메뉴 건너뛰기




Volumn 186, Issue 5, 1997, Pages 655-663

Polymerase chain reaction selects a novel disintegrin proteinase from CD40-activated germinal center dendritic cells

Author keywords

[No Author keywords available]

Indexed keywords

CD40 ANTIGEN; DISINTEGRIN; METALLOPROTEINASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 0030866507     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.186.5.655     Document Type: Article
Times cited : (75)

References (47)
  • 1
    • 0031045622 scopus 로고    scopus 로고
    • Origin, maturation and antigen presenting function of dendritic cells
    • Cella, M., F. Sallusto, and A. Lanzavecchia. 1997. Origin, maturation and antigen presenting function of dendritic cells. Curr. Opin. Immunol. 9:10-16.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 10-16
    • Cella, M.1    Sallusto, F.2    Lanzavecchia, A.3
  • 2
    • 0000068799 scopus 로고    scopus 로고
    • In vitro regulation of dendritic cell development and function
    • T. Whetton and J. Gordon, editors. Plenum Press, London
    • Caux, C., and J. Banchereau. 1996. In vitro regulation of dendritic cell development and function. In Blood Cell Biochemistry. T. Whetton and J. Gordon, editors. Plenum Press, London. 263-301.
    • (1996) Blood Cell Biochemistry , pp. 263-301
    • Caux, C.1    Banchereau, J.2
  • 3
    • 0029913425 scopus 로고    scopus 로고
    • New insights into the mobilization and phagocytic activity of dendritic cells
    • Austyn, J.D. 1996. New insights into the mobilization and phagocytic activity of dendritic cells. J. Exp. Med. 183:1287-1292.
    • (1996) J. Exp. Med. , vol.183 , pp. 1287-1292
    • Austyn, J.D.1
  • 4
  • 5
    • 0026446156 scopus 로고
    • GM-CSF and TNF-α cooperate in the generation of dendritic Langerhans cells
    • Caux, C., C. Dezutter-Dambuyant, D. Schmitt, and J. Banchereau. 1992. GM-CSF and TNF-α cooperate in the generation of dendritic Langerhans cells. Nature (Lond.). 360: 258-261.
    • (1992) Nature (Lond.) , vol.360 , pp. 258-261
    • Caux, C.1    Dezutter-Dambuyant, C.2    Schmitt, D.3    Banchereau, J.4
  • 7
    • 0028289244 scopus 로고
    • Efficient presentation of soluble antigen by cultured human dendritic cells is maintamed by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor alpha
    • Sallusto, F., and A. Lanzavecchia. 1994. Efficient presentation of soluble antigen by cultured human dendritic cells is maintamed by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor alpha. J. Exp. Med. 179:1109-1118.
    • (1994) J. Exp. Med. , vol.179 , pp. 1109-1118
    • Sallusto, F.1    Lanzavecchia, A.2
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 13
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak, M. 1986. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell. 44:283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 14
    • 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, H.E., and H. Birkedal-Hansen. 1990. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl. Acad. Sci. USA. 87:5578-5582.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 15
    • 0025733702 scopus 로고
    • Mammalian subtilisins: The long-sought dibasic processing endoproteases
    • Barr, P.J. 1991. Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell. 66:1-3.
    • (1991) Cell , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 16
    • 0027386056 scopus 로고
    • First structure of a snake venom metalloproteinase: A prototype for matrix metalloproteinases/collagenases
    • Gomis-Ruth, F.X., L.F. Kress, and W. Bode. 1993. First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases. EMBO (Eur. Mol. Biol. Organ.) J. 12:4151-4157.
    • (1993) EMBO (Eur. Mol. Biol. Organ.) J. , vol.12 , pp. 4151-4157
    • Gomis-Ruth, F.X.1    Kress, L.F.2    Bode, W.3
  • 17
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper, N.M. 1994. Families of zinc metalloproteases. FEBS Lett. 354:1-6.
    • (1994) FEBS Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 18
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian, L.M. 1992. The matrix-degrading metalloproteinases. Bioessays. 14:455-463.
    • (1992) Bioessays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 19
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg, T.G., P. Primakoff, D.G. Myles, and J.M. White. 1995. ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 131:275-278.
    • (1995) J. Cell Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.G.1    Primakoff, P.2    Myles, D.G.3    White, J.M.4
  • 20
    • 0028828128 scopus 로고
    • Complete amino acid sequence of a zinc metalloendoprotease from Streptomyces caespitosus
    • Harada, S., T. Kinoshita, N. Kasai, S. Tsunasawa, and F. Sakiyama. 1995. Complete amino acid sequence of a zinc metalloendoprotease from Streptomyces caespitosus. Eur. J. Biochem. 233:683-686.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 683-686
    • Harada, S.1    Kinoshita, T.2    Kasai, N.3    Tsunasawa, S.4    Sakiyama, F.5
  • 22
    • 0028337108 scopus 로고
    • cDNA sequences for four snake venom metalloproteinases: Structure, classification, and their relationship to mammalian reproductive proteins
    • Hite, L.A., L.G. Jia, J.B. Bjarnason, and J.W. Fox. 1994. cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins. Arch. Biochem. Biophys. 308:182-191.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L.G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 23
    • 0027323998 scopus 로고
    • Dendritic cells freshly isolated from human blood express CD4 and mature into typical immunostimulatory dendritic cells after culture in monocyte-conditioned medium
    • O'Doherty, U., R.M. Steinman, M. Peng, P.U. Cameron, S. Gezelter, I. Kopeloff, W.J. Swiggard, M. Pope, and N. Bhardwaj. 1993. Dendritic cells freshly isolated from human blood express CD4 and mature into typical immunostimulatory dendritic cells after culture in monocyte-conditioned medium. J. Exp. Med. 178:1067-1078.
    • (1993) J. Exp. Med. , vol.178 , pp. 1067-1078
    • O'Doherty, U.1    Steinman, R.M.2    Peng, M.3    Cameron, P.U.4    Gezelter, S.5    Kopeloff, I.6    Swiggard, W.J.7    Pope, M.8    Bhardwaj, N.9
  • 24
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C.P., T.G. Wolfsberg, C.W. Turck, D.G. Myles, P. Primakoff, and J.M. White. 1992. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature (Lond.). 356:248-252.
    • (1992) Nature (Lond.) , 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
  • 26
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis
    • Rooke, J., D. Pan, T. Xu, and G.M. Rubin. 1996. KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science (Wash. DC). 273:1227-1231.
    • (1996) Science (Wash. DC) , vol.273 , pp. 1227-1231
    • Rooke, J.1    Pan, D.2    Xu, T.3    Rubin, G.M.4
  • 27
    • 0025290037 scopus 로고
    • Binding of the snake venom-derived proteins applaggin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb.IIIa complex inhibits receptor function
    • Savage, B., U.M. Marzec, B.H. Chao, L.A. Harker, J.M. Maraganore, and Z.M. Ruggeri. 1990. Binding of the snake venom-derived proteins applaggin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb.IIIa complex inhibits receptor function. J. Biol. Chem. 265:11766-11772.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11766-11772
    • Savage, B.1    Marzec, U.M.2    Chao, B.H.3    Harker, L.A.4    Maraganore, J.M.5    Ruggeri, Z.M.6
  • 28
    • 15844406752 scopus 로고    scopus 로고
    • Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors
    • Arribas, J., L. Goodly, P. Vollmer, T.K. Kishimoto, S. Rose-John, and J. Massague. 1996. Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors. J. Biol. Chem. 271:11376-11382.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11376-11382
    • Arribas, J.1    Goodly, L.2    Vollmer, P.3    Kishimoto, T.K.4    Rose-John, S.5    Massague, J.6
  • 29
    • 0028919856 scopus 로고
    • A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes
    • Crowe, P.D., B.N. Walter, K.M. Mohler, C. Otten-Evans, R.A. Black, and C.F. Ware. 1995. A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes. J. Exp. Med. 181:1205-1210.
    • (1995) J. Exp. Med. , vol.181 , pp. 1205-1210
    • Crowe, P.D.1    Walter, B.N.2    Mohler, K.M.3    Otten-Evans, C.4    Black, R.A.5    Ware, C.F.6
  • 33
    • 0029975125 scopus 로고    scopus 로고
    • Hydroxamate-based metalloprotease inhibitor blocks shedding of L-selectin adhesion molecule from leukocytes: Functional consequences for neutrophil aggregation
    • Bennett, T.A., E.B. Lynam, L.A. Sklar, and S. Rogelj. 1996. Hydroxamate-based metalloprotease inhibitor blocks shedding of L-selectin adhesion molecule from leukocytes: functional consequences for neutrophil aggregation. J. Immunol. 156:3093-3097.
    • (1996) J. Immunol. , vol.156 , pp. 3093-3097
    • Bennett, T.A.1    Lynam, E.B.2    Sklar, L.A.3    Rogelj, S.4
  • 37
  • 38
    • 0026451216 scopus 로고
    • Families of metalloendopeptidases and their relationships
    • Jiang, W., and J.S. Bond. 1992. Families of metalloendopeptidases and their relationships. FEBS Lett. 312:110-114.
    • (1992) FEBS Lett. , vol.312 , pp. 110-114
    • Jiang, W.1    Bond, J.S.2
  • 39
    • 0024690967 scopus 로고
    • Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavorviridis
    • Takeya, H., M. Arakawa, T. Miyata, S. Iwanaga, and T. Omori-Satoh. 1989. Primary structure of H2-proteinase, a non-hemorrhagic metalloproteinase, isolated from the venom of the habu snake, Trimeresurus flavorviridis. J. Biochem. (Tokyo). 106:151-157.
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 151-157
    • Takeya, H.1    Arakawa, M.2    Miyata, T.3    Iwanaga, S.4    Omori-Satoh, T.5
  • 40
    • 0022996811 scopus 로고
    • Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein
    • Goldberg, G.I., S.M. Wilhelm, A. Kronberger, E.A. Bauer, G.A. Grant, and A.Z. Eisen. 1986. Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein. J. Biol. Chem. 261: 6600-6605.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6600-6605
    • Goldberg, G.I.1    Wilhelm, S.M.2    Kronberger, A.3    Bauer, E.A.4    Grant, G.A.5    Eisen, A.Z.6
  • 42
    • 0025333259 scopus 로고
    • The metalloprotease gene of Serratia marcescens strain SM6
    • Braunagel, S.C., and M.J. Benedik. 1990. The metalloprotease gene of Serratia marcescens strain SM6. Mol. Gen. Genet. 222:446-451.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 446-451
    • Braunagel, S.C.1    Benedik, M.J.2
  • 43
    • 0015517321 scopus 로고
    • Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide
    • Titani, K., M.A. Hermodson, L.H. Ericsson, K.A. Walsh, and H. Neurath. 1972. Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide. Biochemistry. 11:2427-2435.
    • (1972) Biochemistry , vol.11 , pp. 2427-2435
    • Titani, K.1    Hermodson, M.A.2    Ericsson, L.H.3    Walsh, K.A.4    Neurath, H.5
  • 44
    • 0026771067 scopus 로고
    • A novel cell-surface molecule expressed by human interdigitating reticulum cells, Langerhans cells, and activated lymphocytes is a new member of the Ig superfamily
    • Zhou, L.-J., R. Schwarting, H.M. Smith, and T.F. Tedder. 1992. A novel cell-surface molecule expressed by human interdigitating reticulum cells, Langerhans cells, and activated lymphocytes is a new member of the Ig superfamily. J. Immunol. 149:735-742.
    • (1992) J. Immunol. , vol.149 , pp. 735-742
    • Zhou, L.-J.1    Schwarting, R.2    Smith, H.M.3    Tedder, T.F.4
  • 45
    • 0029009977 scopus 로고
    • The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing
    • Jiang, W., W.J. Swiggard, C. Huefler, M. Peng, A. Mirza, R.M. Steinman, and M.C. Nussenzweig. 1995. The receptor DEC-205 expressed by dendritic cells and thymic epithelial cells is involved in antigen processing. Nature (Loud.). 3275: 151-155.
    • (1995) Nature (Loud.) , vol.3275 , pp. 151-155
    • Jiang, W.1    Swiggard, W.J.2    Huefler, C.3    Peng, M.4    Mirza, A.5    Steinman, R.M.6    Nussenzweig, M.C.7
  • 46
    • 0024360163 scopus 로고
    • A human rel proto-oncogene cDNA containing an Alu fragment as a potential coding exon
    • Brownell, E., N. Mittereder, and N.R. Rice. 1989. A human rel proto-oncogene cDNA containing an Alu fragment as a potential coding exon. Oncogene. 4:935-942.
    • (1989) Oncogene , vol.4 , pp. 935-942
    • Brownell, E.1    Mittereder, N.2    Rice, N.R.3
  • 47
    • 0029953942 scopus 로고    scopus 로고
    • Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors
    • Uren, A.g., M. Pakusch, C.J. Hawkins, K.L. Puls, and D.L. Vaux. 1996. Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors. Proc. Natl. Acad. Sci. USA. 93:4974-4978.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4974-4978
    • Uren, A.G.1    Pakusch, M.2    Hawkins, C.J.3    Puls, K.L.4    Vaux, D.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.