메뉴 건너뛰기




Volumn 36, Issue 4, 2006, Pages 968-976

ADAM17 activity during human neutrophil activation and apoptosis

Author keywords

Apoptosis; Human; Inflammation; Neutrophil

Indexed keywords

COMPLEMENT RECEPTOR; FAS ANTIGEN; FORMYLPEPTIDE; L SELECTIN; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

EID: 33645955275     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200535257     Document Type: Article
Times cited : (50)

References (63)
  • 1
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • Arribas, J. and Borroto, A., Protein ectodomain shedding. Chem. Rev. 2002. 102: 4627-4638.
    • (2002) Chem. Rev. , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 2
    • 0036185667 scopus 로고    scopus 로고
    • Functional and biochemical characterization of ADAMS and their predicted role in protein ectodomain shedding
    • Blobel, C. P., Functional and biochemical characterization of ADAMS and their predicted role in protein ectodomain shedding. Inflamm. Res. 2002. 51: 83-84.
    • (2002) Inflamm. Res. , vol.51 , pp. 83-84
    • Blobel, C.P.1
  • 3
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss, M. L., Jin, S. L., Milla, M. E., Bickett, D. M., Burkhart, W., Carter, H. L., Chen, W. J. et al., Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 1997. 385: 733-736.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Bickett, D.M.4    Burkhart, W.5    Carter, H.L.6    Chen, W.J.7
  • 6
    • 0032846604 scopus 로고    scopus 로고
    • Cutting edge: A dominant negative form of TNF-alpha converting enzyme inhibits proTNF and TNFRII secretion
    • Solomon, K. A., Pesti, N., Wu, G. and Newton, R. C., Cutting edge: a dominant negative form of TNF-alpha converting enzyme inhibits proTNF and TNFRII secretion. J. Immunol. 1999. 163: 4105-4108.
    • (1999) J. Immunol. , vol.163 , pp. 4105-4108
    • Solomon, K.A.1    Pesti, N.2    Wu, G.3    Newton, R.C.4
  • 7
    • 0034640286 scopus 로고    scopus 로고
    • Functional analysis of the domain structure of tumor necrosis factor- alpha converting enzyme
    • Reddy, P., Slack, J. L., Davis, R., Cerretti, D. P., Kozlosky, C. J., Blanton, R. A., Shows, D. et al., Functional analysis of the domain structure of tumor necrosis factor- alpha converting enzyme. J. Biol. Chem. 2000. 275: 14608-14614.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14608-14614
    • Reddy, P.1    Slack, J.L.2    Davis, R.3    Cerretti, D.P.4    Kozlosky, C.J.5    Blanton, R.A.6    Shows, D.7
  • 8
    • 0034020230 scopus 로고    scopus 로고
    • The importance of shedding of membrane proteins for cytokine biology
    • Mullberg, J., Althoff, K., Jostock, T. and Rose-John, S., The importance of shedding of membrane proteins for cytokine biology. Eur. Cytokine Netw. 2000. 11: 27-38.
    • (2000) Eur. Cytokine Netw. , vol.11 , pp. 27-38
    • Mullberg, J.1    Althoff, K.2    Jostock, T.3    Rose-John, S.4
  • 9
    • 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. and Della Sbarba, P., TNF-alpha-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation. J. Immunol. 2001. 166: 1583-1589.
    • (2001) J. Immunol. , vol.166 , pp. 1583-1589
    • Rovida, E.1    Paccagnini, A.2    Del Rosso, M.3    Peschon, J.4    Della Sbarba, P.5
  • 10
    • 0141866756 scopus 로고    scopus 로고
    • Cellular cholesterol depletion triggers shedding of the human interleukin-6 receptor by ADAM10 and ADAM17 (TACE)
    • Matthews, V., Schuster, B., Schutze, S., Bussmeyer, I., Ludwig, A., Hundhausen, C., Sadowski, T. et al., Cellular cholesterol depletion triggers shedding of the human interleukin-6 receptor by ADAM10 and ADAM17 (TACE). J. Biol. Chem. 2003. 278: 38829-38839.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38829-38839
    • Matthews, V.1    Schuster, B.2    Schutze, S.3    Bussmeyer, I.4    Ludwig, A.5    Hundhausen, C.6    Sadowski, T.7
  • 11
    • 0141509970 scopus 로고    scopus 로고
    • Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17)
    • Garton, K. J., Gough, P. J., Philalay, J., Wille, P. T., Blobel, C. P., Whitehead, R. H., Dempsey, P. J. and Raines, E. W., Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17). J. Biol. Chem. 2003. 278: 37459-37464.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37459-37464
    • Garton, K.J.1    Gough, P.J.2    Philalay, J.3    Wille, P.T.4    Blobel, C.P.5    Whitehead, R.H.6    Dempsey, P.J.7    Raines, E.W.8
  • 12
    • 4944248857 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates GPIbalpha shedding from platelets in vitro and in vivo
    • Bergmeier, W., Piffath, C. L., Cheng, G., Dole, V. S., Zhang, Y., von Andrian, U. H. and Wagner, D. D., Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates GPIbalpha shedding from platelets in vitro and in vivo. Circ. Res. 2004. 95: 677-683.
    • (2004) Circ. Res. , vol.95 , pp. 677-683
    • Bergmeier, W.1    Piffath, C.L.2    Cheng, G.3    Dole, V.S.4    Zhang, Y.5    von Andrian, U.H.6    Wagner, D.D.7
  • 14
    • 0024420563 scopus 로고
    • Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors
    • Kishimoto, T. K., Jutila, M. A., Berg, E. L. and Butcher, E. C., Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors. Science 1989. 245: 1238-1241.
    • (1989) Science , vol.245 , pp. 1238-1241
    • Kishimoto, T.K.1    Jutila, M.A.2    Berg, E.L.3    Butcher, E.C.4
  • 15
    • 0035477971 scopus 로고    scopus 로고
    • L-selectin shedding is independent of its subsurface structures and topographic distribution
    • Fors, B. P., Goodarzi, K. and von Andrian, U. H., L-selectin shedding is independent of its subsurface structures and topographic distribution. J. Immunol. 2001. 167: 3642-3651.
    • (2001) J. Immunol. , vol.167 , pp. 3642-3651
    • Fors, B.P.1    Goodarzi, K.2    von Andrian, U.H.3
  • 16
    • 0043095391 scopus 로고    scopus 로고
    • TACE/ADAM-17 enzymatic activity is increased in response to cellular stimulation
    • Doedens, J. R., Mahimkar, R. M. and Black, R. A., TACE/ADAM-17 enzymatic activity is increased in response to cellular stimulation. Biochem. Biophys. Res. Commun. 2003. 308: 331-338.
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 331-338
    • Doedens, J.R.1    Mahimkar, R.M.2    Black, R.A.3
  • 17
    • 0034640428 scopus 로고    scopus 로고
    • Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme
    • Doedens, J. R. and Black, R. A., Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme. J. Biol. Chem. 2000. 275: 14598-14607.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14598-14607
    • Doedens, J.R.1    Black, R.A.2
  • 18
    • 20444507968 scopus 로고    scopus 로고
    • Regulation of peritoneal and systemic neutrophil-derived tumor necrosis factor-alpha release in patients with severe peritonitis: Role of tumor necrosis factor-alpha converting enzyme cleavage
    • Kermarrec, N., Selloum, S., Plantefeve, G., Chosidow, D., Paoletti, X., Lopez, A., Mantz, J. et al., Regulation of peritoneal and systemic neutrophil-derived tumor necrosis factor-alpha release in patients with severe peritonitis: role of tumor necrosis factor-alpha converting enzyme cleavage. Crit. Care Med. 2005. 33: 1359-1364.
    • (2005) Crit. Care Med. , vol.33 , pp. 1359-1364
    • Kermarrec, N.1    Selloum, S.2    Plantefeve, G.3    Chosidow, D.4    Paoletti, X.5    Lopez, A.6    Mantz, J.7
  • 19
    • 0002337409 scopus 로고    scopus 로고
    • The N-formylpeptide chemotactic receptors
    • CRC Press, Inc, Boca Raton, FL
    • Murphy, P. M., The N-formylpeptide chemotactic receptors.CRC Press, Inc, Boca Raton, FL 1996
    • (1996)
    • Murphy, P.M.1
  • 20
    • 0344393518 scopus 로고    scopus 로고
    • Regulation of neutrophil apoptosis via death receptors
    • Akgul, C. and Edwards, S. W., Regulation of neutrophil apoptosis via death receptors. Cell Mol. Life Sci. 2003. 60: 2402-2408.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 2402-2408
    • Akgul, C.1    Edwards, S.W.2
  • 21
    • 0037716445 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation
    • Endres, K., Anders, A., Kojro, E., Gilbert, S., Fahrenholz, F. and Postina, R., Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation. Eur. J. Biochem. 2003. 270: 2386-2393.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2386-2393
    • Endres, K.1    Anders, A.2    Kojro, E.3    Gilbert, S.4    Fahrenholz, F.5    Postina, R.6
  • 22
    • 0033821976 scopus 로고    scopus 로고
    • Effects of selective protein kinase C inhibitors on the proteolytic down-regulation of L-selectin from chemoattractant-activated neutrophils
    • Alexander, S. R., Kishimoto, T. K. and Walcheck, B., Effects of selective protein kinase C inhibitors on the proteolytic down-regulation of L-selectin from chemoattractant-activated neutrophils. J. Leukoc. Biol. 2000. 67: 415-422.
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 415-422
    • Alexander, S.R.1    Kishimoto, T.K.2    Walcheck, B.3
  • 23
    • 0025275476 scopus 로고
    • Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils
    • Ord, D. C., Ernst, T. J., Zhou, L. J., Rambaldi, A., Spertini, O., Griffin, J. and Tedder, T. F., Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils. J. Biol. Chem. 1990. 265: 7760-7767.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7760-7767
    • Ord, D.C.1    Ernst, T.J.2    Zhou, L.J.3    Rambaldi, A.4    Spertini, O.5    Griffin, J.6    Tedder, T.F.7
  • 24
    • 0028269635 scopus 로고
    • Membrane proximal cleavage of L-selectin: Identification of the cleavage site and a 6-kD transmembrane peptide fragment of L-selectin
    • Kahn, J., Ingraham, R. H., Shirley, F., Migaki, G. I. and Kishimoto, T. K., Membrane proximal cleavage of L-selectin: Identification of the cleavage site and a 6-kD transmembrane peptide fragment of L-selectin. J. Cell Biol. 1994. 125: 461-470.
    • (1994) J. Cell Biol. , vol.125 , pp. 461-470
    • Kahn, J.1    Ingraham, R.H.2    Shirley, F.3    Migaki, G.I.4    Kishimoto, T.K.5
  • 26
    • 0028919856 scopus 로고
    • A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes
    • Crowe, P. D., Walter, B. N., Mohler, K. M., Otten-Evans, C, Black, R. A. and Ware, C. F., A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes. J. Exp. Med. 1995. 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
  • 28
    • 0031698581 scopus 로고    scopus 로고
    • ADAMS: Focus on the protease domain
    • Black, R. A. and White, J. M., ADAMS: focus on the protease domain. Curr. Opin. Cell Biol. 1998. 10: 654-659.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 29
    • 0029014220 scopus 로고
    • Regulation of cell adhesion molecule expression and function associated with neutrophil apoptosis
    • Dransfield, I., Stocks, S. C. and Haslett, C., Regulation of cell adhesion molecule expression and function associated with neutrophil apoptosis. Blood 1995. 85: 3264-3273.
    • (1995) Blood , vol.85 , pp. 3264-3273
    • Dransfield, I.1    Stocks, S.C.2    Haslett, C.3
  • 30
    • 0029924173 scopus 로고    scopus 로고
    • Shedding of the lymphocyte L-selectin adhesion molecule is inhibited by a hydroxamic acid-based protease inhibitor
    • Feehan, C., Darlak, K., Kahn, J., Walcheck, B., Spatola, A. F. and Kishimoto, T. K., Shedding of the lymphocyte L-selectin adhesion molecule is inhibited by a hydroxamic acid-based protease inhibitor. J. Biol. Chem. 1996. 271: 7019-7024.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7019-7024
    • Feehan, C.1    Darlak, K.2    Kahn, J.3    Walcheck, B.4    Spatola, A.F.5    Kishimoto, T.K.6
  • 31
    • 11544252167 scopus 로고    scopus 로고
    • Neutrophil rolling altered by inhibition of L-selectin shedding in vitro
    • Walcheck, B., Kahn, J., Fisher, J. M., Wang, B. B., Fisk, R. S., Payan, D. G., Feehan, C. et al., Neutrophil rolling altered by inhibition of L-selectin shedding in vitro. Nature 1996. 380: 720-723.
    • (1996) Nature , vol.380 , pp. 720-723
    • Walcheck, B.1    Kahn, J.2    Fisher, J.M.3    Wang, B.B.4    Fisk, R.S.5    Payan, D.G.6    Feehan, C.7
  • 32
    • 0038541768 scopus 로고    scopus 로고
    • Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE)
    • Schlondorff, J., Becherer, J. D. and Blobel, C. P., Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE). Biochem. J. 2000. 347 Pt 1: 131-138.
    • (2000) Biochem. J. , vol.347 , Issue.PART 1 , pp. 131-138
    • Schlondorff, J.1    Becherer, J.D.2    Blobel, C.P.3
  • 33
    • 21044444181 scopus 로고    scopus 로고
    • ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking
    • Soond, S. M., Everson, B., Riches, D. W. and Murphy, G., ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking. J. Cell Sci. 2005. 118: 2371-2380.
    • (2005) J. Cell Sci. , vol.118 , pp. 2371-2380
    • Soond, S.M.1    Everson, B.2    Riches, D.W.3    Murphy, G.4
  • 35
    • 0025172109 scopus 로고
    • Release of tumor necrosis factor by human polymorphonuclear leukocytes
    • Djeu, J. Y., Serbousek, D. and Blanchard, D. K., Release of tumor necrosis factor by human polymorphonuclear leukocytes. Blood 1990. 76: 1405-1409.
    • (1990) Blood , vol.76 , pp. 1405-1409
    • Djeu, J.Y.1    Serbousek, D.2    Blanchard, D.K.3
  • 36
    • 0033966350 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7-dependent release of tumor necrosis factor-alpha in a model of herniated disc resorption
    • Haro, H., Crawford, H. C., Fingleton, B., Shinomiya, K., Spengler, D. M. and Matrisian, L. M., Matrix metalloproteinase-7-dependent release of tumor necrosis factor-alpha in a model of herniated disc resorption. J. Clin. Invest. 2000. 105: 143-150.
    • (2000) J. Clin. Invest. , vol.105 , pp. 143-150
    • Haro, H.1    Crawford, H.C.2    Fingleton, B.3    Shinomiya, K.4    Spengler, D.M.5    Matrisian, L.M.6
  • 38
    • 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, M. S., Ko, S. C., Long, D. L., Brewer, M. T., Rosenzweig, B., Hedl, E., Anderson, L. 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: 24588-24593.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24588-24593
    • Rosendahl, M.S.1    Ko, S.C.2    Long, D.L.3    Brewer, M.T.4    Rosenzweig, B.5    Hedl, E.6    Anderson, L.7
  • 39
    • 0026522926 scopus 로고
    • Rapid activation-independent shedding of leukocyte L-selectin induced by cross-linking of the surface antigen
    • Palecanda, A., Walcheck, B., Bishop, D. K. and Jutila, M. A., Rapid activation-independent shedding of leukocyte L-selectin induced by cross-linking of the surface antigen. Eur. J. Immunol. 1992. 22: 1279-1286.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1279-1286
    • Palecanda, A.1    Walcheck, B.2    Bishop, D.K.3    Jutila, M.A.4
  • 40
    • 0026660377 scopus 로고
    • Soluble L-selectin is present in human plasma at high levels and retains functional activity
    • Schleiffenbaum, B., Spertini, O. and Tedder, T. F., Soluble L-selectin is present in human plasma at high levels and retains functional activity. J. Cell Biol. 1992. 119: 229-238.
    • (1992) J. Cell Biol. , vol.119 , pp. 229-238
    • Schleiffenbaum, B.1    Spertini, O.2    Tedder, T.F.3
  • 43
    • 0036904267 scopus 로고    scopus 로고
    • Soluble L-selectin levels predict survival in sepsis
    • Seidelin, J. B., Nielsen, O. H. and Strom, J., Soluble L-selectin levels predict survival in sepsis. Intensive Care Med. 2002. 28: 1613-1618.
    • (2002) Intensive Care Med. , vol.28 , pp. 1613-1618
    • Seidelin, J.B.1    Nielsen, O.H.2    Strom, J.3
  • 44
    • 0032478798 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase-dependent and -independent intracellular signal transduction pathways leading to apoptosis in human neutrophils
    • Frasch, S. C., Nick, J. A., Fadok, V. A., Bratton, D. L., Worthen, G. S. and Henson, P. M., p38 mitogen-activated protein kinase-dependent and -independent intracellular signal transduction pathways leading to apoptosis in human neutrophils. J. Biol. Chem. 1998. 273: 8389-8397.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8389-8397
    • Frasch, S.C.1    Nick, J.A.2    Fadok, V.A.3    Bratton, D.L.4    Worthen, G.S.5    Henson, P.M.6
  • 45
    • 0033082466 scopus 로고    scopus 로고
    • Role of p38-mitogen-activated protein kinase in spontaneous apoptosis of human neutrophils
    • Aoshiba, K., Yasui, S., Hayashi, M., Tamaoki, J. and Nagai, A., Role of p38-mitogen-activated protein kinase in spontaneous apoptosis of human neutrophils. J. Immunol. 1999. 162: 1692-1700.
    • (1999) J. Immunol. , vol.162 , pp. 1692-1700
    • Aoshiba, K.1    Yasui, S.2    Hayashi, M.3    Tamaoki, J.4    Nagai, A.5
  • 47
    • 0036356391 scopus 로고    scopus 로고
    • p38 Mitogen-activated protein kinase and phosphatidylinositol 3-kinase activities have opposite effects on human neutrophil apoptosis
    • Alvarado-Kristensson, M., Porn-Ares, M. I., Grethe, S., Smith, D., Zheng, L. and Andersson, T., p38 Mitogen-activated protein kinase and phosphatidylinositol 3-kinase activities have opposite effects on human neutrophil apoptosis. FASEB J. 2002. 16: 129-131.
    • (2002) FASEB J. , vol.16 , pp. 129-131
    • Alvarado-Kristensson, M.1    Porn-Ares, M.I.2    Grethe, S.3    Smith, D.4    Zheng, L.5    Andersson, T.6
  • 48
    • 0029960839 scopus 로고    scopus 로고
    • Neutrophils undergo apoptosis following ingestion of Escherichia coli
    • Watson, R. W., Redmond, H. P., Wang, J. H., Condron, C. and Bouchier-Hayes, D., Neutrophils undergo apoptosis following ingestion of Escherichia coli. J. Immunol. 1996. 156: 3986-3992.
    • (1996) J. Immunol. , vol.156 , pp. 3986-3992
    • Watson, R.W.1    Redmond, H.P.2    Wang, J.H.3    Condron, C.4    Bouchier-Hayes, D.5
  • 49
    • 0030483324 scopus 로고    scopus 로고
    • A novel role for the beta 2 integrin CD11b/CD18 in neutrophil apoptosis: A homeostatic mechanism in inflammation
    • Coxon, A., Rieu, P., Barkalow, F. J., Askari, S., Sharpe, A. H., von Andrian, U. H., Arnaout, M. A. and Mayadas, T. N., A novel role for the beta 2 integrin CD11b/CD18 in neutrophil apoptosis: a homeostatic mechanism in inflammation. Immunity 1996. 5: 653-666.
    • (1996) Immunity , vol.5 , pp. 653-666
    • Coxon, A.1    Rieu, P.2    Barkalow, F.J.3    Askari, S.4    Sharpe, A.H.5    von Andrian, U.H.6    Arnaout, M.A.7    Mayadas, T.N.8
  • 50
    • 0037076395 scopus 로고    scopus 로고
    • Global changes in gene expression by human polymorphonuclear leukocytes during receptor-mediated phagocytosis: Cell fate is regulated at the level of gene expression
    • Kobayashi, S. D., Voyich, J. M., Buhl, C. L., Stahl, R. M. and DeLeo, F. R., Global changes in gene expression by human polymorphonuclear leukocytes during receptor-mediated phagocytosis: cell fate is regulated at the level of gene expression. Proc. Natl. Acad. Sci. USA 2002. 99: 6901-6906.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6901-6906
    • Kobayashi, S.D.1    Voyich, J.M.2    Buhl, C.L.3    Stahl, R.M.4    DeLeo, F.R.5
  • 51
    • 0041707781 scopus 로고    scopus 로고
    • Elucidation of molecular events leading to neutrophil apoptosis following phagocytosis: Cross-talk between caspase 8, reactive oxygen species, and MAPK/ERK activation
    • Zhang, B., Hirahashi, J., Cullere, X. and Mayadas, T. N., Elucidation of molecular events leading to neutrophil apoptosis following phagocytosis: cross-talk between caspase 8, reactive oxygen species, and MAPK/ERK activation. J. Biol. Chem. 2003. 278: 28443-28454.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28443-28454
    • Zhang, B.1    Hirahashi, J.2    Cullere, X.3    Mayadas, T.N.4
  • 52
    • 0030767702 scopus 로고    scopus 로고
    • Regulation of neutrophil apoptosis by tumor necrosis factor-alpha: Requirement for TNFR55 and TNFR75 for induction of apoptosis in vitro
    • Murray, J., Barbara, J. A., Dunkley, S. A., Lopez, A. F., Van Ostade, X., Condliffe, A. M., Dransflield, I. et al., Regulation of neutrophil apoptosis by tumor necrosis factor-alpha: requirement for TNFR55 and TNFR75 for induction of apoptosis in vitro. Blood 1997. 90: 2772-2783.
    • (1997) Blood , vol.90 , pp. 2772-2783
    • Murray, J.1    Barbara, J.A.2    Dunkley, S.A.3    Lopez, A.F.4    Van Ostade, X.5    Condliffe, A.M.6    Dransflield, I.7
  • 53
    • 0031938030 scopus 로고    scopus 로고
    • Downregulation of Fas ligand by shedding
    • Tanaka, M., Itai, T., Adachi, M. and Nagata, S., Downregulation of Fas ligand by shedding. Nat. Med. 1998. 4: 31-36.
    • (1998) Nat. Med. , vol.4 , pp. 31-36
    • Tanaka, M.1    Itai, T.2    Adachi, M.3    Nagata, S.4
  • 54
    • 0035117246 scopus 로고    scopus 로고
    • Fas (CD95)-Fas ligand interactions are responsible for monocyte apoptosis occurring as a result of phagocytosis and killing of Staphylococcus aureus
    • Baran, J., Weglarczyk, K., Mysiak, M., Guzik, K., Ernst, M, Flad, H. D. and Pryjma, J., Fas (CD95)-Fas ligand interactions are responsible for monocyte apoptosis occurring as a result of phagocytosis and killing of Staphylococcus aureus. Infect. Immun. 2001. 69: 1287-1297.
    • (2001) Infect. Immun. , vol.69 , pp. 1287-1297
    • Baran, J.1    Weglarczyk, K.2    Mysiak, M.3    Guzik, K.4    Ernst, M.5    Flad, H.D.6    Pryjma, J.7
  • 55
    • 0842287210 scopus 로고    scopus 로고
    • Regulation of tumour necrosis factor-related apoptosis-inducing ligand (TRAIL) and TRAIL receptor expression in human neutrophils
    • Kamohara, H., Matsuyama, W., Shimozato, O., Abe, K., Galligan, C., Hashimoto, S., Matsushima, K. and Yoshimura, T., Regulation of tumour necrosis factor-related apoptosis-inducing ligand (TRAIL) and TRAIL receptor expression in human neutrophils. Immunology 2004. 111: 186-194.
    • (2004) Immunology , vol.111 , pp. 186-194
    • Kamohara, H.1    Matsuyama, W.2    Shimozato, O.3    Abe, K.4    Galligan, C.5    Hashimoto, S.6    Matsushima, K.7    Yoshimura, T.8
  • 56
    • 0025210021 scopus 로고
    • Identification of a human peripheral lymph node homing receptor: A rapidly down-regulated adhesion molecule
    • Kishimoto, T. K., Jutila, M. A. and Butcher, E. C., Identification of a human peripheral lymph node homing receptor: A rapidly down-regulated adhesion molecule. Proc. Natl. Acad. Sci. USA 1990. 87: 2244-2248.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2244-2248
    • Kishimoto, T.K.1    Jutila, M.A.2    Butcher, E.C.3
  • 57
    • 0022617584 scopus 로고
    • Contributions of the Mac-1 glycoprotein family to adherence-dependent granulocyte functions: Structure-function assessments employing subunit-specific monoclonal antibodies
    • Anderson, D. C., Miller, L. J., Schmalstieg, F. C., Rothlein, R. and Springer, T. A., Contributions of the Mac-1 glycoprotein family to adherence-dependent granulocyte functions: Structure-function assessments employing subunit-specific monoclonal antibodies. J. Immunol. 1986. 137: 15-27.
    • (1986) J. Immunol. , vol.137 , pp. 15-27
    • Anderson, D.C.1    Miller, L.J.2    Schmalstieg, F.C.3    Rothlein, R.4    Springer, T.A.5
  • 58
    • 0038546822 scopus 로고    scopus 로고
    • Small molecule LFA-1 antagonists compete with an anti-LFA-1 monoclonal antibody for binding to the CD11a I domain: Development of a flow-cytometry-based receptor occupancy assay
    • Woska, J. R. Jr., Last-Barney, K., Rothlein, R., Kroe, R. R., Reilly, P. L., Jeanfavre, D. D., Mainolfi, E. A. et al., Small molecule LFA-1 antagonists compete with an anti-LFA-1 monoclonal antibody for binding to the CD11a I domain: development of a flow-cytometry-based receptor occupancy assay. J. Immunol. Methods 2003. 277: 101-115.
    • (2003) J. Immunol. Methods , vol.277 , pp. 101-115
    • Woska Jr., J.R.1    Last-Barney, K.2    Rothlein, R.3    Kroe, R.R.4    Reilly, P.L.5    Jeanfavre, D.D.6    Mainolfi, E.A.7
  • 59
    • 0037443759 scopus 로고    scopus 로고
    • Down-regulation of proinflammatory capacity during apoptosis in human polymorphonuclear leukocytes
    • Kobayashi, S. D., Voyich, J. M., Braughton, K. R. and DeLeo, F. R., Down-regulation of proinflammatory capacity during apoptosis in human polymorphonuclear leukocytes. J. Immunol. 2003. 170: 3357-3368.
    • (2003) J. Immunol. , vol.170 , pp. 3357-3368
    • Kobayashi, S.D.1    Voyich, J.M.2    Braughton, K.R.3    DeLeo, F.R.4
  • 60
    • 0035425359 scopus 로고    scopus 로고
    • The cytoplasmic domain of L-selectin participates in regulating L-selectin endoproteolysis
    • Matala, E., Alexander, S. R., Kishimoto, T. K. and Walcheck, B., The cytoplasmic domain of L-selectin participates in regulating L-selectin endoproteolysis. J. Immunol. 2001. 167: 1617-1623.
    • (2001) J. Immunol. , vol.167 , pp. 1617-1623
    • Matala, E.1    Alexander, S.R.2    Kishimoto, T.K.3    Walcheck, B.4
  • 61
    • 0036625015 scopus 로고    scopus 로고
    • The monoclonal antibody CHO-131 binds to a core 2 O-glycan terminated with sialyl-Lewis x, which is a functional glycan ligand for P-selectin
    • Walcheck, B., Leppanen, A., Cummings, R. D., Knibbs, R. N., Stoolman, L. M., Alexander, S. R., Mattila, P. E. and McEver, R. P., The monoclonal antibody CHO-131 binds to a core 2 O-glycan terminated with sialyl-Lewis x, which is a functional glycan ligand for P-selectin. Blood 2002. 99: 4063-4069.
    • (2002) Blood , vol.99 , pp. 4063-4069
    • Walcheck, B.1    Leppanen, A.2    Cummings, R.D.3    Knibbs, R.N.4    Stoolman, L.M.5    Alexander, S.R.6    Mattila, P.E.7    McEver, R.P.8
  • 62
    • 0032549712 scopus 로고    scopus 로고
    • Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism
    • Kahn, J., Walcheck, B., Migaki, G. I., Jutila, M. A. and Kishimoto, T. K., Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism. Cell 1998. 92: 809-818.
    • (1998) Cell , vol.92 , pp. 809-818
    • Kahn, J.1    Walcheck, B.2    Migaki, G.I.3    Jutila, M.A.4    Kishimoto, T.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.