메뉴 건너뛰기




Volumn 61, Issue 1, 2013, Pages 161-167

Citrullination of TNF-α by peptidylarginine deiminases reduces its capacity to stimulate the production of inflammatory chemokines

Author keywords

Citrullination; Cytokine; IL 1 ; Posttranslational modification; TNF

Indexed keywords

GAMMA INTERFERON INDUCIBLE PROTEIN 10; INFLIXIMAB; INTERLEUKIN 1BETA; INTERLEUKIN 8; MONOCYTE CHEMOTACTIC PROTEIN 1; PROTEIN ARGININE DEIMINASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 84869862967     PISSN: 10434666     EISSN: 10960023     Source Type: Journal    
DOI: 10.1016/j.cyto.2012.09.011     Document Type: Article
Times cited : (27)

References (40)
  • 2
    • 53749083136 scopus 로고    scopus 로고
    • Regulation of chemokine activity by posttranslational modification
    • Mortier A., Van Damme J., Proost P. Regulation of chemokine activity by posttranslational modification. Pharmacol Ther 2008, 120:197-217.
    • (2008) Pharmacol Ther , vol.120 , pp. 197-217
    • Mortier, A.1    Van Damme, J.2    Proost, P.3
  • 3
    • 0033548086 scopus 로고    scopus 로고
    • I, Truncation of macrophage-derived chemokine by CD26/ dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction
    • Proost P., Struyf S., Schols D., Opdenakker G., Sozzani S., Allavena P., et al. I, Truncation of macrophage-derived chemokine by CD26/ dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction. J Biol Chem 1999, 274:3988-3993.
    • (1999) J Biol Chem , vol.274 , pp. 3988-3993
    • Proost, P.1    Struyf, S.2    Schols, D.3    Opdenakker, G.4    Sozzani, S.5    Allavena, P.6
  • 4
    • 79952102426 scopus 로고    scopus 로고
    • Effect of posttranslational processing on the in vitro and in vivo activity of chemokines
    • Mortier A., Gouwy M., Van Damme J., Proost P. Effect of posttranslational processing on the in vitro and in vivo activity of chemokines. Exp Cell Res 2010, 317:642-654.
    • (2010) Exp Cell Res , vol.317 , pp. 642-654
    • Mortier, A.1    Gouwy, M.2    Van Damme, J.3    Proost, P.4
  • 5
    • 51049113366 scopus 로고    scopus 로고
    • Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
    • Proost P., Loos T., Mortier A., Schutyser E., Gouwy M., Noppen S., et al. Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation. J Exp Med 2008, 205:2085-2097.
    • (2008) J Exp Med , vol.205 , pp. 2085-2097
    • Proost, P.1    Loos, T.2    Mortier, A.3    Schutyser, E.4    Gouwy, M.5    Noppen, S.6
  • 6
    • 53449087927 scopus 로고    scopus 로고
    • Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation
    • Loos T., Mortier A., Gouwy M., Ronsse I., Put W., Lenaerts J.P., et al. Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation. Blood 2008, 112:2648-2656.
    • (2008) Blood , vol.112 , pp. 2648-2656
    • Loos, T.1    Mortier, A.2    Gouwy, M.3    Ronsse, I.4    Put, W.5    Lenaerts, J.P.6
  • 7
    • 0242720407 scopus 로고    scopus 로고
    • PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
    • Vossenaar E.R., Zendman A.J., van Venrooij W.J., Pruijn G.J. PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. Bioessays 2003, 25:1106-1118.
    • (2003) Bioessays , vol.25 , pp. 1106-1118
    • Vossenaar, E.R.1    Zendman, A.J.2    van Venrooij, W.J.3    Pruijn, G.J.4
  • 8
    • 0029824853 scopus 로고    scopus 로고
    • Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin
    • Tarcsa E., Marekov L.N., Mei G., Melino G., Lee S.C., Steinert P.M. Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J Biol Chem 1996, 271:30709-30716.
    • (1996) J Biol Chem , vol.271 , pp. 30709-30716
    • Tarcsa, E.1    Marekov, L.N.2    Mei, G.3    Melino, G.4    Lee, S.C.5    Steinert, P.M.6
  • 9
    • 33745331328 scopus 로고    scopus 로고
    • Citrullination: a posttranslational modification in health and disease
    • Gyorgy B., Toth E., Tarcsa E., Falus A., Buzas E.I. Citrullination: a posttranslational modification in health and disease. Int J Biochem Cell Biol 2006, 38:1662-1677.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 1662-1677
    • Gyorgy, B.1    Toth, E.2    Tarcsa, E.3    Falus, A.4    Buzas, E.I.5
  • 10
    • 35748974228 scopus 로고    scopus 로고
    • Mechanisms of disease: genetics of rheumatoid arthritis-ethnic differences in disease-associated genes
    • Yamada R., Yamamoto K. Mechanisms of disease: genetics of rheumatoid arthritis-ethnic differences in disease-associated genes. Nat Clin Practice Rheumatol 2007, 3:644-650.
    • (2007) Nat Clin Practice Rheumatol , vol.3 , pp. 644-650
    • Yamada, R.1    Yamamoto, K.2
  • 11
    • 27744515706 scopus 로고    scopus 로고
    • Citrullinated proteins have increased immunogenicity and arthritogenicity and their presence in arthritic joints correlates with disease severity
    • Lundberg K., Nijenhuis S., Vossenaar E.R., Palmblad K., van Venrooij W.J., Klareskog L., et al. Citrullinated proteins have increased immunogenicity and arthritogenicity and their presence in arthritic joints correlates with disease severity. Arthritis Res Ther 2005, 7:R458-R467.
    • (2005) Arthritis Res Ther , vol.7
    • Lundberg, K.1    Nijenhuis, S.2    Vossenaar, E.R.3    Palmblad, K.4    van Venrooij, W.J.5    Klareskog, L.6
  • 12
    • 33645210449 scopus 로고    scopus 로고
    • Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope
    • Musse A.A., Boggs J.M., Harauz G. Deimination of membrane-bound myelin basic protein in multiple sclerosis exposes an immunodominant epitope. Proc Natl Acad Sci USA 2006, 103:4422-4427.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4422-4427
    • Musse, A.A.1    Boggs, J.M.2    Harauz, G.3
  • 15
    • 0033765449 scopus 로고    scopus 로고
    • Role of interleukin 1 and interleukin 1 receptor antagonist in the mediation of rheumatoid arthritis
    • Schiff M.H. Role of interleukin 1 and interleukin 1 receptor antagonist in the mediation of rheumatoid arthritis. Ann Rheum Dis 2000, 59(Suppl 1):i103-i108.
    • (2000) Ann Rheum Dis , vol.59 , Issue.SUPPL. 1
    • Schiff, M.H.1
  • 16
    • 36049041609 scopus 로고    scopus 로고
    • Peptidyl arginine deiminase type 2 (PAD-2) and PAD-4 but not PAD-1, PAD-3, and PAD-6 are expressed in rheumatoid arthritis synovium in close association with tissue inflammation
    • Foulquier C., Sebbag M., Clavel C., Chapuy-Regaud S., Al Badine R., Mechin M.C., et al. Peptidyl arginine deiminase type 2 (PAD-2) and PAD-4 but not PAD-1, PAD-3, and PAD-6 are expressed in rheumatoid arthritis synovium in close association with tissue inflammation. Arthritis Rheum 2007, 56:3541-3553.
    • (2007) Arthritis Rheum , vol.56 , pp. 3541-3553
    • Foulquier, C.1    Sebbag, M.2    Clavel, C.3    Chapuy-Regaud, S.4    Al Badine, R.5    Mechin, M.C.6
  • 17
    • 12344327644 scopus 로고    scopus 로고
    • Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis
    • Chang X., Yamada R., Suzuki A., Sawada T., Yoshino S., Tokuhiro S., et al. Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis. Rheumatology (Oxford) 2005, 44:40-50.
    • (2005) Rheumatology (Oxford) , vol.44 , pp. 40-50
    • Chang, X.1    Yamada, R.2    Suzuki, A.3    Sawada, T.4    Yoshino, S.5    Tokuhiro, S.6
  • 18
    • 0042667153 scopus 로고    scopus 로고
    • Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis
    • Suzuki A., Yamada R., Chang X., Tokuhiro S., Sawada T., Suzuki M., et al. Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis. Nat Genet 2003, 34:395-402.
    • (2003) Nat Genet , vol.34 , pp. 395-402
    • Suzuki, A.1    Yamada, R.2    Chang, X.3    Tokuhiro, S.4    Sawada, T.5    Suzuki, M.6
  • 20
    • 69249152923 scopus 로고    scopus 로고
    • Targeted analysis of protein citrullination using chemical modification and tandem mass spectrometry
    • Stensland M., Holm A., Kiehne A., Fleckenstein B. Targeted analysis of protein citrullination using chemical modification and tandem mass spectrometry. Rapid Commun Mass Spectrom 2009, 23:2754-2762.
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 2754-2762
    • Stensland, M.1    Holm, A.2    Kiehne, A.3    Fleckenstein, B.4
  • 21
    • 83455221107 scopus 로고    scopus 로고
    • Detection and quantification of citrullinated chemokines
    • Moelants E.A.V., Van Damme J., Proost P. Detection and quantification of citrullinated chemokines. PLoS ONE 2011, 6:e28976.
    • (2011) PLoS ONE , vol.6
    • Moelants, E.A.V.1    Van Damme, J.2    Proost, P.3
  • 22
    • 0024383261 scopus 로고
    • The chemotactic activity for granulocytes produced by virally infected fibroblasts is identical to monocyte-derived interleukin 8
    • Van Damme J., Decock B., Conings R., Lenaerts J.P., Opdenakker G., Billiau A. The chemotactic activity for granulocytes produced by virally infected fibroblasts is identical to monocyte-derived interleukin 8. Eur J Immunol 1989, 19:1189-1194.
    • (1989) Eur J Immunol , vol.19 , pp. 1189-1194
    • Van Damme, J.1    Decock, B.2    Conings, R.3    Lenaerts, J.P.4    Opdenakker, G.5    Billiau, A.6
  • 23
    • 0037241927 scopus 로고    scopus 로고
    • The CXC chemokine GCP-2/CXCL6 is predominantly induced in mesenchymal cells by interleukin-1beta and is down-regulated by interferon-gamma: comparison with interleukin-8/CXCL8
    • Wuyts A., Struyf S., Gijsbers K., Schutyser E., Put W., Conings R., et al. The CXC chemokine GCP-2/CXCL6 is predominantly induced in mesenchymal cells by interleukin-1beta and is down-regulated by interferon-gamma: comparison with interleukin-8/CXCL8. Lab Invest 2003, 83:23-34.
    • (2003) Lab Invest , vol.83 , pp. 23-34
    • Wuyts, A.1    Struyf, S.2    Gijsbers, K.3    Schutyser, E.4    Put, W.5    Conings, R.6
  • 24
    • 0242391978 scopus 로고    scopus 로고
    • Microbial toll-like receptor ligands differentially regulate CXCL10/IP-10 expression in fibroblasts and mononuclear leukocytes in synergy with IFN-gamma and provide a mechanism for enhanced synovial chemokine levels in septic arthritis
    • Proost P., Vynckier A.K., Mahieu F., Put W., Grillet B., Struyf S., et al. Microbial toll-like receptor ligands differentially regulate CXCL10/IP-10 expression in fibroblasts and mononuclear leukocytes in synergy with IFN-gamma and provide a mechanism for enhanced synovial chemokine levels in septic arthritis. Eur J Immunol 2003, 33:3146-3153.
    • (2003) Eur J Immunol , vol.33 , pp. 3146-3153
    • Proost, P.1    Vynckier, A.K.2    Mahieu, F.3    Put, W.4    Grillet, B.5    Struyf, S.6
  • 26
    • 78049416444 scopus 로고    scopus 로고
    • Modulation of RIP1 ubiquitylation and distribution by MeBS to sensitize cancer cells to tumor necrosis factor alpha-induced apoptosis
    • Kim S., Ohoka N., Okuhira K., Sai K., Nishimaki-Mogami T., Naito M. Modulation of RIP1 ubiquitylation and distribution by MeBS to sensitize cancer cells to tumor necrosis factor alpha-induced apoptosis. Cancer Sci 2010, 101:2425-2429.
    • (2010) Cancer Sci , vol.101 , pp. 2425-2429
    • Kim, S.1    Ohoka, N.2    Okuhira, K.3    Sai, K.4    Nishimaki-Mogami, T.5    Naito, M.6
  • 27
    • 33847725556 scopus 로고    scopus 로고
    • Simultaneous induction of apoptotic and survival signaling pathways in macrophage-like THP-1 cells by Shiga toxin 1
    • Lee S.Y., Cherla R.P., Tesh V.L. Simultaneous induction of apoptotic and survival signaling pathways in macrophage-like THP-1 cells by Shiga toxin 1. Infect Immun 2007, 75:1291-1302.
    • (2007) Infect Immun , vol.75 , pp. 1291-1302
    • Lee, S.Y.1    Cherla, R.P.2    Tesh, V.L.3
  • 29
    • 77956899749 scopus 로고    scopus 로고
    • 2-terminal region of CXCL5 by proteases or peptidylarginine deiminases (PAD) differently affects its biological activity
    • 2-terminal region of CXCL5 by proteases or peptidylarginine deiminases (PAD) differently affects its biological activity. J Biol Chem 2010, 285:29750-29759.
    • (2010) J Biol Chem , vol.285 , pp. 29750-29759
    • Mortier, A.1    Loos, T.2    Gouwy, M.3    Ronsse, I.4    Van Damme, J.5    Proost, P.6
  • 30
    • 70349636703 scopus 로고    scopus 로고
    • Citrullination of CXCL8 increases this chemokine's ability to mobilize neutrophils into the blood circulation
    • Loos T., Opdenakker G., Van Damme J., Proost P. Citrullination of CXCL8 increases this chemokine's ability to mobilize neutrophils into the blood circulation. Haematologica 2009, 94:1346-1353.
    • (2009) Haematologica , vol.94 , pp. 1346-1353
    • Loos, T.1    Opdenakker, G.2    Van Damme, J.3    Proost, P.4
  • 31
    • 55249084235 scopus 로고    scopus 로고
    • Citrullination: the loss of tolerance and development of autoimmunity in rheumatoid arthritis
    • Alivernini S., Fedele A.L., Cuoghi I., Tolusso B., Ferraccioli G. Citrullination: the loss of tolerance and development of autoimmunity in rheumatoid arthritis. Reumatismo 2008, 60:85-94.
    • (2008) Reumatismo , vol.60 , pp. 85-94
    • Alivernini, S.1    Fedele, A.L.2    Cuoghi, I.3    Tolusso, B.4    Ferraccioli, G.5
  • 32
    • 72149084899 scopus 로고    scopus 로고
    • Peptidylarginine deiminase 4 and citrullination in health and disease
    • Anzilotti C., Pratesi F., Tommasi C., Migliorini P. Peptidylarginine deiminase 4 and citrullination in health and disease. Autoimmun Rev 2010, 9:158-160.
    • (2010) Autoimmun Rev , vol.9 , pp. 158-160
    • Anzilotti, C.1    Pratesi, F.2    Tommasi, C.3    Migliorini, P.4
  • 33
    • 34249827580 scopus 로고    scopus 로고
    • Proteomic analysis of secreted proteins in early rheumatoid arthritis: anti-citrulline autoreactivity is associated with up regulation of proinflammatory cytokines
    • Hueber W., Tomooka B.H., Zhao X., Kidd B.A., Drijfhout J.W., Fries J.F., et al. Proteomic analysis of secreted proteins in early rheumatoid arthritis: anti-citrulline autoreactivity is associated with up regulation of proinflammatory cytokines. Ann Rheum Dis 2007, 66:712-719.
    • (2007) Ann Rheum Dis , vol.66 , pp. 712-719
    • Hueber, W.1    Tomooka, B.H.2    Zhao, X.3    Kidd, B.A.4    Drijfhout, J.W.5    Fries, J.F.6
  • 35
    • 29644431581 scopus 로고    scopus 로고
    • Immunological therapies for rheumatoid arthritis
    • Edwards C.J. Immunological therapies for rheumatoid arthritis. Brit Med Bull 2005, 73-74:71-82.
    • (2005) Brit Med Bull , pp. 71-82
    • Edwards, C.J.1
  • 36
    • 58149343265 scopus 로고    scopus 로고
    • Structure-function relationship of tumor necrosis factor (TNF) and its receptor interaction based on 3D structural analysis of a fully active TNFR1-selective TNF mutant
    • Mukai Y., Shibata H., Nakamura T., Yoshioka Y., Abe Y., Nomura T., et al. Structure-function relationship of tumor necrosis factor (TNF) and its receptor interaction based on 3D structural analysis of a fully active TNFR1-selective TNF mutant. J Mol Biol 2009, 385:1221-1229.
    • (2009) J Mol Biol , vol.385 , pp. 1221-1229
    • Mukai, Y.1    Shibata, H.2    Nakamura, T.3    Yoshioka, Y.4    Abe, Y.5    Nomura, T.6
  • 37
  • 39
    • 85047692516 scopus 로고    scopus 로고
    • Signalling pathways of the TNF superfamily: a double-edged sword
    • Aggarwal B.B. Signalling pathways of the TNF superfamily: a double-edged sword. Nat Rev Immunol 2003, 3:745-756.
    • (2003) Nat Rev Immunol , vol.3 , pp. 745-756
    • Aggarwal, B.B.1
  • 40
    • 0033452005 scopus 로고    scopus 로고
    • Regulated commitment of TNF receptor signaling: a molecular switch for death or activation
    • Pimentel-Muinos F.X., Seed B. Regulated commitment of TNF receptor signaling: a molecular switch for death or activation. Immunity 1999, 11:783-793.
    • (1999) Immunity , vol.11 , pp. 783-793
    • Pimentel-Muinos, F.X.1    Seed, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.