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Volumn 136, Issue 4, 2012, Pages 380-384

The multi-faceted nature of HLA class I dimer molecules

Author keywords

Dimers; HLA B27; HLA G; MHCI; Redox

Indexed keywords

DIMER; HLA ANTIGEN CLASS 1; HLA B27 ANTIGEN; HLA G ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

EID: 84863227284     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/j.1365-2567.2012.03593.x     Document Type: Review
Times cited : (25)

References (45)
  • 1
    • 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 et al. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 2002; 16:99-109.
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3
  • 2
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
    • Garbi N, Tanaka S, Momburg F, Hammerling GJ. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat Immunol 2006; 7:93-102.
    • (2006) Nat Immunol , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 3
    • 0033681184 scopus 로고    scopus 로고
    • Impaired assembly yet normal trafficking of MHC class I molecules in Tapasin mutant mice [In Process Citation]
    • Grandea AG IIII, Golovina TN, Hamilton SE et al. Impaired assembly yet normal trafficking of MHC class I molecules in Tapasin mutant mice [In Process Citation]. Immunity 2000; 13:213-22.
    • (2000) Immunity , vol.13 , pp. 213-222
    • Grandea IIII, A.G.1    Golovina, T.N.2    Hamilton, S.E.3
  • 4
    • 33744961082 scopus 로고    scopus 로고
    • Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules
    • Zhang Y, Baig E, Williams DB. Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules. J Biol Chem 2006; 281:14622-31.
    • (2006) J Biol Chem , vol.281 , pp. 14622-14631
    • Zhang, Y.1    Baig, E.2    Williams, D.B.3
  • 7
  • 8
    • 35748981184 scopus 로고    scopus 로고
    • Association scan of 14,500 nonsynonymous SNPs in four diseases identifies autoimmunity variants
    • Burton PR, Clayton DG, Cardon LR et al. Association scan of 14, 500 nonsynonymous SNPs in four diseases identifies autoimmunity variants. Nat Genet 2007; 39:1329-37.
    • (2007) Nat Genet , vol.39 , pp. 1329-1337
    • Burton, P.R.1    Clayton, D.G.2    Cardon, L.R.3
  • 9
    • 79960899377 scopus 로고    scopus 로고
    • Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility
    • Evans DM, Spencer CC, Pointon JJ et al. Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility. Nat Genet 2011; 43:761-7.
    • (2011) Nat Genet , vol.43 , pp. 761-767
    • Evans, D.M.1    Spencer, C.C.2    Pointon, J.J.3
  • 10
    • 0033136630 scopus 로고    scopus 로고
    • Cutting edge: HLA-B27 can form a novel β2-microglobulin-free heavy chain homodimer structure
    • Allen RL, O'Callaghan CA, McMichael AJ, Bowness P. Cutting edge: HLA-B27 can form a novel β2-microglobulin-free heavy chain homodimer structure. J Immunol 1999; 162:5045-8.
    • (1999) J Immunol , vol.162 , pp. 5045-5048
    • Allen, R.L.1    O'Callaghan, C.A.2    McMichael, A.J.3    Bowness, P.4
  • 12
    • 3242798755 scopus 로고    scopus 로고
    • HLA-B27 heavy chain homodimers are expressed in HLA-B27 transgenic rodent models of spondyloarthritis and are ligands for paired Ig-like receptors
    • Kollnberger S, Bird LA, Roddis M et al. HLA-B27 heavy chain homodimers are expressed in HLA-B27 transgenic rodent models of spondyloarthritis and are ligands for paired Ig-like receptors. J Immunol 2004; 173:1699-710.
    • (2004) J Immunol , vol.173 , pp. 1699-1710
    • Kollnberger, S.1    Bird, L.A.2    Roddis, M.3
  • 13
    • 0036246467 scopus 로고    scopus 로고
    • Free HLA class I heavy chain-carrying monocytes - a potential role in the pathogenesis of spondyloarthropathies
    • Tsai WC, Chen CJ, Yen JH, Ou TT, Tsai JJ, Liu CS, Liu HW. Free HLA class I heavy chain-carrying monocytes - a potential role in the pathogenesis of spondyloarthropathies. J Rheumatol 2002; 29:966-72.
    • (2002) J Rheumatol , vol.29 , pp. 966-972
    • Tsai, W.C.1    Chen, C.J.2    Yen, J.H.3    Ou, T.T.4    Tsai, J.J.5    Liu, C.S.6    Liu, H.W.7
  • 14
    • 0037352755 scopus 로고    scopus 로고
    • Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling
    • Bird LA, Peh CA, Kollnberger S, Elliott T, McMichael AJ, Bowness P. Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling. Eur J Immunol 2003; 33:748-59.
    • (2003) Eur J Immunol , vol.33 , pp. 748-759
    • Bird, L.A.1    Peh, C.A.2    Kollnberger, S.3    Elliott, T.4    McMichael, A.J.5    Bowness, P.6
  • 15
    • 33750807019 scopus 로고    scopus 로고
    • Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d)
    • Shiroishi M, Kuroki K, Rasubala L et al. Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d). Proc Natl Acad Sci U S A 2006; 103:16412-7.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 16412-16417
    • Shiroishi, M.1    Kuroki, K.2    Rasubala, L.3
  • 16
    • 0035889905 scopus 로고    scopus 로고
    • Leukocyte receptor complex-encoded immunomodulatory receptors show differing specificity for alternative HLA-B27 structures
    • Allen RL, Raine T, Haude A, Trowsdale J, Wilson MJ. Leukocyte receptor complex-encoded immunomodulatory receptors show differing specificity for alternative HLA-B27 structures. J Immunol 2001; 167:5543-7.
    • (2001) J Immunol , vol.167 , pp. 5543-5547
    • Allen, R.L.1    Raine, T.2    Haude, A.3    Trowsdale, J.4    Wilson, M.J.5
  • 17
    • 79952760897 scopus 로고    scopus 로고
    • HLA class I allelic sequence and conformation regulate leukocyte Ig-like receptor binding
    • Jones DC, Kosmoliaptsis V, Apps R et al. HLA class I allelic sequence and conformation regulate leukocyte Ig-like receptor binding. J Immunol 2011; 186:2990-7.
    • (2011) J Immunol , vol.186 , pp. 2990-2997
    • Jones, D.C.1    Kosmoliaptsis, V.2    Apps, R.3
  • 18
    • 1542305542 scopus 로고    scopus 로고
    • Formation of HLA-B27 homodimers and their relationship to assembly kinetics
    • Antoniou AN, Ford S, Taurog JD, Butcher GW, Powis SJ. Formation of HLA-B27 homodimers and their relationship to assembly kinetics. J Biol Chem 2004; 279:8895-902.
    • (2004) J Biol Chem , vol.279 , pp. 8895-8902
    • Antoniou, A.N.1    Ford, S.2    Taurog, J.D.3    Butcher, G.W.4    Powis, S.J.5
  • 19
    • 0037189545 scopus 로고    scopus 로고
    • HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum
    • Dangoria NS, DeLay ML, Kingsbury DJ, Mear JP, Uchanska-Ziegler B, Ziegler A, Colbert RA. HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum. J Biol Chem 2002; 277:23459-68.
    • (2002) J Biol Chem , vol.277 , pp. 23459-23468
    • 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
  • 20
    • 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 JP, Schreiber KL, Munz C, Zhu X, Stevanovic S, Rammensee HG, Rowland-Jones SL, Colbert RA. Misfolding of HLA-B27 as a result of its B pocket suggests a novel mechanism for its role in susceptibility to spondyloarthropathies. J Immunol 1999; 163:6665-70.
    • (1999) J Immunol , vol.163 , pp. 6665-6670
    • 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
  • 21
    • 39749093082 scopus 로고    scopus 로고
    • Folding of HLA-B27 subtypes is determined by the global effect of polymorphic residues and shows incomplete correspondence to ankylosing spondylitis
    • Galocha B, de Castro JA. Folding of HLA-B27 subtypes is determined by the global effect of polymorphic residues and shows incomplete correspondence to ankylosing spondylitis. Arthritis Rheum 2008; 58:401-12.
    • (2008) Arthritis Rheum , vol.58 , pp. 401-412
    • Galocha, B.1    de Castro, J.A.2
  • 23
    • 23444431837 scopus 로고    scopus 로고
    • HLA-B27 misfolding in transgenic rats is associated with activation of the unfolded protein response
    • Turner MJ, Sowders DP, DeLay ML et al. HLA-B27 misfolding in transgenic rats is associated with activation of the unfolded protein response. J Immunol 2005; 175:2438-48.
    • (2005) J Immunol , vol.175 , pp. 2438-2448
    • Turner, M.J.1    Sowders, D.P.2    DeLay, M.L.3
  • 24
    • 0025633436 scopus 로고
    • Spontaneous inflammatory disease in transgenic rats expressing HLA-B27 and human β2m: an animal model of HLA-B27-associated human disorders
    • Hammer RE, Maika SD, Richardson JA, Tang JP, Taurog JD. Spontaneous inflammatory disease in transgenic rats expressing HLA-B27 and human β2m: an animal model of HLA-B27-associated human disorders. Cell 1990; 63:1099-112.
    • (1990) Cell , vol.63 , pp. 1099-1112
    • Hammer, R.E.1    Maika, S.D.2    Richardson, J.A.3    Tang, J.P.4    Taurog, J.D.5
  • 26
    • 0041845075 scopus 로고    scopus 로고
    • Protein expression and peptide binding suggest unique and interacting functional roles for HLA-E, F, and G in maternal-placental immune recognition
    • Ishitani A, Sageshima N, Lee N, Dorofeeva N, Hatake K, Marquardt H, Geraghty DE. Protein expression and peptide binding suggest unique and interacting functional roles for HLA-E, F, and G in maternal-placental immune recognition. J Immunol 2003; 171:1376-84.
    • (2003) J Immunol , vol.171 , pp. 1376-1384
    • Ishitani, A.1    Sageshima, N.2    Lee, N.3    Dorofeeva, N.4    Hatake, K.5    Marquardt, H.6    Geraghty, D.E.7
  • 27
    • 35748955823 scopus 로고    scopus 로고
    • Intracellular cysteine residues in the tail of MHC class I proteins are crucial for extracellular recognition by leukocyte Ig-like receptor 1
    • Gruda R, Achdout H, Stern-Ginossar N et al. Intracellular cysteine residues in the tail of MHC class I proteins are crucial for extracellular recognition by leukocyte Ig-like receptor 1. J Immunol 2007; 179:3655-61.
    • (2007) J Immunol , vol.179 , pp. 3655-3661
    • Gruda, R.1    Achdout, H.2    Stern-Ginossar, N.3
  • 28
    • 0034866115 scopus 로고    scopus 로고
    • The truncated cytoplasmic tail of HLA-G serves a quality-control function in post-ER compartments
    • Park B, Lee S, Kim E, Chang S, Jin M, Ahn K. The truncated cytoplasmic tail of HLA-G serves a quality-control function in post-ER compartments. Immunity 2001; 15:213-24.
    • (2001) Immunity , vol.15 , pp. 213-224
    • Park, B.1    Lee, S.2    Kim, E.3    Chang, S.4    Jin, M.5    Ahn, K.6
  • 29
    • 0033583430 scopus 로고    scopus 로고
    • The transmembrane sequence of human histocompatibility leukocyte antigen (HLA)-C as a determinant in inhibition of a subset of natural killer cells
    • Davis DM, Mandelboim O, Luque I, Baba E, Boyson J, Strominger JL. The transmembrane sequence of human histocompatibility leukocyte antigen (HLA)-C as a determinant in inhibition of a subset of natural killer cells. J Exp Med 1999; 189:1265-74.
    • (1999) J Exp Med , vol.189 , pp. 1265-1274
    • Davis, D.M.1    Mandelboim, O.2    Luque, I.3    Baba, E.4    Boyson, J.5    Strominger, J.L.6
  • 31
    • 20044390568 scopus 로고    scopus 로고
    • Crystal structure of HLA-G: a nonclassical MHC class I molecule expressed at the fetal-maternal interface
    • Clements CS, Kjer-Nielsen L, Kostenko L et al. Crystal structure of HLA-G: a nonclassical MHC class I molecule expressed at the fetal-maternal interface. Proc Natl Acad Sci U S A 2005; 102:3360-5.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3360-3365
    • Clements, C.S.1    Kjer-Nielsen, L.2    Kostenko, L.3
  • 34
    • 34047170246 scopus 로고    scopus 로고
    • A commentary on gestational programming and functions of HLA-G in pregnancy
    • Hunt JS, Morales PJ, Pace JL, Fazleabas AT, Langat DK. A commentary on gestational programming and functions of HLA-G in pregnancy. Placenta 2007; 28(Suppl A):S57-63.
    • (2007) Placenta , vol.28 , Issue.SUPPL. A
    • Hunt, J.S.1    Morales, P.J.2    Pace, J.L.3    Fazleabas, A.T.4    Langat, D.K.5
  • 35
    • 0037058924 scopus 로고    scopus 로고
    • Disulfide bond-mediated dimerization of HLA-G on the cell surface
    • Boyson JE, Erskine R, Whitman MC et al. Disulfide bond-mediated dimerization of HLA-G on the cell surface. Proc Natl Acad Sci U S A 2002; 99:16180-5.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16180-16185
    • Boyson, J.E.1    Erskine, R.2    Whitman, M.C.3
  • 36
    • 80052241683 scopus 로고    scopus 로고
    • Ex vivo functional responses to HLA-G differ between blood and decidual NK cells
    • Apps R, Sharkey A, Gardner L et al. Ex vivo functional responses to HLA-G differ between blood and decidual NK cells. Mol Hum Reprod 2011; 17:577-86.
    • (2011) Mol Hum Reprod , vol.17 , pp. 577-586
    • Apps, R.1    Sharkey, A.2    Gardner, L.3
  • 37
    • 34447545481 scopus 로고    scopus 로고
    • A homodimeric complex of HLA-G on normal trophoblast cells modulates antigen-presenting cells via LILRB1
    • Apps R, Gardner L, Sharkey AM, Holmes N, Moffett A. A homodimeric complex of HLA-G on normal trophoblast cells modulates antigen-presenting cells via LILRB1. Eur J Immunol 2007; 37:1924-37.
    • (2007) Eur J Immunol , vol.37 , pp. 1924-1937
    • Apps, R.1    Gardner, L.2    Sharkey, A.M.3    Holmes, N.4    Moffett, A.5
  • 39
    • 0043205005 scopus 로고    scopus 로고
    • Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G
    • Shiroishi M, Tsumoto K, Amano K et al. Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G. Proc Natl Acad Sci U S A 2003; 100:8856-61.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8856-8861
    • Shiroishi, M.1    Tsumoto, K.2    Amano, K.3
  • 40
    • 0041845115 scopus 로고    scopus 로고
    • Complexes of HLA-G protein on the cell surface are important for leukocyte Ig-like receptor-1 function
    • Gonen-Gross T, Achdout H, Gazit R et al. Complexes of HLA-G protein on the cell surface are important for leukocyte Ig-like receptor-1 function. J Immunol 2003; 171:1343-51.
    • (2003) J Immunol , vol.171 , pp. 1343-1351
    • Gonen-Gross, T.1    Achdout, H.2    Gazit, R.3
  • 41
    • 26844481034 scopus 로고    scopus 로고
    • The CD85J/leukocyte inhibitory receptor-1 distinguishes between conformed and β2-microglobulin-free HLA-G molecules
    • Gonen-Gross T, Achdout H, Arnon TI et al. The CD85J/leukocyte inhibitory receptor-1 distinguishes between conformed and β2-microglobulin-free HLA-G molecules. J Immunol 2005; 175:4866-74.
    • (2005) J Immunol , vol.175 , pp. 4866-4874
    • Gonen-Gross, T.1    Achdout, H.2    Arnon, T.I.3
  • 43
    • 68849129712 scopus 로고    scopus 로고
    • Membrane vesicles as conveyors of immune responses
    • Thery C, Ostrowski M, Segura E. Membrane vesicles as conveyors of immune responses. Nat Rev Immunol 2009; 9:581-93.
    • (2009) Nat Rev Immunol , vol.9 , pp. 581-593
    • Thery, C.1    Ostrowski, M.2    Segura, E.3
  • 44
    • 84862942759 scopus 로고    scopus 로고
    • MHC class I dimer formation by alteration of the cellular redox environment and induction of apoptosis
    • Makhadiyeva D, Lam L, Moatari M, Vallance J, Zheng Y, Campbell EC, Powis SJ. MHC class I dimer formation by alteration of the cellular redox environment and induction of apoptosis. Immunology 2012; 135:133-9.
    • (2012) Immunology , vol.135 , pp. 133-139
    • Makhadiyeva, D.1    Lam, L.2    Moatari, M.3    Vallance, J.4    Zheng, Y.5    Campbell, E.C.6    Powis, S.J.7
  • 45
    • 79957819259 scopus 로고    scopus 로고
    • Expression of MHC class I dimers and ERAP1 in an ankylosing spondylitis patient cohort
    • Campbell EC, Fettke F, Bhat S, Morley KD, Powis SJ. Expression of MHC class I dimers and ERAP1 in an ankylosing spondylitis patient cohort. Immunology 2011; 133:379-85.
    • (2011) Immunology , vol.133 , pp. 379-385
    • Campbell, E.C.1    Fettke, F.2    Bhat, S.3    Morley, K.D.4    Powis, S.J.5


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