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Volumn 14, Issue 6, 2009, Pages 662-666

Proteasome inhibition for antibody-mediated rejection

Author keywords

Bortezomib; Humoral rejection; Proteasome inhibition

Indexed keywords

BORTEZOMIB; HLA ANTIBODY; HLA ANTIGEN; IMMUNOGLOBULIN; LACTACYSTIN BETA LACTONE; PROTEASOME; PROTEASOME INHIBITOR; RITUXIMAB;

EID: 74349101176     PISSN: 10872418     EISSN: 15317013     Source Type: Journal    
DOI: 10.1097/MOT.0b013e328330f304     Document Type: Review
Times cited : (80)

References (29)
  • 1
    • 33846185024 scopus 로고    scopus 로고
    • The effect of desensitization protocols on human splenic B-cell populations in vivo
    • Ramos EJ, Pollinger HS, Stegall MD, et al. The effect of desensitization protocols on human splenic B-cell populations in vivo. Am J Transplant 2007; 7:402-407.
    • (2007) Am J Transplant , vol.7 , pp. 402-407
    • Ramos, E.J.1    Pollinger, H.S.2    Stegall, M.D.3
  • 2
    • 65249160252 scopus 로고    scopus 로고
    • Reducing de novo donor-specific antibody levels during acute rejection diminishes renal allograft loss
    • Everly MJ, Everly JJ, Arend LJ, et al. Reducing de novo donor-specific antibody levels during acute rejection diminishes renal allograft loss. Am J Transplant 2009; 9:1-9.
    • (2009) Am J Transplant , vol.9 , pp. 1-9
    • Everly, M.J.1    Everly, J.J.2    Arend, L.J.3
  • 3
    • 58849136282 scopus 로고    scopus 로고
    • Bortezomib provides effective therapy for antibody-and cell-mediated acute rejection
    • Everly MJ, Everly JJ, Susskind B, et al. Bortezomib provides effective therapy for antibody-and cell-mediated acute rejection. Transplantation 2008; 86:1754-1761.
    • (2008) Transplantation , vol.86 , pp. 1754-1761
    • Everly, M.J.1    Everly, J.J.2    Susskind, B.3
  • 4
    • 58049200722 scopus 로고    scopus 로고
    • Proteasome inhibition causes apoptosis of normal human plasma cells preventing alloantibody production
    • Perry DK, Burns JM, Pollinger HS, et al. Proteasome inhibition causes apoptosis of normal human plasma cells preventing alloantibody production. Am J Transplant 2009; 9:201-209.
    • (2009) Am J Transplant , vol.9 , pp. 201-209
    • Perry, D.K.1    Burns, J.M.2    Pollinger, H.S.3
  • 5
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae
    • Lee DH, Goldberg AL. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae. J Biol Chem 1996; 271:27280-27284.
    • (1996) J Biol Chem , vol.271 , pp. 27280-27284
    • Lee, D.H.1    Goldberg, A.L.2
  • 6
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class i molecules
    • Rock KL, Gramm C, Rothstein L, et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994; 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3
  • 7
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature 2003; 426:895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 8
    • 0036483901 scopus 로고    scopus 로고
    • Deadly encounter: Ubiquitin meets apoptosis
    • Jesenberger V, Jentsch S. Deadly encounter: Ubiquitin meets apoptosis. Nat Rev Mol Cell Biol 2002; 3:112-121.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 112-121
    • Jesenberger, V.1    Jentsch, S.2
  • 9
    • 0036678959 scopus 로고    scopus 로고
    • Role and function of the 26S proteasome in proliferation and apoptosis
    • Naujokat C, Hoffmann S. Role and function of the 26S proteasome in proliferation and apoptosis. Lab Invest 2002; 82:965-980.
    • (2002) Lab Invest , vol.82 , pp. 965-980
    • Naujokat, C.1    Hoffmann, S.2
  • 10
    • 0242344011 scopus 로고    scopus 로고
    • The role of ubiquitin-proteasome pathway in oncogenic signaling
    • Fuchs SY. The role of ubiquitin-proteasome pathway in oncogenic signaling. Cancer Biol Ther 2002; 1:337-341.
    • (2002) Cancer Biol Ther , vol.1 , pp. 337-341
    • Fuchs, S.Y.1
  • 11
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani M, Tansey WP. How the ubiquitin-proteasome system controls transcription. Nat Rev Mol Cell Biol 2003; 4:192-201.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 12
    • 0346655115 scopus 로고    scopus 로고
    • Regulated ubiquitination of proteins in GPCR-initiated signaling pathways
    • Wojcikiewicz RJ. Regulated ubiquitination of proteins in GPCR-initiated signaling pathways. Trends Pharmacol Sci 2004; 25:35-41.
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 35-41
    • Wojcikiewicz, R.J.1
  • 13
    • 1042278905 scopus 로고    scopus 로고
    • Proteasome and peptidase function in MHCclass-I-mediated antigen presentation
    • Kloetzel PM, Ossendorp F. Proteasome and peptidase function in MHCclass-I-mediated antigen presentation. Curr Opin Immunol 2004; 16:76-81.
    • (2004) Curr Opin Immunol , vol.16 , pp. 76-81
    • Kloetzel, P.M.1    Ossendorp, F.2
  • 14
    • 33645541393 scopus 로고    scopus 로고
    • Degrade to create: Developmental requirements for ubiquitin-mediated proteolysis during early C. elegans embryogenesis
    • Bowerman B, Kurz T. Degrade to create: Developmental requirements for ubiquitin-mediated proteolysis during early C. elegans embryogenesis. Development 2006; 133:773-784.
    • (2006) Development , vol.133 , pp. 773-784
    • Bowerman, B.1    Kurz, T.2
  • 15
    • 0037569481 scopus 로고    scopus 로고
    • Proteasome inhibition: A new antiinflammatory strategy
    • Elliott PJ, Zollner TM, Boehncke WH. Proteasome inhibition: A new antiinflammatory strategy. J Mol Med 2003; 81:235-245.
    • (2003) J Mol Med , vol.81 , pp. 235-245
    • Elliott, P.J.1    Zollner, T.M.2    Boehncke, W.H.3
  • 16
    • 0035123105 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis of vertebrate G1-and S-phase regulators
    • Yew PR. Ubiquitin-mediated proteolysis of vertebrate G1-and S-phase regulators. J Cell Physiol 2001; 187:1-10.
    • (2001) J Cell Physiol , vol.187 , pp. 1-10
    • Yew, P.R.1
  • 17
    • 33750466230 scopus 로고    scopus 로고
    • Introduction to NF-kappaB: Players, pathways, perspectives
    • Gilmore TD. Introduction to NF-kappaB: Players, pathways, perspectives. Oncogene 2006; 25:6680-6684.
    • (2006) Oncogene , vol.25 , pp. 6680-6684
    • Gilmore, T.D.1
  • 18
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 2000; 150:887-894.
    • (2000) J Cell Biol , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 19
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida H, Matsui T, Yamamoto A, et al. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001; 107:881-891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3
  • 20
    • 21244462014 scopus 로고    scopus 로고
    • BH3-only BIK regulates BAX,BAK-dependent release of Ca2+ from endoplasmic reticulum stores and mitochondrial apoptosis during stress-induced cell death
    • Mathai JP, Germain M, Shore GC. BH3-only BIK regulates BAX,BAK-dependent release of Ca2+ from endoplasmic reticulum stores and mitochondrial apoptosis during stress-induced cell death. J Biol Chem 2005; 280:23829-23836.
    • (2005) J Biol Chem , vol.280 , pp. 23829-23836
    • Mathai, J.P.1    Germain, M.2    Shore, G.C.3
  • 21
    • 68449096176 scopus 로고    scopus 로고
    • Dysregulation of unfolded protein response partially underlies proapoptotic activity of bortezomib in multiple myeloma cells
    • Dong H, Chen L, Chen X, et al. Dysregulation of unfolded protein response partially underlies proapoptotic activity of bortezomib in multiple myeloma cells. Leuk Lymphoma 2009; 50:974-984.
    • (2009) Leuk Lymphoma , vol.50 , pp. 974-984
    • Dong, H.1    Chen, L.2    Chen, X.3
  • 22
    • 53349101501 scopus 로고    scopus 로고
    • Caspase-2 functions upstream of mitochondria in endoplasmic reticulum stress-induced apoptosis by bortezomib in human myeloma cells
    • Gu H, Chen X, Gao G, Dong H. Caspase-2 functions upstream of mitochondria in endoplasmic reticulum stress-induced apoptosis by bortezomib in human myeloma cells. Mol Cancer Ther 2008; 7:2298-2307.
    • (2008) Mol Cancer Ther , vol.7 , pp. 2298-2307
    • Gu, H.1    Chen, X.2    Gao, G.3    Dong, H.4
  • 23
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng EA, Carlson LM, Gutman DM, et al. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 2006; 107:4907-4916.
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3
  • 24
    • 0036870323 scopus 로고    scopus 로고
    • On the role of proteasomes in cell biology and proteasome inhibition as a novel frontier in the development of immunosuppressants
    • Wu J. On the role of proteasomes in cell biology and proteasome inhibition as a novel frontier in the development of immunosuppressants. Am J Transplant 2002; 2:904-912.
    • (2002) Am J Transplant , vol.2 , pp. 904-912
    • Wu, J.1
  • 25
    • 13044316560 scopus 로고    scopus 로고
    • Role of the proteasome and NF-kappaB in Streptococcal cell wall-induced polyarthritis
    • Palombella VJ, Conner EM, Fuseler JW, et al. Role of the proteasome and NF-kappaB in Streptococcal cell wall-induced polyarthritis. Proc Natl Acad Sci U S A 1998; 95:15671-15676.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15671-15676
    • Palombella, V.J.1    Conner, E.M.2    Fuseler, J.W.3
  • 26
    • 0033863764 scopus 로고    scopus 로고
    • Treatment of established relapsing experimental autoimmune encephalomyelitis with the proteasome inhibitor PS-519
    • Vanderlugt CL, Rahbe SM, Elliott PJ, et al. Treatment of established relapsing experimental autoimmune encephalomyelitis with the proteasome inhibitor PS-519. J Autoimmun 2000; 14:205-211.
    • (2000) J Autoimmun , vol.14 , pp. 205-211
    • Vanderlugt, C.L.1    Rahbe, S.M.2    Elliott, P.J.3
  • 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, et al. The proteasome inhibitor bortezomib depletes plasma cells and protects mice with lupus-like disease from nephritis. Nat Med 2008; 14:748-755.
    • (2008) Nat Med , vol.14 , pp. 748-755
    • Neubert, K.1    Meister, S.2    Moser, K.3
  • 28
    • 74349084890 scopus 로고    scopus 로고
    • Bortezomib treatment for refractory acute humoral rejection: Intermediate results
    • Abstract 462
    • Walsh RC, Everly JJ, Everly MJ, et al. Bortezomib treatment for refractory acute humoral rejection: Intermediate results. Am J Transpl 2009; 9 (s2):189-383. [Abstract 462].
    • (2009) Am J Transpl , vol.9 , Issue.S2 , pp. 189-383
    • Walsh, R.C.1    Everly, J.J.2    Everly, M.J.3
  • 29
    • 67649586605 scopus 로고    scopus 로고
    • Abrogation of anti-HLA antibodies via proteasome inhibition
    • Trivedi HL, Terasaki PI, Feroz A, et al. Abrogation of anti-HLA antibodies via proteasome inhibition. Transplantation 2009; 87:1555-1561.
    • (2009) Transplantation , vol.87 , pp. 1555-1561
    • Trivedi, H.L.1    Terasaki, P.I.2    Feroz, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.