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Volumn 232, Issue 2, 2007, Pages 195-203

Beneficial effects of treatment with transglutaminase inhibitor cystamine on macrophage response in NZB/W F1 mice

Author keywords

Cystamine; Matrix metalloproteinase (MMP); Systemic lupus erythematosus (SLE); Transglutaminase 2 (TG2)

Indexed keywords

CANCER GROWTH FACTOR; CARDIOLIPIN ANTIBODY; CYSTAMINE; GELATINASE B; MESSENGER RNA; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TUMOR NECROSIS FACTOR ALPHA;

EID: 33846846255     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (13)

References (43)
  • 1
    • 0001404232 scopus 로고
    • An overview of the pathogenesis of systemic lupus erythematosus
    • Wallace DJ, Hahn BH, Eds, Philadelphia: Williams and Wilkins, pp
    • Hahn BH. An overview of the pathogenesis of systemic lupus erythematosus. In: Wallace DJ, Hahn BH, Eds. Dubois' Lupus Erythematosus. Philadelphia: Williams and Wilkins, pp69-76, 1993.
    • (1993) Dubois' Lupus Erythematosus , pp. 69-76
    • Hahn, B.H.1
  • 2
    • 0002905362 scopus 로고    scopus 로고
    • Systemic lupus erythematosus pathogenesis
    • Koopman WJ, Ed, Birmingham, AL: William and Wilkins, pp
    • Winchester RJ. Systemic lupus erythematosus pathogenesis. In: Koopman WJ, Ed. Arthritis and Allied Conditions. Birmingham, AL: William and Wilkins, pp1361-1391, 1996.
    • (1996) Arthritis and Allied Conditions , pp. 1361-1391
    • Winchester, R.J.1
  • 3
    • 0037668545 scopus 로고    scopus 로고
    • Pathogenesis of systemic lupus erythematosus
    • Mok CC, Lau CS. Pathogenesis of systemic lupus erythematosus. J Clin Pathol 56:481-490, 2003.
    • (2003) J Clin Pathol , vol.56 , pp. 481-490
    • Mok, C.C.1    Lau, C.S.2
  • 4
    • 13444266045 scopus 로고    scopus 로고
    • Cytokine expression in lupus kidneys
    • Aringer M, Smolen JS. Cytokine expression in lupus kidneys. Lupus 14:13-18, 2005.
    • (2005) Lupus , vol.14 , pp. 13-18
    • Aringer, M.1    Smolen, J.S.2
  • 7
    • 33746368389 scopus 로고    scopus 로고
    • Partial construction of apoptotic pathway in PBMC obtained from active SLE patients and the significance of plasma TNF-alpha on this pathway
    • Jan 4
    • Pitidhammabhorn D, Kantachuvesiri S, Totemchokchyakarn K, Kitiyanant Y, Ubol S. Partial construction of apoptotic pathway in PBMC obtained from active SLE patients and the significance of plasma TNF-alpha on this pathway. Clin Rheumatol Jan 4:1-10, 2006.
    • (2006) Clin Rheumatol , pp. 1-10
    • Pitidhammabhorn, D.1    Kantachuvesiri, S.2    Totemchokchyakarn, K.3    Kitiyanant, Y.4    Ubol, S.5
  • 8
    • 0034674770 scopus 로고    scopus 로고
    • GTP binding and signaling by Gh/transglutaminase II involves distinct residues in a unique GTP-binding pocket
    • Iismaa SE, Wu MJ, Nanda N, Church WB, Graham RM. GTP binding and signaling by Gh/transglutaminase II involves distinct residues in a unique GTP-binding pocket. J Biol Chem 275:18259-18265, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 18259-18265
    • Iismaa, S.E.1    Wu, M.J.2    Nanda, N.3    Church, W.B.4    Graham, R.M.5
  • 9
    • 0035872859 scopus 로고    scopus 로고
    • Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2
    • Singh US, Kunar MT, Kao YL, Baker KM. Role of transglutaminase II in retinoic acid-induced activation of RhoA-associated kinase-2. EMBO J 20:2413-2423, 2001.
    • (2001) EMBO J , vol.20 , pp. 2413-2423
    • Singh, U.S.1    Kunar, M.T.2    Kao, Y.L.3    Baker, K.M.4
  • 10
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: An enigmatic enzyme with diverse functions
    • Fesus L, Piacentini M. Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem Sci 27:534-539, 2002.
    • (2002) Trends Biochem Sci , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 11
    • 20444363472 scopus 로고    scopus 로고
    • Transglutaminase 2 in the balance of cell death and survival
    • Fesus L, Szondy Z. Transglutaminase 2 in the balance of cell death and survival. FEBS Lett 579:3297-3302, 2005.
    • (2005) FEBS Lett , vol.579 , pp. 3297-3302
    • Fesus, L.1    Szondy, Z.2
  • 13
    • 0033607671 scopus 로고    scopus 로고
    • Inhibition of "tissue" transglutaminase increases cell survival by preventing apoptosis
    • Oliverio S, Amendola A, Rodolfo C, Spinedi A, Piacentini M. Inhibition of "tissue" transglutaminase increases cell survival by preventing apoptosis. J Biol Chem 274:34123-34128, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 34123-34128
    • Oliverio, S.1    Amendola, A.2    Rodolfo, C.3    Spinedi, A.4    Piacentini, M.5
  • 14
    • 18944366339 scopus 로고    scopus 로고
    • Transglutaminase type II is a key element in the regulation of the anti-inflammatory response elicited by apoptotic cell engulfment
    • Falasca L, Iadevaia V, Ciccosanti F, Melino G, Serafino A, Piacentini M. Transglutaminase type II is a key element in the regulation of the anti-inflammatory response elicited by apoptotic cell engulfment. J Immunol 174:7330-7340, 2005.
    • (2005) J Immunol , vol.174 , pp. 7330-7340
    • Falasca, L.1    Iadevaia, V.2    Ciccosanti, F.3    Melino, G.4    Serafino, A.5    Piacentini, M.6
  • 15
    • 0030028043 scopus 로고    scopus 로고
    • Matrix metalloproteinases and immunity
    • Goetzl EJ, Banda MJ, Leppert D. Matrix metalloproteinases and immunity. J Immunol 156:1-4, 1996.
    • (1996) J Immunol , vol.156 , pp. 1-4
    • Goetzl, E.J.1    Banda, M.J.2    Leppert, D.3
  • 16
    • 0036126735 scopus 로고    scopus 로고
    • Activity of matrix metalloproteinase-9 is elevated in sera of patients with systemic lupus erythematosus
    • Faber-Elmann A, Sthoeger Z, Tcherniack A, Dayan M, Mozes E. Activity of matrix metalloproteinase-9 is elevated in sera of patients with systemic lupus erythematosus. Clin Exp Immunol 127:393-398, 2002.
    • (2002) Clin Exp Immunol , vol.127 , pp. 393-398
    • Faber-Elmann, A.1    Sthoeger, Z.2    Tcherniack, A.3    Dayan, M.4    Mozes, E.5
  • 17
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart HE, Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A 87:5578-5582, 1990.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 18
    • 0033532205 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion
    • Ramos-DeSimone N, Hahn-Dantona E, Sipley J, Nagase H, French DL, Quigley JP. Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion. J Biol Chem 274:13066-13076, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 13066-13076
    • Ramos-DeSimone, N.1    Hahn-Dantona, E.2    Sipley, J.3    Nagase, H.4    French, D.L.5    Quigley, J.P.6
  • 19
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Effectors of development and normal physiology
    • Vu TH, Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev 14:2123-2133, 2000.
    • (2000) Genes Dev , vol.14 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 21
    • 0018816617 scopus 로고
    • Transglutaminases
    • Folk JE. Transglutaminases. Annu Rev Biochem 49:517-531, 1980.
    • (1980) Annu Rev Biochem , vol.49 , pp. 517-531
    • Folk, J.E.1
  • 23
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew K, Dinakarpandian D, Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta 1477:267-283, 2000.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 26
    • 0037423204 scopus 로고    scopus 로고
    • Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders
    • Lesort M, Lee M, Tucholski J, Johnson GV. Cystamine inhibits caspase activity. Implications for the treatment of polyglutamine disorders. J Biol Chem 278:3825-3830, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 3825-3830
    • Lesort, M.1    Lee, M.2    Tucholski, J.3    Johnson, G.V.4
  • 27
    • 0036172346 scopus 로고    scopus 로고
    • Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine
    • Karpuj MV, Becher MW, Springer JE, Chabas D, Youssef S, Pedotti R, Mitchell D, Steinman L. Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine. Nat Med 8:143-149, 2002.
    • (2002) Nat Med , vol.8 , pp. 143-149
    • Karpuj, M.V.1    Becher, M.W.2    Springer, J.E.3    Chabas, D.4    Youssef, S.5    Pedotti, R.6    Mitchell, D.7    Steinman, L.8
  • 28
    • 0028070650 scopus 로고
    • Purification and partial biochemical characterization of a Mycoplasma fermentans-derived substance that activates macrophages to release nitric oxide, tumor necrosis factor, and interleukin-6
    • Muhlradt PF, Frisch M. Purification and partial biochemical characterization of a Mycoplasma fermentans-derived substance that activates macrophages to release nitric oxide, tumor necrosis factor, and interleukin-6. Infect Immun 62:3801-3807, 1994.
    • (1994) Infect Immun , vol.62 , pp. 3801-3807
    • Muhlradt, P.F.1    Frisch, M.2
  • 29
    • 0026660488 scopus 로고
    • A microtiter plate transglutaminase assay utilizing 5-(biotinamido) pentylamine as substrate
    • Slaughter TF, Achyuthan KE, Lai TS, Greenberg CS. A microtiter plate transglutaminase assay utilizing 5-(biotinamido) pentylamine as substrate. Anal Biochem 205:166-171, 1992.
    • (1992) Anal Biochem , vol.205 , pp. 166-171
    • Slaughter, T.F.1    Achyuthan, K.E.2    Lai, T.S.3    Greenberg, C.S.4
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-684, 1970.
    • (1970) Nature , vol.227 , pp. 680-684
    • Laemmli, U.K.1
  • 34
    • 0031569093 scopus 로고    scopus 로고
    • Kinetics of cytokine production in experimental systemic lupus erythematosus: Involvement of T helper cell 1/T helper cell 2-type cytokines in disease
    • Segal R, Bermas BL, Dayan M, Kalush F, Shearer GM, Mozes F. Kinetics of cytokine production in experimental systemic lupus erythematosus: involvement of T helper cell 1/T helper cell 2-type cytokines in disease. J Immunol 158:3009-3016, 1997.
    • (1997) J Immunol , vol.158 , pp. 3009-3016
    • Segal, R.1    Bermas, B.L.2    Dayan, M.3    Kalush, F.4    Shearer, G.M.5    Mozes, F.6
  • 38
    • 1642536490 scopus 로고    scopus 로고
    • Innate immune discrimination of apoptotic cells: Repression of proinflammatory macrophage transcription is coupled directly to specific recognition
    • Cvetanovic M, Ucker DS. Innate immune discrimination of apoptotic cells: repression of proinflammatory macrophage transcription is coupled directly to specific recognition. J Immunol 172:880-889, 2004.
    • (2004) J Immunol , vol.172 , pp. 880-889
    • Cvetanovic, M.1    Ucker, D.S.2
  • 39
    • 0037668545 scopus 로고    scopus 로고
    • Pathogenesis of systemic lupus erythematosus
    • Mok CC, Lau CS. Pathogenesis of systemic lupus erythematosus. J Clin Pathol 56:481-490, 2003.
    • (2003) J Clin Pathol , vol.56 , pp. 481-490
    • Mok, C.C.1    Lau, C.S.2
  • 40
    • 21344443488 scopus 로고    scopus 로고
    • T- and B-cell abnormalities in systemic lupus erythematosus
    • Nagy G, Koncz A, Perl A. T- and B-cell abnormalities in systemic lupus erythematosus. Crit Rev Immunol 25:123-140, 2005.
    • (2005) Crit Rev Immunol , vol.25 , pp. 123-140
    • Nagy, G.1    Koncz, A.2    Perl, A.3
  • 41
    • 14844347540 scopus 로고    scopus 로고
    • A splice variant of the TCR zeta mRNA lacking exon 7 leads to the down-regulation of TCR zeta, the TCR/CD3 complex, and IL-2 production in systemic lupus erythematosus T cells
    • Tsuzaka K, Setoyama Y, Yoshimoto K, Shiraishi K, Suzuki K, Abe T, Takeuchi T. A splice variant of the TCR zeta mRNA lacking exon 7 leads to the down-regulation of TCR zeta, the TCR/CD3 complex, and IL-2 production in systemic lupus erythematosus T cells. J Immunol 174:3518-3525, 2005.
    • (2005) J Immunol , vol.174 , pp. 3518-3525
    • Tsuzaka, K.1    Setoyama, Y.2    Yoshimoto, K.3    Shiraishi, K.4    Suzuki, K.5    Abe, T.6    Takeuchi, T.7
  • 42
    • 0037443775 scopus 로고    scopus 로고
    • Lupus-prone mice have an abnormal response to thioglycolate and an impaired clearance of apoptotic cells
    • Potter PK, Cortes-Hernandez J, Quartier P, Botto M, Walport MJ. Lupus-prone mice have an abnormal response to thioglycolate and an impaired clearance of apoptotic cells. J Immunol 170:3223-3232, 2003.
    • (2003) J Immunol , vol.170 , pp. 3223-3232
    • Potter, P.K.1    Cortes-Hernandez, J.2    Quartier, P.3    Botto, M.4    Walport, M.J.5


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