메뉴 건너뛰기




Volumn 146, Issue 4, 2009, Pages 471-479

Dynamic expression of peptidylarginine deiminase 2 in human monocytic leukaemia THP-1 cells during macrophage differentiation

Author keywords

Citrullinated proteins; Monocytes; Protein deimination; Rheumatoid arthritis; Vimentin

Indexed keywords

CALCIMYCIN; MESSENGER RNA; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN ARGININE DEIMINASE; PROTEIN ARGININE DEIMINASE 2; UNCLASSIFIED DRUG; VIMENTIN;

EID: 70350072817     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp097     Document Type: Article
Times cited : (22)

References (42)
  • 1
    • 0242720407 scopus 로고    scopus 로고
    • PAD, a growing family of citrullinating enzymes: Genes, features and involvement in disease
    • Vossenaar, E.R., Zendman, A.J.W., van Venrooij, W.J., and Pruijn, G.J.M. (2003) PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. BioEssays 25, 1106-1118
    • (2003) BioEssays , vol.25 , pp. 1106-1118
    • Vossenaar, E.R.1    Zendman, A.J.W.2    Van Venrooij, W.J.3    Pruijn, G.J.M.4
  • 4
    • 34948865716 scopus 로고    scopus 로고
    • Citrullination by peptidylarginine deiminase in rheumatoid arthritis
    • Suzuki, A., Yamada, R., and Yamamoto, K. (2007) Citrullination by peptidylarginine deiminase in rheumatoid arthritis. Ann. N.Y. Acad. Sci. 1108, 323-339
    • (2007) Ann. N.Y. Acad. Sci. , vol.1108 , pp. 323-339
    • Suzuki, A.1    Yamada, R.2    Yamamoto, K.3
  • 7
    • 0034968874 scopus 로고    scopus 로고
    • Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils
    • Asaga, H., Nakashima, K., Senshu, T., Ishigami, A., and Yamada, M. (2001) Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils. J. Leukoc. Biol. 70, 46-51
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 46-51
    • Asaga, H.1    Nakashima, K.2    Senshu, T.3    Ishigami, A.4    Yamada, M.5
  • 8
    • 0031974911 scopus 로고    scopus 로고
    • Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies
    • Schellekens, G.A., de Jong, B.A., van den Hoogen, F.H., van de Putte, L.B., and van Venrooij, W.J. (1998) Citrulline is an essential constituent of antigenic determinants recognized by rheumatoid arthritis-specific autoantibodies. J. Clin. Invest. 101, 273-281
    • (1998) J. Clin. Invest. , vol.101 , pp. 273-281
    • Schellekens, G.A.1    De Jong, B.A.2    Van Den Hoogen, F.H.3    Van De Putte, L.B.4    Van Venrooij, W.J.5
  • 9
    • 0032960781 scopus 로고    scopus 로고
    • The epitopes targeted by the rheumatoid arthritis-associated antifilaggrin autoantibodies are posttranslationally generated on various sites of (pro)filaggrin by deimination of arginine residues
    • Girbal-Neuhauser, E., Durieux, J.J., Arnaud, M., Dalbon, P., Sebbag, M., Vincent, C., Simon, M., Senshu, T., Masson-Bessiere, C., Jolivet-Reynaud, C., Jolivet, M., and Serre, G. (1999) The epitopes targeted by the rheumatoid arthritis-associated antifilaggrin autoantibodies are posttranslationally generated on various sites of (pro)filaggrin by deimination of arginine residues. J. Immunol. 162, 585-594
    • (1999) J. Immunol. , vol.162 , pp. 585-594
    • Girbal-Neuhauser, E.1    Durieux, J.J.2    Arnaud, M.3    Dalbon, P.4    Sebbag, M.5    Vincent, C.6    Simon, M.7    Senshu, T.8    Masson-Bessiere, C.9    Jolivet-Reynaud, C.10    Jolivet, M.11    Serre, G.12
  • 12
    • 0033600723 scopus 로고    scopus 로고
    • Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1a,25- dihydroxyvitamin D3
    • Nakashima, K., Hagiwara, T., Ishigami, A., Nagata, S., Asaga, H., Kuramoto, M., Senshu, T., and Yamada, M. (1999) Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1a,25- dihydroxyvitamin D3. J. Biol. Chem. 274, 27786-27792
    • (1999) J. Biol. Chem. , vol.274 , pp. 27786-27792
    • Nakashima, K.1    Hagiwara, T.2    Ishigami, A.3    Nagata, S.4    Asaga, H.5    Kuramoto, M.6    Senshu, T.7    Yamada, M.8
  • 13
    • 0037147140 scopus 로고    scopus 로고
    • Nuclear localization of peptidylarginine deiminase v and histone deimination in granulocytes
    • Nakashima, K., Hagiwara, T., and Yamada, M. (2002) Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes. J. Biol. Chem. 277, 49562-49568
    • (2002) J. Biol. Chem. , vol.277 , pp. 49562-49568
    • Nakashima, K.1    Hagiwara, T.2    Yamada, M.3
  • 14
    • 40749128547 scopus 로고    scopus 로고
    • Histone deimination as a response to inflammatory stimuli in neutrophils
    • Neeli, I., Khan, S.N., and Radic, M. (2008) Histone deimination as a response to inflammatory stimuli in neutrophils. J. Immunol. 180, 1895-1902
    • (2008) J. Immunol. , vol.180 , pp. 1895-1902
    • Neeli, I.1    Khan, S.N.2    Radic, M.3
  • 16
    • 0032562113 scopus 로고    scopus 로고
    • Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages
    • Asaga, H., Yamada, M., and Senshu, T. (1998) Selective deimination of vimentin in calcium ionophore-induced apoptosis of mouse peritoneal macrophages. Biochem. Biophys. Res. Commun. 243, 641-646
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 641-646
    • Asaga, H.1    Yamada, M.2    Senshu, T.3
  • 17
    • 28544446111 scopus 로고    scopus 로고
    • Monocyte and macrophage heterogeneity
    • Gordon, S. and Taylor, P.R. (2005) Monocyte and macrophage heterogeneity. Nat. Rev. Immunol. 5, 953-964
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 953-964
    • Gordon, S.1    Taylor, P.R.2
  • 18
    • 0018871095 scopus 로고
    • Establishment and characterization of a human acute monocytic leukemia cell line (THP-1)
    • Tsuchiya, S., Yamabe, M., Yamaguchi, Y., Kobayashi, Y., Konno, T., and Tada, K. (1980) Establishment and characterization of a human acute monocytic leukemia cell line (THP-1). Int. J. Cancer 26, 71-76
    • (1980) Int. J. Cancer , vol.26 , pp. 71-76
    • Tsuchiya, S.1    Yamabe, M.2    Yamaguchi, Y.3    Kobayashi, Y.4    Konno, T.5    Tada, K.6
  • 19
    • 0025963002 scopus 로고
    • The human leukemia cell line THP-1: A multifacetted model for the study of monocyte-macrophage differentiation
    • Auwerx, J. (1991) The human leukemia cell line, THP-1: a multifacetted model for the study of monocyte-macrophage differentiation. Experientia 47, 22-31
    • (1991) Experientia , vol.47 , pp. 22-31
    • Auwerx, J.1
  • 20
    • 0030013991 scopus 로고    scopus 로고
    • Differences in the state of differentiation of THP-1 cells induced by phorbol ester and 1,25-dihydroxyvitamin D3
    • Schwende, H., Fitzke, E., Ambs, P., and Dieter, P. (1996) Differences in the state of differentiation of THP-1 cells induced by phorbol ester and 1,25-dihydroxyvitamin D3. J. Leukoc. Biol. 59, 555-561
    • (1996) J. Leukoc. Biol. , vol.59 , pp. 555-561
    • Schwende, H.1    Fitzke, E.2    Ambs, P.3    Dieter, P.4
  • 21
    • 0029103435 scopus 로고
    • Detection of citrullinated proteins in rat skin: Probing with a monospecific antibody after modification of citrulline residues
    • Senshu, T., Akiyama, K., Kan, S., Asaga, H., Ishigami, A., and Manabe, M. (1995) Detection of citrullinated proteins in rat skin: probing with a monospecific antibody after modification of citrulline residues. J. Invest. Dermatol. 105, 163-169
    • (1995) J. Invest. Dermatol. , vol.105 , pp. 163-169
    • Senshu, T.1    Akiyama, K.2    Kan, S.3    Asaga, H.4    Ishigami, A.5    Manabe, M.6
  • 22
    • 0026764429 scopus 로고
    • Detection of citrulline residues in citrullinated proteins on polyvinylidene difluoride membrane
    • Senshu, T., Sato, T., Inoue, T., Akiyama, K., and Asaga, H. (1992) Detection of citrulline residues in citrullinated proteins on polyvinylidene difluoride membrane. Anal. Biochem. 203, 94-100
    • (1992) Anal. Biochem. , vol.203 , pp. 94-100
    • Senshu, T.1    Sato, T.2    Inoue, T.3    Akiyama, K.4    Asaga, H.5
  • 23
    • 0024281847 scopus 로고
    • Combined biochemical and immunochemical comparison of peptidylarginine deiminases present in various tissues
    • Watanabe, K., Akiyama, K., Hikichi, K., Ohtsuka, R., Okuyama, A., and Senshu, T. (1988) Combined biochemical and immunochemical comparison of peptidylarginine deiminases present in various tissues. Biochim. Biophys. Acta. 966, 375-383
    • (1988) Biochim. Biophys. Acta. , vol.966 , pp. 375-383
    • Watanabe, K.1    Akiyama, K.2    Hikichi, K.3    Ohtsuka, R.4    Okuyama, A.5    Senshu, T.6
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate- phenolchloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate- phenolchloroform extraction. Anal. Biochem. 162, 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 28
    • 0036295234 scopus 로고    scopus 로고
    • Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes
    • Hagiwara, T., Nakashima, K., Hirano, H., Senshu, T., and Yamada, M. (2002) Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes. Biochem. Biophys. Res. Commun. 290, 979-983
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 979-983
    • Hagiwara, T.1    Nakashima, K.2    Hirano, H.3    Senshu, T.4    Yamada, M.5
  • 29
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. (1975) High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 30
    • 18244363581 scopus 로고    scopus 로고
    • Regulation of the expression of peptidylarginine deiminase type II gene (PADI2) in human keratinocytes involves Sp1 and Sp3 transcription factors
    • Dong, S., Kojima, T., Shiraiwa, M., Mechin, MC., Chavanas, S., Serre, G., Simon, M., Kawada, A., and Takahara, H. (2005) Regulation of the expression of peptidylarginine deiminase type II gene (PADI2) in human keratinocytes involves Sp1 and Sp3 transcription factors. J. Invest. Dermatol. 124, 1026-1033
    • (2005) J. Invest. Dermatol. , vol.124 , pp. 1026-1033
    • Dong, S.1    Kojima, T.2    Shiraiwa, M.3    Mechin, M.C.4    Chavanas, S.5    Serre, G.6    Simon, M.7    Kawada, A.8    Takahara, H.9
  • 31
    • 1642565184 scopus 로고    scopus 로고
    • Identification and characterization of a phorbol ester-responsive element in the murine 8S-lipoxygenase gene
    • Kim, E., Muga, S.J., and Fischer, S.M. (2004) Identification and characterization of a phorbol ester-responsive element in the murine 8S-lipoxygenase gene. J. Biol. Chem. 279, 11188-11197
    • (2004) J. Biol. Chem. , vol.279 , pp. 11188-11197
    • Kim, E.1    Muga, S.J.2    Fischer, S.M.3
  • 32
    • 0024473081 scopus 로고
    • Ca2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain
    • Inagaki, M., Takahara, H., Nishi, Y., Sugawara, K., and Sato, C. (1989) Ca2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain. J. Biol. Chem. 264, 18119-18127
    • (1989) J. Biol. Chem. , vol.264 , pp. 18119-18127
    • Inagaki, M.1    Takahara, H.2    Nishi, Y.3    Sugawara, K.4    Sato, C.5
  • 33
    • 34249682108 scopus 로고    scopus 로고
    • Novel functions of vimentin in cell adhesion, migration, and signaling
    • Ivaska, J., Pallari, H.M., Nevo, J., and Eriksson, J.E. (2007) Novel functions of vimentin in cell adhesion, migration, and signaling. Exp. Cell Res. 313, 2050-2067
    • (2007) Exp. Cell Res. , vol.313 , pp. 2050-2067
    • Ivaska, J.1    Pallari, H.M.2    Nevo, J.3    Eriksson, J.E.4
  • 34
    • 65449188330 scopus 로고    scopus 로고
    • Head and rod 1 interactions in vimentin: Identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance
    • Aziz, A., Hess, J.F., Budamagunta, M.S., Fitzgerald, P.G., and Voss, J.C. (2009) Head and Rod 1 Interactions in Vimentin: identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance. J. Biol. Chem. 284, 7330-7338
    • (2009) J. Biol. Chem. , vol.284 , pp. 7330-7338
    • Aziz, A.1    Hess, J.F.2    Budamagunta, M.S.3    Fitzgerald, P.G.4    Voss, J.C.5
  • 35
    • 0034764032 scopus 로고    scopus 로고
    • Isolation of SDS-stable complexes of the intermediate filament protein vimentin with repetitive, mobile, nuclear matrix attachment region, and mitochondrial DNA sequence elements from cultured mouse and human fibroblasts
    • Tolstonog, G.V., Mothes, E., Shoeman, R.L., and Traub, P. (2001) Isolation of SDS-stable complexes of the intermediate filament protein vimentin with repetitive, mobile, nuclear matrix attachment region, and mitochondrial DNA sequence elements from cultured mouse and human fibroblasts. DNA Cell Biol. 20, 531-554
    • (2001) DNA Cell Biol. , vol.20 , pp. 531-554
    • Tolstonog, G.V.1    Mothes, E.2    Shoeman, R.L.3    Traub, P.4
  • 36
    • 0033598182 scopus 로고    scopus 로고
    • Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrinvimentin complexes in macrophages
    • Correia, I., Chu, D., Chou, Y.H., Goldman, R.D., and Matsudaira, P. (1999) Integrating the actin and vimentin cytoskeletons. adhesion-dependent formation of fimbrinvimentin complexes in macrophages. J. Cell Biol. 146, 831-842
    • (1999) J. Cell Biol. , vol.146 , pp. 831-842
    • Correia, I.1    Chu, D.2    Chou, Y.H.3    Goldman, R.D.4    Matsudaira, P.5
  • 37
    • 18744397853 scopus 로고    scopus 로고
    • Senescence-associated alterations of cytoskeleton: Extraordinary production of vimentin that anchors cytoplasmic p53 in senescent human fibroblasts
    • Nishio, K. and Inoue, A. (2005) Senescence-associated alterations of cytoskeleton: extraordinary production of vimentin that anchors cytoplasmic p53 in senescent human fibroblasts. Histochem. Cell Biol. 123, 263-273
    • (2005) Histochem. Cell Biol. , vol.123 , pp. 263-273
    • Nishio, K.1    Inoue, A.2
  • 39
    • 0038011833 scopus 로고    scopus 로고
    • Evolving concepts of rheumatoid arthritis
    • Firestein, G.S. (2003) Evolving concepts of rheumatoid arthritis. Nature 423, 356-361
    • (2003) Nature , vol.423 , pp. 356-361
    • Firestein, G.S.1
  • 41
    • 0035869593 scopus 로고    scopus 로고
    • The major synovial targets of the rheumatoidarthritisspecific antifilaggrinautoantibodies are deiminated forms of the alpha- and beta-chains of fibrin
    • Masson-Bessière, C., Sebbag, M., Girbal-Neuhauser, E., Nogueira, L., Vincent, C., Senshu, T., and Serre, G. (2001) The major synovial targets of the rheumatoidarthritisspecific antifilaggrinautoantibodies are deiminated forms of the alpha- and beta-chains of fibrin. J. Immunol. 166, 4177-4184
    • (2001) J. Immunol. , vol.166 , pp. 4177-4184
    • Masson-Bessière, C.1    Sebbag, M.2    Girbal-Neuhauser, E.3    Nogueira, L.4    Vincent, C.5    Senshu, T.6    Serre, G.7
  • 42
    • 1842619397 scopus 로고    scopus 로고
    • Rheumatoid arthritis specific anti-Sa antibodies target citrullinated vimentin
    • Vossenaar, E.R., Senshu, T., van Venrooij, W.J., and Menard, H. (2004) Rheumatoid arthritis specific anti-Sa antibodies target citrullinated vimentin. Arthritis Res. Ther. 6, 142-150
    • (2004) Arthritis Res. Ther. , vol.6 , pp. 142-150
    • Vossenaar, E.R.1    Senshu, T.2    Van Venrooij, W.J.3    Menard, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.