tissue Antigens , vol.22 , pp. 107
    • Rebai, N.1    Malissen, B.2
  • 27
    • 0031051852 scopus 로고    scopus 로고
    • Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome
    • Hughes, E. A., C. Hammond, and P. Cresswell. 1997. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proc. Natl. Acad. Sci. USA 94:1896.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1896
    • Hughes, E.A.1    Hammond, C.2    Cresswell, P.3
  • 28
    • 0020574933 scopus 로고
    • The cellular basis of adjuvant arthritis, 1. Enhancement of cell-mediated passive transfer by concanavalin A and by immunosuppressive pretreatment of the recipient
    • Taurog, J. D., G. P. Sandberg, and M. L. Mahowald. 1983. The cellular basis of adjuvant arthritis, 1. Enhancement of cell-mediated passive transfer by concanavalin A and by immunosuppressive pretreatment of the recipient. Cell. Immunol. 75:271.
    • (1983) Cell. Immunol. , vol.75 , pp. 271
    • Taurog, J.D.1    Sandberg, G.P.2    Mahowald, M.L.3
  • 29
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick, T. P., N. Bangia, D. R. Peaper, and P. Cresswell. 2002. Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 16:87.
    • (2002) Immunity , vol.16 , pp. 87
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 31
    • 0028200169 scopus 로고
    • Mechanism and subcellular localization of secretory IgM polymer assembly
    • Brewer, J. W., T. D. Randall, R. M. Parkhouse, and R. B. Corley. 1994. Mechanism and subcellular localization of secretory IgM polymer assembly. J. Biol. Chem. 269:17338.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17338
    • Brewer, J.W.1    Randall, T.D.2    Parkhouse, R.M.3    Corley, R.B.4
  • 32
    • 0028592574 scopus 로고
    • The sequence of a cDNA encoding the major vault protein from Rattus norvegicus
    • Kickhoefer, V. A., and L. H. Rome. 1994. The sequence of a cDNA encoding the major vault protein from Rattus norvegicus. Gene 151:257.
    • (1994) Gene , vol.151 , pp. 257
    • Kickhoefer, V.A.1    Rome, L.H.2
  • 33
    • 1542305542 scopus 로고    scopus 로고
    • Formation of HLA-B27 homodimers and their relationship to assembly kinetics
    • Antoniou, A. N., S. Ford, J. D. Taurog, G. W. Butcher, and S. J. Powis. 2004 Formation of HLA-B27 homodimers and their relationship to assembly kinetics. J. Biol. Chem. 279:8895.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8895
    • Antoniou, A.N.1    Ford, S.2    Taurog, J.D.3    Butcher, G.W.4    Powis, S.J.5
  • 34
    • 0029564918 scopus 로고
    • Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment
    • Raposo, G., H. M. van Santen, R. Leijendekker, H. J. Geuze, and H. L. Ploegh. 1995. Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment. J. Cell Biol. 131:1403.
    • (1995) J. Cell Biol. , vol.131 , pp. 1403
    • Raposo, G.1    Van Santen, H.M.2    Leijendekker, R.3    Geuze, H.J.4    Ploegh, H.L.5
  • 35
    • 0028917887 scopus 로고
    • Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules
    • Nössner, E., and P. Parham. 1995. Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules. J. Exp. Med. 181:327.
    • (1995) J. Exp. Med. , vol.181 , pp. 327
    • Nössner, E.1    Parham, P.2
  • 36
    • 0037166298 scopus 로고    scopus 로고
    • Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum
    • Paulsson, K. M., M. J. Kleijmeer, J. Griffith, M. Jevon, S. Chen, P. O. Anderson, H. O. Sjogren, S. Li. and P. Wang. 2002. Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum. J. Biol. Chem. 277:18266.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18266
    • Paulsson, K.M.1    Kleijmeer, M.J.2    Griffith, J.3    Jevon, M.4    Chen, S.5    Anderson, P.O.6    Sjogren, H.O.7    Li, S.8    Wang, P.9
  • 37
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi, S., S. E. Cwirla, W. J. Dower, R. J. Lipshutz, S. R. Sprang, J. F. Sambrook, and M. J. Gething. 1993. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75:717.
    • (1993) Cell , vol.75 , pp. 717
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.F.6    Gething, M.J.7
  • 38
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J., and J. Sambrook. 1992. Protein folding in the cell. Nature 355:33.
    • (1992) Nature , vol.355 , pp. 33
    • Gething, M.J.1    Sambrook, J.2
  • 39
    • 0035966320 scopus 로고    scopus 로고
    • The unfolding tale of the unfolded protein response
    • Ma, Y., and L. M. Hendershot. 2001. The unfolding tale of the unfolded protein response. Cell 107:827.
    • (2001) Cell , vol.107 , pp. 827
    • Ma, Y.1    Hendershot, L.M.2
  • 40
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A., Y. Zhang, L. M. Hendershot, H. P. Harding, and D. Ron. 2000. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2:326.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 326
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 41
    • 0036314984 scopus 로고    scopus 로고
    • Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response
    • Ma, Y., J. W. Brewer, J. A. Diehl, and L. M. Hendershot. 2002. Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response. J. Mol. Biol. 318:1351.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1351
    • Ma, Y.1    Brewer, J.W.2    Diehl, J.A.3    Hendershot, L.M.4
  • 42
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen, J., X. Chen, L. Hendershot, and R. Prywes. 2002. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev. Cell 3:99.
    • (2002) Dev. Cell , vol.3 , pp. 99
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 43
    • 0034214169 scopus 로고    scopus 로고
    • HLA-B27 misfolding: A solution to the spondyloarthropathy conundrum?
    • Colbert, R. A. 2000. HLA-B27 misfolding: a solution to the spondyloarthropathy conundrum? Mol. Med. Today 6:224.
    • (2000) Mol. Med. Today , vol.6 , pp. 224
    • Colbert, R.A.1
  • 44
    • 0032779694 scopus 로고    scopus 로고
    • Signal transduction from the endoplasmic reticulum to the cell nucleus
    • Pahl, H. L. 1999. Signal transduction from the endoplasmic reticulum to the cell nucleus. Physiol. Rev. 79:683.
    • (1999) Physiol. Rev. , vol.79 , pp. 683
    • Pahl, H.L.1
  • 45
    • 0031081340 scopus 로고    scopus 로고
    • The ER-overload response: Activation of NF-κB
    • Pahl, H. L., and P. A. Baeuerle. 1997. The ER-overload response: activation of NF-κB. Trends Biochem. Sci. 22:63.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 63
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 47
    • 0033789614 scopus 로고    scopus 로고
    • 2-microglobulin-deficient mice without expression of HLA-B27: Association with deficiency of endogenous major histocompatibility complex class I expression
    • 2-microglobulin-deficient mice without expression of HLA-B27: association with deficiency of endogenous major histocompatibility complex class I expression. Arthritis Rheum. 43:2290.
    • (2000) Arthritis Rheum. , vol.43 , pp. 2290
    • Kingsbury, D.J.1    Mear, J.P.2    Witte, D.P.3    Taurog, J.D.4    Roopenian, D.C.5    Colbert, R.A.6
  • 48
    • 0037157856 scopus 로고    scopus 로고
    • Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER
    • Molinari, M., C. Galli, V. Piccaluga, M. Pieren, and P. Paganetti. 2002. Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER. J. Cell Biol. 158:247.
    • (2002) J. Cell Biol. , vol.158 , pp. 247
    • Molinari, M.1    Galli, C.2    Piccaluga, V.3    Pieren, M.4    Paganetti, P.5
  • 49
    • 0022341853 scopus 로고
    • Organization, sequence and expression of the HLA-B27 gene: A molecular approach to analyze HLA and disease associations
    • Weiss, E. H., W. Kuon, C. Dorner, M. Lang, and G. Riethmuller. 1985. Organization, sequence and expression of the HLA-B27 gene: a molecular approach to analyze HLA and disease associations. Immunobiology 170:367.
    • (1985) Immunobiology , vol.170 , pp. 367
    • Weiss, E.H.1    Kuon, W.2    Dorner, C.3    Lang, M.4    Riethmuller, G.5
  • 50
    • 0025319230 scopus 로고
    • Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: Frequency and nature of errors produced in amplification
    • Ennis, P. D., J. Zemmour, R. D. Salter, and P. Parham. 1990. Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: frequency and nature of errors produced in amplification. Proc. Natl. Acad. Sci. USA 87:2833.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2833
    • Ennis, P.D.1    Zemmour, J.2    Salter, R.D.3    Parham, P.4
  • 51
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari, M., and A. Helenius. 1999. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402:90.
    • (1999) Nature , vol.402 , pp. 90
    • Molinari, M.1    Helenius, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.