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Volumn 288, Issue 50, 2013, Pages 36083-36093

CD154 is released from t-cells by a disintegrin and metalloproteinase domain-containing protein 10 (ADAM10) and ADAM17 in a CD40 protein-dependent manner

Author keywords

[No Author keywords available]

Indexed keywords

DOMAIN-CONTAINING PROTEINS; MATRIX METALLOPROTEINASES; METALLOPROTEINASES; PRO-INFLAMMATORY CYTOKINES; PROTEIN KINASE C; THERAPEUTIC TARGETS; TRANS-MEMBRANE PROTEINS; TUMOR NECROSIS FACTORS;

EID: 84890350704     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.506220     Document Type: Article
Times cited : (47)

References (34)
  • 5
    • 0037064542 scopus 로고    scopus 로고
    • The role of soluble receptors in cytokine biology: The agonistic properties of the sIL-6R/IL-6 complex
    • Jones, S. A., and Rose-John, S. (2002) The role of soluble receptors in cytokine biology: the agonistic properties of the sIL-6R/IL-6 complex. Biochim. Biophys. Acta 1592, 251-263
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 251-263
    • Jones, S.A.1    Rose-John, S.2
  • 6
    • 0035280017 scopus 로고    scopus 로고
    • Characterization of soluble CD40 ligand released from human activated platelets
    • Jin, Y., Nonoyama, S., Morio, T., Imai, K., Ochs, H. D., and Mizutani, S. (2001) Characterization of soluble CD40 ligand released from human activated platelets. J. Med. Dent. Sci. 48, 23-27
    • (2001) J. Med. Dent. Sci. , vol.48 , pp. 23-27
    • Jin, Y.1    Nonoyama, S.2    Morio, T.3    Imai, K.4    Ochs, H.D.5    Mizutani, S.6
  • 7
    • 0035883087 scopus 로고    scopus 로고
    • The inflammatory action of CD40 ligand (CD154) expressed on activated human platelets is temporally limited by coexpressed CD40
    • Henn, V., Steinbach, S., Büchner, K., Presek, P., and Kroczek, R. A. (2001) The inflammatory action of CD40 ligand (CD154) expressed on activated human platelets is temporally limited by coexpressed CD40. Blood 98, 1047-1054
    • (2001) Blood , vol.98 , pp. 1047-1054
    • Henn, V.1    Steinbach, S.2    Büchner, K.3    Presek, P.4    Kroczek, R.A.5
  • 8
    • 77953627903 scopus 로고    scopus 로고
    • Preliminary evidence for a matrix metalloproteinase-2 (MMP-2)-dependent shedding of soluble CD40 ligand (sCD40L) from activated platelets
    • Reinboldt, S., Wenzel, F., Rauch, B. H., Hohlfeld, T., Grandoch, M., Fischer, J. W., and Weber, A. A. (2009) Preliminary evidence for a matrix metalloproteinase-2 (MMP-2)-dependent shedding of soluble CD40 ligand (sCD40L) from activated platelets. Platelets 20, 441-444
    • (2009) Platelets , vol.20 , pp. 441-444
    • Reinboldt, S.1    Wenzel, F.2    Rauch, B.H.3    Hohlfeld, T.4    Grandoch, M.5    Fischer, J.W.6    Weber, A.A.7
  • 10
    • 67649672271 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 is involved in Crohn's disease-associated platelet hyperactivation through the release of soluble CD40 ligand
    • Menchén, L., Marín-Jiménez, I., Arias-Salgado, E. G., Fontela, T., Hernández-Sampelayo, P., Rodríguez, M. C., and Butta, N. V. (2009) Matrix metalloproteinase 9 is involved in Crohn's disease-associated platelet hyperactivation through the release of soluble CD40 ligand. Gut 58, 920-928
    • (2009) Gut , vol.58 , pp. 920-928
    • Menchén, L.1    Marín-Jiménez, I.2    Arias-Salgado, E.G.3    Fontela, T.4    Hernández-Sampelayo, P.5    Rodríguez, M.C.6    Butta, N.V.7
  • 13
    • 33749007945 scopus 로고    scopus 로고
    • Differential regulation of soluble and membrane CD40L proteins in T cells
    • Matthies, K. M., Newman, J. L., Hodzic, A., and Wingett, D. G. (2006) Differential regulation of soluble and membrane CD40L proteins in T cells. Cell Immunol. 241, 47-58
    • (2006) Cell Immunol. , vol.241 , pp. 47-58
    • Matthies, K.M.1    Newman, J.L.2    Hodzic, A.3    Wingett, D.G.4
  • 17
    • 84865054315 scopus 로고    scopus 로고
    • Requirement of transmembrane domain for CD154 association to lipid rafts and subsequent biological events
    • Benslimane, N., Hassan, G. S., Yacoub, D., and Mourad, W. (2012) Requirement of transmembrane domain for CD154 association to lipid rafts and subsequent biological events. PLoS One 7, e43070
    • (2012) PLoS One , vol.7
    • Benslimane, N.1    Hassan, G.S.2    Yacoub, D.3    Mourad, W.4
  • 18
    • 0028365149 scopus 로고
    • T lymphocyte T cell-B cell-activating molecule/CD40-L molecules induce normal B cells or chronic lymphocytic leukemia B cells to express CD80 (B7/BB-1) and enhance their costimulatory activity
    • Yellin, M. J., Sinning, J., Covey, L. R., Sherman, W., Lee, J. J., Glickman-Nir, E., Sippel, K. C., Rogers, J., Cleary, A. M., and Parker, M. (1994) T lymphocyte T cell-B cell-activating molecule/CD40-L molecules induce normal B cells or chronic lymphocytic leukemia B cells to express CD80 (B7/BB-1) and enhance their costimulatory activity. J. Immunol. 153, 666-674
    • (1994) J. Immunol. , vol.153 , pp. 666-674
    • Yellin, M.J.1    Sinning, J.2    Covey, L.R.3    Sherman, W.4    Lee, J.J.5    Glickman-Nir, E.6    Sippel, K.C.7    Rogers, J.8    Cleary, A.M.9    Parker, M.10
  • 19
    • 79953229244 scopus 로고    scopus 로고
    • Crystallographic and mutational analysis of the CD40-CD154 complex and its implications for receptor activation
    • An, H. J., Kim, Y. J., Song, D. H., Park, B. S., Kim, H. M., Lee, J. D., Paik, S. G., Lee, J. O., and Lee, H. (2011) Crystallographic and mutational analysis of the CD40-CD154 complex and its implications for receptor activation. J. Biol. Chem. 286, 11226-11235
    • (2011) J. Biol. Chem. , vol.286 , pp. 11226-11235
    • An, H.J.1    Kim, Y.J.2    Song, D.H.3    Park, B.S.4    Kim, H.M.5    Lee, J.D.6    Paik, S.G.7    Lee, J.O.8    Lee, H.9
  • 20
    • 78751479184 scopus 로고    scopus 로고
    • Low cholesterol triggers membrane microdomain-dependent CD44 shedding and suppresses tumor cell migration
    • Murai, T., Maruyama, Y., Mio, K., Nishiyama, H., Suga, M., and Sato, C. (2011) Low cholesterol triggers membrane microdomain-dependent CD44 shedding and suppresses tumor cell migration. J. Biol. Chem. 286, 1999-2007
    • (2011) J. Biol. Chem. , vol.286 , pp. 1999-2007
    • Murai, T.1    Maruyama, Y.2    Mio, K.3    Nishiyama, H.4    Suga, M.5    Sato, C.6
  • 22
    • 34247198835 scopus 로고    scopus 로고
    • Shedding of the p75NTR neurotrophin receptor is modulated by lipid rafts
    • Gil, C., Cubí, R., and Aguilera, J. (2007) Shedding of the p75NTR neurotrophin receptor is modulated by lipid rafts. FEBS Lett. 581, 1851-1858
    • (2007) FEBS Lett. , vol.581 , pp. 1851-1858
    • Gil, C.1    Cubí, R.2    Aguilera, J.3
  • 23
    • 80053030745 scopus 로고    scopus 로고
    • Shedding of the Mer tyrosine kinase receptor is mediated by ADAM17 protein through a pathway involving reactive oxygen species, protein kinase Cδ, and p38 mitogen-activated protein kinase (MAPK)
    • Thorp, E., Vaisar, T., Subramanian, M., Mautner, L., Blobel, C., and Tabas, I. (2011) Shedding of the Mer tyrosine kinase receptor is mediated by ADAM17 protein through a pathway involving reactive oxygen species, protein kinase Cδ, and p38 mitogen-activated protein kinase (MAPK). J. Biol. Chem. 286, 33335-33344
    • (2011) J. Biol. Chem. , vol.286 , pp. 33335-33344
    • Thorp, E.1    Vaisar, T.2    Subramanian, M.3    Mautner, L.4    Blobel, C.5    Tabas, I.6
  • 24
    • 77952574514 scopus 로고    scopus 로고
    • The cytoplasmic domains of TNFα-converting enzyme (TACE/ADAM17) and L-selectin are regulated differently by p38 MAPK and PKC to promote ectodomain shedding
    • Killock, D. J., and Ivetić, A. (2010) The cytoplasmic domains of TNFα-converting enzyme (TACE/ADAM17) and L-selectin are regulated differently by p38 MAPK and PKC to promote ectodomain shedding. Biochem. J. 428, 293-304
    • (2010) Biochem. J. , vol.428 , pp. 293-304
    • Killock, D.J.1    Ivetić, A.2
  • 25
    • 76849107016 scopus 로고    scopus 로고
    • Direct activation of TACE-mediated ectodomain shedding by p38MAPkinase regulates EGF receptor-dependent cell proliferation
    • Xu, P., and Derynck, R. (2010) Direct activation of TACE-mediated ectodomain shedding by p38MAPkinase regulates EGF receptor-dependent cell proliferation. Mol. Cell 37, 551-566
    • (2010) Mol. Cell , vol.37 , pp. 551-566
    • Xu, P.1    Derynck, R.2
  • 28
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D., and Simons, K. (2010) Lipid rafts as a membrane-organizing principle. Science 327, 46-50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 29
    • 80655149468 scopus 로고    scopus 로고
    • Different signaling pathways stimulate a disintegrin and metalloprotease-17 (ADAM17) in neutrophils during apoptosis and activation
    • Wang, Y., Robertson, J. D., and Walcheck, B. (2011) Different signaling pathways stimulate a disintegrin and metalloprotease-17 (ADAM17) in neutrophils during apoptosis and activation. J. Biol. Chem. 286, 38980-38988
    • (2011) J. Biol. Chem. , vol.286 , pp. 38980-38988
    • Wang, Y.1    Robertson, J.D.2    Walcheck, B.3
  • 31
    • 65549120390 scopus 로고    scopus 로고
    • ADAM10-mediated N-cadherin cleavage is protein kinase C-α-dependent and promotes glioblastoma cell migration
    • Kohutek, Z. A., diPierro, C. G., Redpath, G. T., and Hussaini, I. M. (2009) ADAM10-mediated N-cadherin cleavage is protein kinase C-α-dependent and promotes glioblastoma cell migration. J. Neurosci. 29, 4605-4615
    • (2009) J. Neurosci. , vol.29 , pp. 4605-4615
    • Kohutek, Z.A.1    DiPierro, C.G.2    Redpath, G.T.3    Hussaini, I.M.4
  • 33
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase, H., and Woessner, J. F., Jr. (1999) Matrix metalloproteinases. J. Biol. Chem. 274, 21491-21494
    • (1999) J. Biol. Chem. , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.