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Volumn 110, Issue 4, 2003, Pages 450-457

Inverse regulation of the ADAM-family members, decysin and MADDAM/ADAM19 during monocyte differentiation

Author keywords

[No Author keywords available]

Indexed keywords

A DISINTEGRIN AND METALLOPROTEASE; ADAM 19; CALCITRIOL; CD40 LIGAND; CELL MARKER; DECYSIN; MEMBRANE PROTEIN; MESSENGER RNA; METALLOPROTEASE AND DISINTEGRIN DENDRITIC CELL ANTIGEN MARKER; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 0346851877     PISSN: 00192805     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2567.2003.01754.x     Document Type: Article
Times cited : (31)

References (54)
  • 1
    • 0029900269 scopus 로고    scopus 로고
    • Dendritic cells: From ontogenetic orphans to myelomonocytic descendants
    • Peters JH, Gieseler R, Thiele B, Steinbach F. Dendritic cells: from ontogenetic orphans to myelomonocytic descendants. Immunol Today 1996; 17:273-8.
    • (1996) Immunol Today , vol.17 , pp. 273-278
    • Peters, J.H.1    Gieseler, R.2    Thiele, B.3    Steinbach, F.4
  • 2
    • 0020683175 scopus 로고
    • Primary cultures of human blood-born macrophages grown on hydrophobic teflon membranes
    • Andreesen R, Picht J, Lohr GW. Primary cultures of human blood-born macrophages grown on hydrophobic teflon membranes. J Immunol Methods 1983; 56:295-304.
    • (1983) J Immunol Methods , vol.56 , pp. 295-304
    • Andreesen, R.1    Picht, J.2    Lohr, G.W.3
  • 3
    • 0023608127 scopus 로고
    • Veiled accessory cells deduced from monocytes
    • Peters JH, Ruhl S, Friedrichs D. Veiled accessory cells deduced from monocytes. Immunobiology 1987; 176:154-66.
    • (1987) Immunobiology , vol.176 , pp. 154-166
    • Peters, J.H.1    Ruhl, S.2    Friedrichs, D.3
  • 6
    • 0032538522 scopus 로고    scopus 로고
    • Differentiation of monocytes into dendritic cells in a model of transendothelial trafficking
    • Randolph GJ, Beaulieu S, Lebecque S, Steinman RM, Muller WA. Differentiation of monocytes into dendritic cells in a model of transendothelial trafficking. Science 1998; 282:480-3.
    • (1998) Science , vol.282 , pp. 480-483
    • Randolph, G.J.1    Beaulieu, S.2    Lebecque, S.3    Steinman, R.M.4    Muller, W.A.5
  • 11
    • 0034161714 scopus 로고    scopus 로고
    • 3 inhibits differentiation, maturation, activation, and survival of dendritic cells leading to impaired alloreactive T cell activation
    • 3 inhibits differentiation, maturation, activation, and survival of dendritic cells leading to impaired alloreactive T cell activation. J Immunol 2000; 164:2405-11.
    • (2000) J Immunol , vol.164 , pp. 2405-2411
    • Penna, G.1    Adorini, L.2
  • 12
    • 0034178251 scopus 로고    scopus 로고
    • V. Vitamin D3 affects differentiation, maturation, and function of human monocyte-derived dendritic cells
    • Piemonti L, Monti P, Sironi M, Fraticelli P, Leone BE, Dal Cin E, Di Allavena PC, V. Vitamin D3 affects differentiation, maturation, and function of human monocyte-derived dendritic cells. J Immunol 2000; 164:4443-51.
    • (2000) J Immunol , vol.164 , pp. 4443-4451
    • Piemonti, L.1    Monti, P.2    Sironi, M.3    Fraticelli, P.4    Leone, B.E.5    Dal Cin, E.6    Di Allavena, P.C.7
  • 13
    • 0034661829 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a human metalloprotease disintegrin - A novel marker for dendritic cell differentiation
    • Fritsche J, Moser M, Faust S, Peuker A, Buttner R, Andreesen R, Kreutz M. Molecular cloning and characterization of a human metalloprotease disintegrin - a novel marker for dendritic cell differentiation. Blood 2000; 96:732-9.
    • (2000) Blood , vol.96 , pp. 732-739
    • Fritsche, J.1    Moser, M.2    Faust, S.3    Peuker, A.4    Buttner, R.5    Andreesen, R.6    Kreutz, M.7
  • 14
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNF alpha and Notch
    • Blobel CP. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch. Cell 1997; 90:589-92.
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 15
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg TG, Straight PD, Gerena RL, Huovila AP, Primakoff P, Myles DG, White JM. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol 1995; 169:378-83.
    • (1995) Dev Biol , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3    Huovila, A.P.4    Primakoff, P.5    Myles, D.G.6    White, J.M.7
  • 17
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • Primakoff P, Myles DG. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet 2000; 16:83-7.
    • (2000) Trends Genet , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 18
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black RA, Rauch CT, Kozlosky CJ et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 1997; 385:729-33.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3
  • 19
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel CP, Wolfsberg TG, Turck CW, Myles DG, Primakoff P, White JM. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 1992; 356:248-52.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 20
    • 0034672264 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells
    • Kang Q, Cao Y, Zolkiewska A. Metalloprotease-disintegrin ADAM 12 binds to the SH3 domain of Src and activates Src tyrosine kinase in C2C12 cells. Biochem J 2000; 352 Part 3:883-92.
    • (2000) Biochem J , vol.352 , Issue.3 PART , pp. 883-892
    • Kang, Q.1    Cao, Y.2    Zolkiewska, A.3
  • 21
    • 0033532191 scopus 로고    scopus 로고
    • Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)- converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival
    • Lum L, Wong BR, Josien R et al. Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival. J Biol Chem 1999; 274:13613-8.
    • (1999) J Biol Chem , vol.274 , pp. 13613-13618
    • Lum, L.1    Wong, B.R.2    Josien, R.3
  • 22
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss ML, Jin SL, Milla ME et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 1997; 385:733-6.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3
  • 24
    • 0030866507 scopus 로고    scopus 로고
    • Polymerase chain reaction selects a novel disintegrin proteinase from CD40-activated germinal center dendritic cells
    • Mueller CG, Rissoan MC, Salinas B et al. Polymerase chain reaction selects a novel disintegrin proteinase from CD40-activated germinal center dendritic cells. J Exp Med 1997; 186:655-63.
    • (1997) J Exp Med , vol.186 , pp. 655-663
    • Mueller, C.G.1    Rissoan, M.C.2    Salinas, B.3
  • 27
    • 0030844633 scopus 로고    scopus 로고
    • Human dendritic cell responses to lipopolysaccharide and CD40 ligation are differentially regulated by interleukin-10
    • Buelens C, Verhasselt V, De Groote D, Thielemans K, Goldman M, Willems F. Human dendritic cell responses to lipopolysaccharide and CD40 ligation are differentially regulated by interleukin-10. Eur J Immunol 1997; 27:1848-52.
    • (1997) Eur J Immunol , vol.27 , pp. 1848-1852
    • Buelens, C.1    Verhasselt, V.2    De Groote, D.3    Thielemans, K.4    Goldman, M.5    Willems, F.6
  • 30
    • 0023939138 scopus 로고
    • Transcriptional activation of the lipoprotein lipase and apolipoprotein E genes accompanies differentiation in some human macrophage-like cell lines
    • Auwerx JH, Deeb S, Brunzell JD, Peng R, Chait A. Transcriptional activation of the lipoprotein lipase and apolipoprotein E genes accompanies differentiation in some human macrophage-like cell lines. Biochemistry 1988; 27:2651-5.
    • (1988) Biochemistry , vol.27 , pp. 2651-2655
    • Auwerx, J.H.1    Deeb, S.2    Brunzell, J.D.3    Peng, R.4    Chait, A.5
  • 32
    • 0019408387 scopus 로고
    • Early changes in phosphatidylcholine metabolism in human acute promyelocytic leukemia cells stimulated to differentiate by phorbol ester
    • Cassileth PA, Suholet D, Cooper RA. Early changes in phosphatidylcholine metabolism in human acute promyelocytic leukemia cells stimulated to differentiate by phorbol ester. Blood 1981; 58:237-43.
    • (1981) Blood , vol.58 , pp. 237-243
    • Cassileth, P.A.1    Suholet, D.2    Cooper, R.A.3
  • 35
    • 0031802150 scopus 로고    scopus 로고
    • Isolation and phenotypic characterization of colonie macrophages
    • Rogler G, Hausmann M, Vogl D et al. Isolation and phenotypic characterization of colonie macrophages. Clin Exp Immunol 1998; 112:205-15.
    • (1998) Clin Exp Immunol , vol.112 , pp. 205-215
    • Rogler, G.1    Hausmann, M.2    Vogl, D.3
  • 36
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162:156-9.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 37
    • 0033168650 scopus 로고    scopus 로고
    • Calcium mobilization in human myeloid cells results in acquisition of individual dendritic cell-like characteristics through discrete signaling pathways
    • Koski GK, Schwartz GN, Weng DE, Czerniecki BJ, Carter C, Gress RE, Cohen PA. Calcium mobilization in human myeloid cells results in acquisition of individual dendritic cell-like characteristics through discrete signaling pathways. J Immunol 1999; 163:82-92.
    • (1999) J Immunol , vol.163 , pp. 82-92
    • Koski, G.K.1    Schwartz, G.N.2    Weng, D.E.3    Czerniecki, B.J.4    Carter, C.5    Gress, R.E.6    Cohen, P.A.7
  • 38
    • 0033566626 scopus 로고    scopus 로고
    • Calcium ionophore-treated myeloid cells acquire many dendritic cell characteristics independent of prior differentiation state, transformation status, or sensitivity to biologic agents
    • Koski GK, Schwartz GN, Weng DE, Cress RE, Engels FH, Tsokos M, Czerniecki BJ, Cohen PA. Calcium ionophore-treated myeloid cells acquire many dendritic cell characteristics independent of prior differentiation state, transformation status, or sensitivity to biologic agents. Blood 1999; 94:1359-71.
    • (1999) Blood , vol.94 , pp. 1359-1371
    • Koski, G.K.1    Schwartz, G.N.2    Weng, D.E.3    Cress, R.E.4    Engels, F.H.5    Tsokos, M.6    Czerniecki, B.J.7    Cohen, P.A.8
  • 39
    • 0029995478 scopus 로고    scopus 로고
    • Molecular cloning of MADM, a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types
    • Howard L, Lu X, Mitchell S, Griffiths S, Glynn P. Molecular cloning of MADM, a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem J 1996; 317 (1):45-50.
    • (1996) Biochem J , vol.317 , Issue.1 , pp. 45-50
    • Howard, L.1    Lu, X.2    Mitchell, S.3    Griffiths, S.4    Glynn, P.5
  • 40
    • 9844253890 scopus 로고    scopus 로고
    • Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases
    • Rosendahl MS, Ko SC, Long DL et al. Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases. J Biol Chem 1997; 272:24588-93.
    • (1997) J Biol Chem , vol.272 , pp. 24588-24593
    • Rosendahl, M.S.1    Ko, S.C.2    Long, D.L.3
  • 41
    • 0031577162 scopus 로고    scopus 로고
    • Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies
    • Wu E, Croucher PI, McKie N. Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies. Biochem Biophys Res Commun 1997; 235:437-42.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 437-442
    • Wu, E.1    Croucher, P.I.2    McKie, N.3
  • 42
    • 0032080801 scopus 로고    scopus 로고
    • TNF-alpha convertase enzyme from human arthritis-affected cartilage: Isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-alpha
    • Patel IR, Attur MG, Patel RN, Stuchin SA, Abagyan RA, Abramson SB, Amin AR. TNF-alpha convertase enzyme from human arthritis-affected cartilage: isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-alpha. J Immunol 1998; 160:4570-9.
    • (1998) J Immunol , vol.160 , pp. 4570-4579
    • Patel, I.R.1    Attur, M.G.2    Patel, R.N.3    Stuchin, S.A.4    Abagyan, R.A.5    Abramson, S.B.6    Amin, A.R.7
  • 45
    • 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, Tada K. Establishment and characterization of a human acute monocytic leukemia cell line (THP-1). Int J Cancer 1980; 26:171-6.
    • (1980) Int J Cancer , vol.26 , pp. 171-176
    • Tsuchiya, S.1    Yamabe, M.2    Yamaguchi, Y.3    Kobayashi, Y.4    Konno, T.5    Tada, K.6
  • 49
    • 0027291589 scopus 로고
    • 1,25-Dihydroxyvitamin D3 production and vitamin D3 receptor expression are developmentally regulated during differentiation of human monocytes into macrophages
    • Kreutz M, Andreesen R, Krause SW, Szabo A, Ritz E, Reichel H. 1,25-dihydroxyvitamin D3 production and vitamin D3 receptor expression are developmentally regulated during differentiation of human monocytes into macrophages. Blood 1993; 82: 1300-7.
    • (1993) Blood , vol.82 , pp. 1300-1307
    • Kreutz, M.1    Andreesen, R.2    Krause, S.W.3    Szabo, A.4    Ritz, E.5    Reichel, H.6
  • 51
    • 0033017290 scopus 로고    scopus 로고
    • Meltrin-alpha, a fusion protein involved in multinucleated giant cell and osteoclast formation
    • Abe E, Mocharla H, Yamate T, Taguchi Y, Manolagas SC. Meltrin-alpha, a fusion protein involved in multinucleated giant cell and osteoclast formation. Calcif Tissue Int 1999; 64:508-15.
    • (1999) Calcif Tissue Int , vol.64 , pp. 508-515
    • Abe, E.1    Mocharla, H.2    Yamate, T.3    Taguchi, Y.4    Manolagas, S.C.5
  • 52
    • 0032512831 scopus 로고    scopus 로고
    • Cloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cells
    • Inoue D, Reid M, Lum L, Kratzschmar J, Weskamp G, Myung YM, Baron R, Blobel CP. Cloning and initial characterization of mouse meltrin beta and analysis of the expression of four metalloprotease-disintegrins in bone cells. J Biol Chem 1998; 273:4180-7.
    • (1998) J Biol Chem , vol.273 , pp. 4180-4187
    • Inoue, D.1    Reid, M.2    Lum, L.3    Kratzschmar, J.4    Weskamp, G.5    Myung, Y.M.6    Baron, R.7    Blobel, C.P.8
  • 53
    • 0034957288 scopus 로고    scopus 로고
    • Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin
    • Schwettmann L, Tschesche H. Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin. Protein Expr Purif 2001; 21:65-70.
    • (2001) Protein Expr Purif , vol.21 , pp. 65-70
    • Schwettmann, L.1    Tschesche, H.2
  • 54
    • 0035253355 scopus 로고    scopus 로고
    • TNF-alpha-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation
    • Rovida E, Paccagnini A, Del Rosso M, Peschon J, Dello SP. TNF-alpha-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation. J Immunol 2001; 166:1583-9.
    • (2001) J Immunol , vol.166 , pp. 1583-1589
    • Rovida, E.1    Paccagnini, A.2    Del Rosso, M.3    Peschon, J.4    Dello, S.P.5


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