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Volumn 4, Issue 11, 2009, Pages

Immunoproteasome overexpression underlies the pathogenesis of thyroid oncocytes and primary hypothyroidism: Studies in humans and mice

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA INTERFERON; MAJOR HISTOCOMPATIBILITY ANTIGEN; PROTEASOME; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR LMP2; TRANSCRIPTION FACTOR LMP7; TRANSCRIPTOME; UNCLASSIFIED DRUG;

EID: 70849127013     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007857     Document Type: Article
Times cited : (27)

References (39)
  • 1
    • 0141819043 scopus 로고    scopus 로고
    • The epidemiology of autoimmune diseases
    • Cooper GS, Stroehla BC (2003) The epidemiology of autoimmune diseases. Autoimmun Rev 2: 119-125.
    • (2003) Autoimmun Rev , vol.2 , pp. 119-125
    • Cooper, G.S.1    Stroehla, B.C.2
  • 2
    • 14844282063 scopus 로고    scopus 로고
    • Karl Hurthle! Now, who was he?
    • Caturegli P, Ruggere C (2005) Karl Hurthle! Now, who was he? Thyroid 15: 121-123.
    • (2005) Thyroid , vol.15 , pp. 121-123
    • Caturegli, P.1    Ruggere, C.2
  • 4
    • 49449095164 scopus 로고    scopus 로고
    • The thyroid Hurthle (oncocytic) cell and its associated pathologic conditions: A surgical pathology and cytopathology review
    • Montone KT, Baloch ZW, LiVolsi VA (2008) The thyroid Hurthle (oncocytic) cell and its associated pathologic conditions: a surgical pathology and cytopathology review. Arch Pathol Lab Med 132: 1241-1250.
    • (2008) Arch Pathol Lab Med , vol.132 , pp. 1241-1250
    • Montone, K.T.1    Baloch, Z.W.2    LiVolsi, V.A.3
  • 6
    • 17144413358 scopus 로고    scopus 로고
    • Increased thyroidal fat and goitrous hypothyroidism induced by interferon-gamma
    • Kimura H, Kimura M, Westra WH, Rose NR, Caturegli P (2005) Increased thyroidal fat and goitrous hypothyroidism induced by interferon-gamma. Int J Exp Pathol 86: 97-106.
    • (2005) Int J Exp Pathol , vol.86 , pp. 97-106
    • Kimura, H.1    Kimura, M.2    Westra, W.H.3    Rose, N.R.4    Caturegli, P.5
  • 7
    • 59249084491 scopus 로고    scopus 로고
    • The proteasome: Overview of structure and functions
    • Tanaka K (2009) The proteasome: overview of structure and functions. Proc Jpn Acad Ser B Phys Biol Sci 85: 12-36.
    • (2009) Proc Jpn Acad Ser B Phys Biol Sci , vol.85 , pp. 12-36
    • Tanaka, K.1
  • 8
    • 3242771511 scopus 로고    scopus 로고
    • Generation of major histocompatibility complex class I antigens: Functional interplay between proteasomes and TPPII
    • Kloetzel PM (2004) Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII. Nat Immunol 5: 661-669.
    • (2004) Nat Immunol , vol.5 , pp. 661-669
    • Kloetzel, P.M.1
  • 9
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: A novel class of potent and effective antitumor agents
    • Adams J, Palombella VJ, Sausville EA, Johnson J, Destree A, et al. (1999) Proteasome inhibitors: a novel class of potent and effective antitumor agents. Cancer Res 59: 2615-2622.
    • (1999) Cancer Res , vol.59 , pp. 2615-2622
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3    Johnson, J.4    Destree, A.5
  • 10
    • 0342470536 scopus 로고    scopus 로고
    • LMP2 polymorphism is associated with extraspinal disease in HLA-B27 negative Caucasian and Mexican Mestizo patients with ankylosing spondylitis
    • Maksymowych WP, Tao S, Vaile J, Suarez-Almazor M, Ramos-Remus C, et al. (2000) LMP2 polymorphism is associated with extraspinal disease in HLA-B27 negative Caucasian and Mexican Mestizo patients with ankylosing spondylitis. J Rheumatol 27: 183-189.
    • (2000) J Rheumatol , vol.27 , pp. 183-189
    • Maksymowych, W.P.1    Tao, S.2    Vaile, J.3    Suarez-Almazor, M.4    Ramos-Remus, C.5
  • 11
    • 3242754268 scopus 로고    scopus 로고
    • Genes of the LMP/TAP cluster are associated with the human autoimmune disease vitiligo
    • Casp CB, She JX, McCormack WT (2003) Genes of the LMP/TAP cluster are associated with the human autoimmune disease vitiligo. Genes Immun 4: 492-499.
    • (2003) Genes Immun , vol.4 , pp. 492-499
    • Casp, C.B.1    She, J.X.2    McCormack, W.T.3
  • 12
    • 34548452605 scopus 로고    scopus 로고
    • Strong associations of psoriasis with antigen processing LMP and transport genes TAP differ by gender and phenotype
    • Kramer U, Illig T, Grune T, Krutmann J, Esser C (2007) Strong associations of psoriasis with antigen processing LMP and transport genes TAP differ by gender and phenotype. Genes Immun 8: 513-517.
    • (2007) Genes Immun , vol.8 , pp. 513-517
    • Kramer, U.1    Illig, T.2    Grune, T.3    Krutmann, J.4    Esser, C.5
  • 13
    • 0036790834 scopus 로고    scopus 로고
    • Circulating proteasomes are markers of cell damage and immunologic activity in autoimmune diseases
    • Egerer K, Kuckelkorn U, Rudolph PE, Ruckert JC, Dorner T, et al. (2002) Circulating proteasomes are markers of cell damage and immunologic activity in autoimmune diseases. J Rheumatol 29: 2045-2052.
    • (2002) J Rheumatol , vol.29 , pp. 2045-2052
    • Egerer, K.1    Kuckelkorn, U.2    Rudolph, P.E.3    Ruckert, J.C.4    Dorner, T.5
  • 14
    • 42949126300 scopus 로고    scopus 로고
    • Autoimmune reactivity against the 20S-proteasome includes immunosubunits LMP2 (beta1i), MECL1 (beta2i) and LMP7 (beta5i)
    • Scheffler S, Kuckelkorn U, Egerer K, Dorner T, Reiter K, et al. (2008) Autoimmune reactivity against the 20S-proteasome includes immunosubunits LMP2 (beta1i), MECL1 (beta2i) and LMP7 (beta5i). Rheumatology (Oxford) 47: 622-626.
    • (2008) Rheumatology (Oxford) , vol.47 , pp. 622-626
    • Scheffler, S.1    Kuckelkorn, U.2    Egerer, K.3    Dorner, T.4    Reiter, K.5
  • 15
    • 33646474855 scopus 로고    scopus 로고
    • Tissue-specific up-regulation of the proteasome subunit beta5i (LMP7) in Sjogren's syndrome
    • Egerer T, Martinez-Gamboa L, Dankof A, Stuhlmuller B, Dorner T, et al. (2006) Tissue-specific up-regulation of the proteasome subunit beta5i (LMP7) in Sjogren's syndrome. Arthritis Rheum 54: 1501-1508.
    • (2006) Arthritis Rheum , vol.54 , pp. 1501-1508
    • Egerer, T.1    Martinez-Gamboa, L.2    Dankof, A.3    Stuhlmuller, B.4    Dorner, T.5
  • 16
    • 33646471043 scopus 로고    scopus 로고
    • Immunoproteasome subunit LMP2 expression is deregulated in Sjogren's syndrome but not in other autoimmune disorders
    • Krause S, Kuckelkorn U, Dorner T, Burmester GR, Feist E, et al. (2006) Immunoproteasome subunit LMP2 expression is deregulated in Sjogren's syndrome but not in other autoimmune disorders. Ann Rheum Dis 65: 1021-1027.
    • (2006) Ann Rheum Dis , vol.65 , pp. 1021-1027
    • Krause, S.1    Kuckelkorn, U.2    Dorner, T.3    Burmester, G.R.4    Feist, E.5
  • 17
    • 0033499621 scopus 로고    scopus 로고
    • NOD mice are defective in proteasome production and activation of NF-kappaB
    • Hayashi T, Faustman D (1999) NOD mice are defective in proteasome production and activation of NF-kappaB. Mol Cell Biol 19: 8646-8659.
    • (1999) Mol Cell Biol , vol.19 , pp. 8646-8659
    • Hayashi, T.1    Faustman, D.2
  • 18
    • 0000181420 scopus 로고    scopus 로고
    • Reply to 'LMP2 expression and proteasome activity in NOD mice'
    • Hayashi T, Kodama S, Faustman DL (2000) Reply to 'LMP2 expression and proteasome activity in NOD mice'. Nat Med 6: 1065-1066.
    • (2000) Nat Med , vol.6 , pp. 1065-1066
    • Hayashi, T.1    Kodama, S.2    Faustman, D.L.3
  • 20
    • 0033782756 scopus 로고    scopus 로고
    • LMP2 expression and proteasome activity in NOD mice
    • author reply 1065-1066
    • Runnels HA, Watkins WA, Monaco JJ (2000) LMP2 expression and proteasome activity in NOD mice. Nat Med 6: 1064-1065; author reply 1065-1066.
    • (2000) Nat Med , vol.6 , pp. 1064-1065
    • Runnels, H.A.1    Watkins, W.A.2    Monaco, J.J.3
  • 21
    • 8544272515 scopus 로고    scopus 로고
    • Proteasome subunits, low-molecular-mass polypeptides 2 and 7 are hyperexpressed by target cells in autoimmune thyroid disease but not in insulin-dependent diabetes mellitus: Implications for autoimmunity
    • Vives-Pi M, Vargas F, James RF, Trowsdale J, Costa M, et al. (1997) Proteasome subunits, low-molecular-mass polypeptides 2 and 7 are hyperexpressed by target cells in autoimmune thyroid disease but not in insulin-dependent diabetes mellitus: implications for autoimmunity. Tissue Antigens 50: 153-163.
    • (1997) Tissue Antigens , vol.50 , pp. 153-163
    • Vives-Pi, M.1    Vargas, F.2    James, R.F.3    Trowsdale, J.4    Costa, M.5
  • 22
    • 0031973736 scopus 로고    scopus 로고
    • Immunoproteasome assembly: Cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits
    • Griffin TA, Nandi D, Cruz M, Fehling HJ, Kaer LV, et al. (1998) Immunoproteasome assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits. J Exp Med 187: 97-104.
    • (1998) J Exp Med , vol.187 , pp. 97-104
    • Griffin, T.A.1    Nandi, D.2    Cruz, M.3    Fehling, H.J.4    Kaer, L.V.5
  • 23
    • 0030793290 scopus 로고    scopus 로고
    • The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome
    • Groettrup M, Standera S, Stohwasser R, Kloetzel PM (1997) The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome. Proc Natl Acad Sci U S A 94: 8970-8975.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8970-8975
    • Groettrup, M.1    Standera, S.2    Stohwasser, R.3    Kloetzel, P.M.4
  • 24
    • 0036181371 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor PS-341
    • Adams J (2002) Development of the proteasome inhibitor PS-341. Oncologist 7: 9-16.
    • (2002) Oncologist , vol.7 , pp. 9-16
    • Adams, J.1
  • 26
    • 55249102985 scopus 로고    scopus 로고
    • Dual inhibition of proteasomal and lysosomal proteolysis ameliorates autoimmune central nervous system inflammation
    • Fissolo N, Kraus M, Reich M, Ayturan M, Overkleeft H, et al. (2008) Dual inhibition of proteasomal and lysosomal proteolysis ameliorates autoimmune central nervous system inflammation. Eur J Immunol 38: 2401-2411.
    • (2008) Eur J Immunol , vol.38 , pp. 2401-2411
    • Fissolo, N.1    Kraus, M.2    Reich, M.3    Ayturan, M.4    Overkleeft, H.5
  • 27
    • 46749088320 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib depletes plasma cells and protects mice with lupus-like disease from nephritis
    • Neubert K, Meister S, Moser K, Weisel F, Maseda D, et al. (2008) The proteasome inhibitor bortezomib depletes plasma cells and protects mice with lupus-like disease from nephritis. Nat Med 14: 748-755.
    • (2008) Nat Med , vol.14 , pp. 748-755
    • Neubert, K.1    Meister, S.2    Moser, K.3    Weisel, F.4    Maseda, D.5
  • 28
    • 66549099025 scopus 로고    scopus 로고
    • Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors
    • Kuhn DJ, Hunsucker SA, Chen Q, Voorhees PM, Orlowski M, et al. (2009) Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors. Blood 113: 4667-4676.
    • (2009) Blood , vol.113 , pp. 4667-4676
    • Kuhn, D.J.1    Hunsucker, S.A.2    Chen, Q.3    Voorhees, P.M.4    Orlowski, M.5
  • 29
    • 22444449129 scopus 로고    scopus 로고
    • The proteasome inhibitor MLN-273 blocks exoerythrocytic and erythrocytic development of Plasmodium parasites
    • Lindenthal C, Weich N, Chia YS, Heussler V, Klinkert MQ (2005) The proteasome inhibitor MLN-273 blocks exoerythrocytic and erythrocytic development of Plasmodium parasites. Parasitology 131: 37-44.
    • (2005) Parasitology , vol.131 , pp. 37-44
    • Lindenthal, C.1    Weich, N.2    Chia, Y.S.3    Heussler, V.4    Klinkert, M.Q.5
  • 30
    • 33645053287 scopus 로고    scopus 로고
    • Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate
    • Hu G, Lin G, Wang M, Dick L, Xu RM, et al. (2006) Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate. Mol Microbiol 59: 1417-1428.
    • (2006) Mol Microbiol , vol.59 , pp. 1417-1428
    • Hu, G.1    Lin, G.2    Wang, M.3    Dick, L.4    Xu, R.M.5
  • 31
    • 34548266210 scopus 로고    scopus 로고
    • Localized treatment with a novel FDA-approved proteasome inhibitor blocks the degradation of dystrophin and dystrophin-associated proteins in mdx mice
    • Bonuccelli G, Sotgia F, Capozza F, Gazzerro E, Minetti C, et al. (2007) Localized treatment with a novel FDA-approved proteasome inhibitor blocks the degradation of dystrophin and dystrophin-associated proteins in mdx mice. Cell Cycle 6: 1242-1248.
    • (2007) Cell Cycle , vol.6 , pp. 1242-1248
    • Bonuccelli, G.1    Sotgia, F.2    Capozza, F.3    Gazzerro, E.4    Minetti, C.5
  • 32
    • 20044393709 scopus 로고    scopus 로고
    • Effects of proteasome inhibition on the kidney in experimental hypercholesterolemia
    • Chade AR, Herrmann J, Zhu X, Krier JD, Lerman A, et al. (2005) Effects of proteasome inhibition on the kidney in experimental hypercholesterolemia. J Am Soc Nephrol 16: 1005-1012.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 1005-1012
    • Chade, A.R.1    Herrmann, J.2    Zhu, X.3    Krier, J.D.4    Lerman, A.5
  • 33
    • 37349091467 scopus 로고    scopus 로고
    • Targeting proteasome worsens atherosclerosis
    • Fukai T (2007) Targeting proteasome worsens atherosclerosis. Circ Res 101: 859-861.
    • (2007) Circ Res , vol.101 , pp. 859-861
    • Fukai, T.1
  • 34
    • 37349073383 scopus 로고    scopus 로고
    • Chronic proteasome inhibition contributes to coronary atherosclerosis
    • Herrmann J, Saguner AM, Versari D, Peterson TE, Chade A, et al. (2007) Chronic proteasome inhibition contributes to coronary atherosclerosis. Circ Res 101: 865-874.
    • (2007) Circ Res , vol.101 , pp. 865-874
    • Herrmann, J.1    Saguner, A.M.2    Versari, D.3    Peterson, T.E.4    Chade, A.5
  • 35
    • 39449129380 scopus 로고    scopus 로고
    • Targeting of the proteasome worsens atherosclerosis?
    • Ludwig A, Meiners S (2008) Targeting of the proteasome worsens atherosclerosis? Circ Res 102: e37.
    • (2008) Circ Res , vol.102
    • Ludwig, A.1    Meiners, S.2
  • 36
    • 45549094766 scopus 로고    scopus 로고
    • Update on thyroid cancer
    • Benvenga S (2008) Update on thyroid cancer. Horm Metab Res 40: 323-328.
    • (2008) Horm Metab Res , vol.40 , pp. 323-328
    • Benvenga, S.1
  • 37
    • 23244457800 scopus 로고    scopus 로고
    • Immunoproteasome-deficient mice mount largely normal CD8+ T cell responses to lymphocytic choriomeningitis virus infection and DNA vaccination
    • Nussbaum AK, Rodriguez-Carreno MP, Benning N, Botten J, Whitton JL (2005) Immunoproteasome-deficient mice mount largely normal CD8+ T cell responses to lymphocytic choriomeningitis virus infection and DNA vaccination. J Immunol 175: 1153-1160.
    • (2005) J Immunol , vol.175 , pp. 1153-1160
    • Nussbaum, A.K.1    Rodriguez-Carreno, M.P.2    Benning, N.3    Botten, J.4    Whitton, J.L.5
  • 38
    • 0030024563 scopus 로고    scopus 로고
    • Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease
    • Durbin JE, Hackenmiller R, Simon MC, Levy DE (1996) Targeted disruption of the mouse Stat1 gene results in compromised innate immunity to viral disease. Cell 84: 443-450.
    • (1996) Cell , vol.84 , pp. 443-450
    • Durbin, J.E.1    Hackenmiller, R.2    Simon, M.C.3    Levy, D.E.4


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