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Volumn 89, Issue 9, 2007, Pages 1089-1106

The N-formyl peptide receptors and the anaphylatoxin C5a receptors: An overview

Author keywords

Anaphylatoxin; Chemoattractant receptors; Internalization; N formyl peptide; Phosphorylation; Signal transduction

Indexed keywords

COMPLEMENT COMPONENT C5A RECEPTOR; FORMYLPEPTIDE RECEPTOR;

EID: 34547899163     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.02.015     Document Type: Review
Times cited : (135)

References (208)
  • 1
    • 0021333230 scopus 로고
    • Purification and identification of formyl-methionyl-leucyl-phenylalanine as the major peptide neutrophil chemotactic factor produced by Escherichia coli
    • Marasco W.A., Phan S.H., Krutzsch H., Showell H.J., Feltner D.E., Nairn R., Becker E.L., and Ward P.A. Purification and identification of formyl-methionyl-leucyl-phenylalanine as the major peptide neutrophil chemotactic factor produced by Escherichia coli. J. Biol. Chem. 259 (1984) 5430-5439
    • (1984) J. Biol. Chem. , vol.259 , pp. 5430-5439
    • Marasco, W.A.1    Phan, S.H.2    Krutzsch, H.3    Showell, H.J.4    Feltner, D.E.5    Nairn, R.6    Becker, E.L.7    Ward, P.A.8
  • 2
    • 0016795577 scopus 로고
    • The isolation and partial characterization of neutrophil chemotactic factors from Escherichia coli
    • Schiffmann E., Showell H.V., Corcoran B.A., Ward P.A., Smith E., and Becker E.L. The isolation and partial characterization of neutrophil chemotactic factors from Escherichia coli. J. Immunol. 114 (1975) 1831-1837
    • (1975) J. Immunol. , vol.114 , pp. 1831-1837
    • Schiffmann, E.1    Showell, H.V.2    Corcoran, B.A.3    Ward, P.A.4    Smith, E.5    Becker, E.L.6
  • 3
    • 0020062002 scopus 로고
    • Mitochondrial N-formylmethionyl protein as chemoattractants for neutrophils
    • Carp H. Mitochondrial N-formylmethionyl protein as chemoattractants for neutrophils. J. Exp. Med. 155 (1982) 264-275
    • (1982) J. Exp. Med. , vol.155 , pp. 264-275
    • Carp, H.1
  • 4
    • 0030632565 scopus 로고    scopus 로고
    • Structure and function of leukocyte chemoattractant receptors
    • Ye R., and Boulay F. Structure and function of leukocyte chemoattractant receptors. Adv. Pharmacol. 39 (1997) 221-290
    • (1997) Adv. Pharmacol. , vol.39 , pp. 221-290
    • Ye, R.1    Boulay, F.2
  • 5
    • 0017169539 scopus 로고
    • The structure-activity relations of synthetic peptides as chemotactic factors and inducers of lysosomal enzyme secretion for neutrophils
    • Showell H.J., Freer R.J., Zigmond S.H., Schiffmann E., Aswanikumar S., Corcoran B., and Becker E.L. The structure-activity relations of synthetic peptides as chemotactic factors and inducers of lysosomal enzyme secretion for neutrophils. J. Exp. Med. 143 (1976) 1155-1169
    • (1976) J. Exp. Med. , vol.143 , pp. 1155-1169
    • Showell, H.J.1    Freer, R.J.2    Zigmond, S.H.3    Schiffmann, E.4    Aswanikumar, S.5    Corcoran, B.6    Becker, E.L.7
  • 6
    • 0025615835 scopus 로고
    • The human N-formylpeptide receptor. Characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors
    • Boulay F., Tardif M., Brouchon L., and Vignais P. The human N-formylpeptide receptor. Characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors. Biochemistry 29 (1990) 11123-11133
    • (1990) Biochemistry , vol.29 , pp. 11123-11133
    • Boulay, F.1    Tardif, M.2    Brouchon, L.3    Vignais, P.4
  • 7
    • 0025323918 scopus 로고
    • Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA
    • Boulay F., Tardif M., Brouchon L., and Vignais P. Synthesis and use of a novel N-formyl peptide derivative to isolate a human N-formyl peptide receptor cDNA. Biochem. Biophys. Res. Commun. 168 (1990) 1103-1109
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 1103-1109
    • Boulay, F.1    Tardif, M.2    Brouchon, L.3    Vignais, P.4
  • 8
    • 0026736342 scopus 로고
    • Mapping of genes for the human C5a receptor (C5AR), human FMLP receptor (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to chromosome 19
    • Bao L., Gerard N.P., Eddy Jr. R., Shows T.B., and Gerard C. Mapping of genes for the human C5a receptor (C5AR), human FMLP receptor (FPR), and two FMLP receptor homologue orphan receptors (FPRH1, FPRH2) to chromosome 19. Genomics 13 (1992) 437-440
    • (1992) Genomics , vol.13 , pp. 437-440
    • Bao, L.1    Gerard, N.P.2    Eddy Jr., R.3    Shows, T.B.4    Gerard, C.5
  • 9
    • 0026644385 scopus 로고
    • A structural homologue of the N-formyl peptide receptor. Characterization and chromosome mapping of a peptide chemoattractant receptor family
    • Murphy P.M., Ozcelik T., Kenney R.T., Tiffany H.L., McDermott D., and Francke U. A structural homologue of the N-formyl peptide receptor. Characterization and chromosome mapping of a peptide chemoattractant receptor family. J. Biol. Chem. 267 (1992) 7637-7643
    • (1992) J. Biol. Chem. , vol.267 , pp. 7637-7643
    • Murphy, P.M.1    Ozcelik, T.2    Kenney, R.T.3    Tiffany, H.L.4    McDermott, D.5    Francke, U.6
  • 11
    • 0028359379 scopus 로고
    • Identification of a human cDNA encoding a functional high affinity lipoxin A4 receptor
    • Fiore S., Maddox J.F., Perez H.D., and Serhan C.N. Identification of a human cDNA encoding a functional high affinity lipoxin A4 receptor. J. Exp. Med. 180 (1994) 253-260
    • (1994) J. Exp. Med. , vol.180 , pp. 253-260
    • Fiore, S.1    Maddox, J.F.2    Perez, H.D.3    Serhan, C.N.4
  • 14
    • 0035489455 scopus 로고    scopus 로고
    • Contrasting evolution of the human leukocyte N-formylpeptide receptor subtypes FPR and FPRL1R
    • Sahagun-Ruiz A., Colla J.S., Juhn J., Gao J.L., Murphy P.M., and McDermott D.H. Contrasting evolution of the human leukocyte N-formylpeptide receptor subtypes FPR and FPRL1R. Genes Immun. 2 (2001) 335-342
    • (2001) Genes Immun. , vol.2 , pp. 335-342
    • Sahagun-Ruiz, A.1    Colla, J.S.2    Juhn, J.3    Gao, J.L.4    Murphy, P.M.5    McDermott, D.H.6
  • 16
    • 0038459130 scopus 로고    scopus 로고
    • Functional differences between human formyl peptide receptor isoforms 26, 98, and G6
    • Wenzel-Seifert K., and Seifert R. Functional differences between human formyl peptide receptor isoforms 26, 98, and G6. Naunyn Schmiedebergs Arch. Pharmacol. 367 (2003) 509-515
    • (2003) Naunyn Schmiedebergs Arch. Pharmacol. , vol.367 , pp. 509-515
    • Wenzel-Seifert, K.1    Seifert, R.2
  • 17
    • 0034773504 scopus 로고    scopus 로고
    • A proinflammatory peptide from Helicobacter pylori activates monocytes to induce lymphocyte dysfunction and apoptosis
    • Betten A., Bylund J., Cristophe T., Boulay F., Romero A., Hellstrand K., and Dahlgren C. A proinflammatory peptide from Helicobacter pylori activates monocytes to induce lymphocyte dysfunction and apoptosis. J. Clin. Invest. 108 (2001) 1221-1228
    • (2001) J. Clin. Invest. , vol.108 , pp. 1221-1228
    • Betten, A.1    Bylund, J.2    Cristophe, T.3    Boulay, F.4    Romero, A.5    Hellstrand, K.6    Dahlgren, C.7
  • 18
    • 0035877580 scopus 로고    scopus 로고
    • 2 specifically activates neutrophils through FPRL1/LXA4R and is an agonist for the orphan monocyte-expressed chemoattractant receptor FPRL2
    • 2 specifically activates neutrophils through FPRL1/LXA4R and is an agonist for the orphan monocyte-expressed chemoattractant receptor FPRL2. J. Biol. Chem. 276 (2001) 21585-21593
    • (2001) J. Biol. Chem. , vol.276 , pp. 21585-21593
    • Christophe, T.1    Karlsson, A.2    Dugave, C.3    Rabiet, M.J.4    Boulay, F.5    Dahlgren, C.6
  • 20
    • 33751211223 scopus 로고    scopus 로고
    • Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses
    • Migeotte I., Communi D., and Parmentier M. Formyl peptide receptors: a promiscuous subfamily of G protein-coupled receptors controlling immune responses. Cytokine Growth Factor Rev. 17 (2006) 501-519
    • (2006) Cytokine Growth Factor Rev. , vol.17 , pp. 501-519
    • Migeotte, I.1    Communi, D.2    Parmentier, M.3
  • 23
    • 0027154675 scopus 로고
    • Cyclosporin H is a potent and selective formylpeptide receptor antagonist
    • Wenzel-Seifert K., and Seifert R. Cyclosporin H is a potent and selective formylpeptide receptor antagonist. J. Immunol. 150 (1993) 4591-4599
    • (1993) J. Immunol. , vol.150 , pp. 4591-4599
    • Wenzel-Seifert, K.1    Seifert, R.2
  • 24
    • 0032508632 scopus 로고    scopus 로고
    • High constitutive activity of the human formyl peptide receptor
    • Wenzel-Seifert K., Hurt C.M., and Seifert R. High constitutive activity of the human formyl peptide receptor. J. Biol. Chem. 273 (1998) 24181-24189
    • (1998) J. Biol. Chem. , vol.273 , pp. 24181-24189
    • Wenzel-Seifert, K.1    Hurt, C.M.2    Seifert, R.3
  • 25
    • 33746789412 scopus 로고    scopus 로고
    • Peptides derived from HIV-1, HIV-2, Ebola virus, SARS coronavirus and coronavirus 229E exhibit high affinity binding to the formyl peptide receptor
    • Mills J.S. Peptides derived from HIV-1, HIV-2, Ebola virus, SARS coronavirus and coronavirus 229E exhibit high affinity binding to the formyl peptide receptor. Biochim. Biophys. Acta 1762 (2006) 693-703
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 693-703
    • Mills, J.S.1
  • 27
    • 33751565688 scopus 로고    scopus 로고
    • A new staphylococcal anti-inflammatory protein that antagonizes the formyl peptide receptor-like 1
    • Prat C., Bestebroer J., de Haas C.J., van Strijp J.A., and van Kessel K.P. A new staphylococcal anti-inflammatory protein that antagonizes the formyl peptide receptor-like 1. J. Immunol. 177 (2006) 8017-8026
    • (2006) J. Immunol. , vol.177 , pp. 8017-8026
    • Prat, C.1    Bestebroer, J.2    de Haas, C.J.3    van Strijp, J.A.4    van Kessel, K.P.5
  • 28
    • 27544444375 scopus 로고    scopus 로고
    • Integration of virtual screening with high-throughput flow cytometry to identify novel small molecule formylpeptide receptor antagonists
    • Edwards B.S., Bologa C., Young S.M., Balakin K.V., Prossnitz E.R., Savchuck N.P., Sklar L.A., and Oprea T.I. Integration of virtual screening with high-throughput flow cytometry to identify novel small molecule formylpeptide receptor antagonists. Mol. Pharmacol. 68 (2005) 1301-1310
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1301-1310
    • Edwards, B.S.1    Bologa, C.2    Young, S.M.3    Balakin, K.V.4    Prossnitz, E.R.5    Savchuck, N.P.6    Sklar, L.A.7    Oprea, T.I.8
  • 29
    • 2942755913 scopus 로고    scopus 로고
    • Identification of peptides that antagonize formyl peptide receptor-like 1-mediated signaling
    • Bae Y.S., Lee H.Y., Jo E.J., Kim J.I., Kang H.K., Ye R.D., Kwak J.Y., and Ryu S.H. Identification of peptides that antagonize formyl peptide receptor-like 1-mediated signaling. J. Immunol. 173 (2004) 607-614
    • (2004) J. Immunol. , vol.173 , pp. 607-614
    • Bae, Y.S.1    Lee, H.Y.2    Jo, E.J.3    Kim, J.I.4    Kang, H.K.5    Ye, R.D.6    Kwak, J.Y.7    Ryu, S.H.8
  • 31
    • 24744438566 scopus 로고    scopus 로고
    • The two neutrophil members of the formylpeptide receptor family activate the NADPH-oxidase through signals that differ in sensitivity to a gelsolin derived phosphoinositide-binding peptide
    • Fu H., Bjorkman L., Janmey P., Karlsson A., Karlsson J., Movitz C., and Dahlgren C. The two neutrophil members of the formylpeptide receptor family activate the NADPH-oxidase through signals that differ in sensitivity to a gelsolin derived phosphoinositide-binding peptide. BMC Cell Biol. 5 (2004) 50-62
    • (2004) BMC Cell Biol. , vol.5 , pp. 50-62
    • Fu, H.1    Bjorkman, L.2    Janmey, P.3    Karlsson, A.4    Karlsson, J.5    Movitz, C.6    Dahlgren, C.7
  • 32
    • 0009751856 scopus 로고    scopus 로고
    • Identification of the peptides that stimulate the phosphoinositide hydrolysis in lymphocytes cell lines from peptide libraries
    • Baek S.H., Seo J.K., Chae C.-B., Suh P.-G., and Ryu S.H. Identification of the peptides that stimulate the phosphoinositide hydrolysis in lymphocytes cell lines from peptide libraries. J. Biol. Chem. 271 (1996) 8170-8175
    • (1996) J. Biol. Chem. , vol.271 , pp. 8170-8175
    • Baek, S.H.1    Seo, J.K.2    Chae, C.-B.3    Suh, P.-G.4    Ryu, S.H.5
  • 34
    • 0034161336 scopus 로고    scopus 로고
    • The synthetic chemoattractant Trp-Lys-Tyr-Met-Val-dMet activates neutrophils preferentially through the lipoxin A4 receptor
    • Dahlgren C., Christophe T., Boulay F., Madianos P., Rabiet M.-J., and Karlson A. The synthetic chemoattractant Trp-Lys-Tyr-Met-Val-dMet activates neutrophils preferentially through the lipoxin A4 receptor. Blood 95 (2000) 1810-1818
    • (2000) Blood , vol.95 , pp. 1810-1818
    • Dahlgren, C.1    Christophe, T.2    Boulay, F.3    Madianos, P.4    Rabiet, M.-J.5    Karlson, A.6
  • 35
    • 0032742013 scopus 로고    scopus 로고
    • Utilization of two seven-transmembrane, G protein-coupled receptors, formyl peptide receptor-like 1 and formyl peptide receptor, by synthetic hexapeptide WKYMVm for human phagocyte activation
    • Le Y., Gong W., Li B., Dunlop N.M., Shen W., Su S.B., Ye R.D., and Wang J.M. Utilization of two seven-transmembrane, G protein-coupled receptors, formyl peptide receptor-like 1 and formyl peptide receptor, by synthetic hexapeptide WKYMVm for human phagocyte activation. J. Immunol. 163 (1999) 6777-6784
    • (1999) J. Immunol. , vol.163 , pp. 6777-6784
    • Le, Y.1    Gong, W.2    Li, B.3    Dunlop, N.M.4    Shen, W.5    Su, S.B.6    Ye, R.D.7    Wang, J.M.8
  • 37
    • 0033848603 scopus 로고    scopus 로고
    • N36, a synthetic N-terminal heptad repeat domain of the HIV-1 envelope protein gp41, is an activator of human phagocytes
    • Le Y., Jiang S., Hu J., Gong W., Su S., Dunlop N.M., Shen W., Li B., and Ming Wang J. N36, a synthetic N-terminal heptad repeat domain of the HIV-1 envelope protein gp41, is an activator of human phagocytes. Clin. Immunol. 96 (2000) 236-242
    • (2000) Clin. Immunol. , vol.96 , pp. 236-242
    • Le, Y.1    Jiang, S.2    Hu, J.3    Gong, W.4    Su, S.5    Dunlop, N.M.6    Shen, W.7    Li, B.8    Ming Wang, J.9
  • 38
    • 0000934194 scopus 로고    scopus 로고
    • T20/DP178, an ectodomain peptide of human immunodeficiency virus type 1 gp41, is an activator of human phagocyte N-formyl peptide receptor
    • Su S.B., Gong W.H., Gao J.L., Shen W.P., Grimm M.C., Deng X., Murphy P.M., Oppenheim J.J., and Wang J.M. T20/DP178, an ectodomain peptide of human immunodeficiency virus type 1 gp41, is an activator of human phagocyte N-formyl peptide receptor. Blood 93 (1999) 3885-3892
    • (1999) Blood , vol.93 , pp. 3885-3892
    • Su, S.B.1    Gong, W.H.2    Gao, J.L.3    Shen, W.P.4    Grimm, M.C.5    Deng, X.6    Murphy, P.M.7    Oppenheim, J.J.8    Wang, J.M.9
  • 39
    • 0033567052 scopus 로고    scopus 로고
    • A synthetic peptide derived from human immunodeficiency virus type 1 gp120 downregulates the expression and function of chemokine receptors CCR5 and CXCR4 in monocytes by activating the 7-transmembrane G-protein-coupled receptor FPRL1/LXA4R
    • Deng X., Ueda H., Su S.B., Gong W., Dunlop N.M., Gao J.-L., Murphy P.M., and Wang J.M. A synthetic peptide derived from human immunodeficiency virus type 1 gp120 downregulates the expression and function of chemokine receptors CCR5 and CXCR4 in monocytes by activating the 7-transmembrane G-protein-coupled receptor FPRL1/LXA4R. Blood 94 (1999) 1165-1173
    • (1999) Blood , vol.94 , pp. 1165-1173
    • Deng, X.1    Ueda, H.2    Su, S.B.3    Gong, W.4    Dunlop, N.M.5    Gao, J.-L.6    Murphy, P.M.7    Wang, J.M.8
  • 40
    • 0034720462 scopus 로고    scopus 로고
    • Activation of the chemotactic peptide receptor FPRL1 in monocytes phosphorylates the chemokine receptor CCR5 and attenuates cell response to selected chemokines
    • Shen W., Proost P., Li B., Gong W., Le Y., Sargeant R., Murphy P.M., Van Damme J., and Wang J.B. Activation of the chemotactic peptide receptor FPRL1 in monocytes phosphorylates the chemokine receptor CCR5 and attenuates cell response to selected chemokines. Biochem. Biophys. Res. Commun. 272 (2000) 276-283
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 276-283
    • Shen, W.1    Proost, P.2    Li, B.3    Gong, W.4    Le, Y.5    Sargeant, R.6    Murphy, P.M.7    Van Damme, J.8    Wang, J.B.9
  • 41
    • 23844446792 scopus 로고    scopus 로고
    • Human mitochondria-derived N-formylated peptides are novel agonists equally active on FPR and FPRL1, while Listeria monocytogenes-derived peptides preferentially activate FPR
    • Rabiet M.J., Huet E., and Boulay F. Human mitochondria-derived N-formylated peptides are novel agonists equally active on FPR and FPRL1, while Listeria monocytogenes-derived peptides preferentially activate FPR. Eur. J. Immunol. 35 (2005) 2486-2495
    • (2005) Eur. J. Immunol. , vol.35 , pp. 2486-2495
    • Rabiet, M.J.1    Huet, E.2    Boulay, F.3
  • 43
    • 13544274448 scopus 로고    scopus 로고
    • A proinflammatory peptide from herpes simplex virus type 2 glycoprotein G affects neutrophil, monocyte, and NK cell functions
    • Bellner L., Thoren F., Nygren E., Liljeqvist J.A., Karlsson A., and Eriksson K. A proinflammatory peptide from herpes simplex virus type 2 glycoprotein G affects neutrophil, monocyte, and NK cell functions. J. Immunol. 174 (2005) 2235-2241
    • (2005) J. Immunol. , vol.174 , pp. 2235-2241
    • Bellner, L.1    Thoren, F.2    Nygren, E.3    Liljeqvist, J.A.4    Karlsson, A.5    Eriksson, K.6
  • 44
    • 0000485181 scopus 로고    scopus 로고
    • A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells
    • Su S.B., Gong W., Gao J.-L., Shen W., Murphy P.M., Oppenheim J.J., and Wang J.M. A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells. J. Exp. Med. 189 (1999) 395-402
    • (1999) J. Exp. Med. , vol.189 , pp. 395-402
    • Su, S.B.1    Gong, W.2    Gao, J.-L.3    Shen, W.4    Murphy, P.M.5    Oppenheim, J.J.6    Wang, J.M.7
  • 46
    • 18244407519 scopus 로고    scopus 로고
    • Role of formyl peptide receptor-like 1 (FPRL1/FPR2) in mononuclear phagocyte responses in Alzheimer disease
    • Iribarren P., Zhou Y., Hu J., Le Y., and Wang J.M. Role of formyl peptide receptor-like 1 (FPRL1/FPR2) in mononuclear phagocyte responses in Alzheimer disease. Immunol. Res. 31 (2005) 165-176
    • (2005) Immunol. Res. , vol.31 , pp. 165-176
    • Iribarren, P.1    Zhou, Y.2    Hu, J.3    Le, Y.4    Wang, J.M.5
  • 48
    • 2442705358 scopus 로고    scopus 로고
    • Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor
    • Ying G., Iribarren P., Zhou Y., Gong W., Zhang N., Yu Z.X., Le Y., Cui Y., and Wang J.M. Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor. J. Immunol. 172 (2004) 7078-7085
    • (2004) J. Immunol. , vol.172 , pp. 7078-7085
    • Ying, G.1    Iribarren, P.2    Zhou, Y.3    Gong, W.4    Zhang, N.5    Yu, Z.X.6    Le, Y.7    Cui, Y.8    Wang, J.M.9
  • 50
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human blood neutrophils, monocytes, and T cells
    • De Y., Chen Q., Schmidt A.P., Anderson G.M., Wang J.M., Woosters J., and Oppenheim J.J. LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human blood neutrophils, monocytes, and T cells. J. Exp. Med. 192 (2000) 1069-1074
    • (2000) J. Exp. Med. , vol.192 , pp. 1069-1074
    • De, Y.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Woosters, J.6    Oppenheim, J.J.7
  • 52
    • 0033634942 scopus 로고    scopus 로고
    • A novel ligand of the formyl peptide receptor: annexin I regulates neutrophil extravasation by interacting with the FPR
    • Walther A., Riehemann K., and Gerke V. A novel ligand of the formyl peptide receptor: annexin I regulates neutrophil extravasation by interacting with the FPR. Mol. Cell 5 (2000) 831-840
    • (2000) Mol. Cell , vol.5 , pp. 831-840
    • Walther, A.1    Riehemann, K.2    Gerke, V.3
  • 53
    • 33344459382 scopus 로고    scopus 로고
    • Annexin 1 and its bioactive peptide inhibit neutrophil-endothelium interactions under flow: indication of distinct receptor involvement
    • Hayhoe R.P., Kamal A.M., Solito E., Flower R.J., Cooper D., and Perretti M. Annexin 1 and its bioactive peptide inhibit neutrophil-endothelium interactions under flow: indication of distinct receptor involvement. Blood 107 (2006) 2123-2130
    • (2006) Blood , vol.107 , pp. 2123-2130
    • Hayhoe, R.P.1    Kamal, A.M.2    Solito, E.3    Flower, R.J.4    Cooper, D.5    Perretti, M.6
  • 54
    • 24744456325 scopus 로고    scopus 로고
    • Neutrophil NADPH-oxidase activation by an annexin AI peptide is transduced by the formyl peptide receptor (FPR), whereas an inhibitory signal is generated independently of the FPR family receptors
    • Karlsson J., Fu H., Boulay F., Dahlgren C., Hellstrand K., and Movitz C. Neutrophil NADPH-oxidase activation by an annexin AI peptide is transduced by the formyl peptide receptor (FPR), whereas an inhibitory signal is generated independently of the FPR family receptors. J. Leukoc. Biol. 78 (2005) 762-771
    • (2005) J. Leukoc. Biol. , vol.78 , pp. 762-771
    • Karlsson, J.1    Fu, H.2    Boulay, F.3    Dahlgren, C.4    Hellstrand, K.5    Movitz, C.6
  • 55
    • 33644518230 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase-activating polypeptide 27 is a functional ligand for formyl peptide receptor-like 1
    • Kim Y., Lee B.D., Kim O., Bae Y.S., Lee T., Suh P.G., and Ryu S.H. Pituitary adenylate cyclase-activating polypeptide 27 is a functional ligand for formyl peptide receptor-like 1. J. Immunol. 176 (2006) 2969-2975
    • (2006) J. Immunol. , vol.176 , pp. 2969-2975
    • Kim, Y.1    Lee, B.D.2    Kim, O.3    Bae, Y.S.4    Lee, T.5    Suh, P.G.6    Ryu, S.H.7
  • 56
    • 0033557172 scopus 로고    scopus 로고
    • Impaired antibacterial host defense in mice lacking the N-formylpeptide receptor
    • Gao J.L., Lee E.J., and Murphy P.M. Impaired antibacterial host defense in mice lacking the N-formylpeptide receptor. J. Exp. Med. 189 (1999) 657-662
    • (1999) J. Exp. Med. , vol.189 , pp. 657-662
    • Gao, J.L.1    Lee, E.J.2    Murphy, P.M.3
  • 57
    • 0025890276 scopus 로고
    • Expression cloning of a receptor for C5a anaphylatoxin on differentiated HL-60 cells
    • Boulay F., Mery L., Tardif M., Brouchon L., and Vignais P. Expression cloning of a receptor for C5a anaphylatoxin on differentiated HL-60 cells. Biochemistry 30 (1991) 2993-2999
    • (1991) Biochemistry , vol.30 , pp. 2993-2999
    • Boulay, F.1    Mery, L.2    Tardif, M.3    Brouchon, L.4    Vignais, P.5
  • 58
    • 0026078539 scopus 로고
    • The chemotactic receptor for human C5a anaphylatoxin
    • Gerard N.P., and Gerard C. The chemotactic receptor for human C5a anaphylatoxin. Nature 349 (1991) 614-617
    • (1991) Nature , vol.349 , pp. 614-617
    • Gerard, N.P.1    Gerard, C.2
  • 59
    • 0028201342 scopus 로고
    • C5A anaphylatoxin and its seven transmembrane-segment receptor
    • Gerard C., and Gerard N.P. C5A anaphylatoxin and its seven transmembrane-segment receptor. Annu. Rev. Immunol. 12 (1994) 775-808
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 775-808
    • Gerard, C.1    Gerard, N.P.2
  • 60
    • 0033067822 scopus 로고    scopus 로고
    • Characterization of a polymorphism in the coding region of the human C5a anaphylatoxin receptor
    • Marceau F., Bachvarova M., Bergeron J., and Bachvarov D.R. Characterization of a polymorphism in the coding region of the human C5a anaphylatoxin receptor. Immunogenetics 49 (1999) 618-619
    • (1999) Immunogenetics , vol.49 , pp. 618-619
    • Marceau, F.1    Bachvarova, M.2    Bergeron, J.3    Bachvarov, D.R.4
  • 62
    • 0029046606 scopus 로고
    • Probing the "message:address" sites for chemoattractant binding to the C5a receptor
    • Kolakowski L.F., Lu B., Gerard C., and Gerard N. Probing the "message:address" sites for chemoattractant binding to the C5a receptor. J. Biol. Chem. 270 (1995) 18077-18082
    • (1995) J. Biol. Chem. , vol.270 , pp. 18077-18082
    • Kolakowski, L.F.1    Lu, B.2    Gerard, C.3    Gerard, N.4
  • 63
    • 0029795542 scopus 로고    scopus 로고
    • The C5a chemoattractant receptor mediates mucosal defence to infection
    • Höpken U.E., Lu B., Gerard N.P., and Gerard C. The C5a chemoattractant receptor mediates mucosal defence to infection. Nature 383 (1996) 86-89
    • (1996) Nature , vol.383 , pp. 86-89
    • Höpken, U.E.1    Lu, B.2    Gerard, N.P.3    Gerard, C.4
  • 64
    • 0036721025 scopus 로고    scopus 로고
    • Essential role of the C5a receptor in E. coli-induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blood model of inflammation
    • Mollnes T.E., Brekke O.L., Fung M., Fure H., Christiansen D., Bergseth G., Videm V., Lappegard K.T., Kohl J., and Lambris J.D. Essential role of the C5a receptor in E. coli-induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blood model of inflammation. Blood 100 (2002) 1869-1877
    • (2002) Blood , vol.100 , pp. 1869-1877
    • Mollnes, T.E.1    Brekke, O.L.2    Fung, M.3    Fure, H.4    Christiansen, D.5    Bergseth, G.6    Videm, V.7    Lappegard, K.T.8    Kohl, J.9    Lambris, J.D.10
  • 69
    • 33750435578 scopus 로고    scopus 로고
    • Complement-related molecular events in sepsis leading to heart failure
    • Hoesel L.M., Niederbichler A.D., and Ward P.A. Complement-related molecular events in sepsis leading to heart failure. Mol. Immunol. 44 (2007) 95-102
    • (2007) Mol. Immunol. , vol.44 , pp. 95-102
    • Hoesel, L.M.1    Niederbichler, A.D.2    Ward, P.A.3
  • 70
    • 0033709969 scopus 로고    scopus 로고
    • A putative chemoattractant receptor, C5L2, is expressed in granulocyte and immature dendritic cells, but not in mature dendritic cells
    • Ohno M., Hirata T., Enomoto M., Araki T., Ishimaru H., and Takahashi T.A. A putative chemoattractant receptor, C5L2, is expressed in granulocyte and immature dendritic cells, but not in mature dendritic cells. Mol. Immunol. 37 (2000) 407-412
    • (2000) Mol. Immunol. , vol.37 , pp. 407-412
    • Ohno, M.1    Hirata, T.2    Enomoto, M.3    Araki, T.4    Ishimaru, H.5    Takahashi, T.A.6
  • 72
    • 0036510770 scopus 로고    scopus 로고
    • The orphan receptor C5L2 has high affinity binding sites for complement fragments C5a and C5a des-Arg(74)
    • Cain S.A., and Monk P.N. The orphan receptor C5L2 has high affinity binding sites for complement fragments C5a and C5a des-Arg(74). J. Biol. Chem. 277 (2002) 7165-7169
    • (2002) J. Biol. Chem. , vol.277 , pp. 7165-7169
    • Cain, S.A.1    Monk, P.N.2
  • 74
    • 28844434626 scopus 로고    scopus 로고
    • An anti-inflammatory function for the complement anaphylatoxin C5a-binding protein, C5L2
    • Gerard N.P., Lu B., Liu P., Craig S., Fujiwara Y., Okinaga S., and Gerard C. An anti-inflammatory function for the complement anaphylatoxin C5a-binding protein, C5L2. J. Biol. Chem. 280 (2005) 39677-39680
    • (2005) J. Biol. Chem. , vol.280 , pp. 39677-39680
    • Gerard, N.P.1    Lu, B.2    Liu, P.3    Craig, S.4    Fujiwara, Y.5    Okinaga, S.6    Gerard, C.7
  • 78
    • 0034283951 scopus 로고    scopus 로고
    • Differential regulation of responsiveness to fMLP and C5a upon dendritic cell maturation: correlation with receptor expression
    • Yang D., Chen Q., Stoll S., Chen X., Howard O.M., and Oppenheim J.J. Differential regulation of responsiveness to fMLP and C5a upon dendritic cell maturation: correlation with receptor expression. J. Immunol. 165 (2000) 2694-2702
    • (2000) J. Immunol. , vol.165 , pp. 2694-2702
    • Yang, D.1    Chen, Q.2    Stoll, S.3    Chen, X.4    Howard, O.M.5    Oppenheim, J.J.6
  • 79
    • 0036744006 scopus 로고    scopus 로고
    • Human dendritic cells express functional formyl peptide receptor-like-2 (FPRL2) throughout maturation
    • Yang D., Chen Q., Gertz B., He R., Phulsuksombati M., Ye R.D., and Oppenheim J.J. Human dendritic cells express functional formyl peptide receptor-like-2 (FPRL2) throughout maturation. J. Leukoc. Biol. 72 (2002) 598-607
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 598-607
    • Yang, D.1    Chen, Q.2    Gertz, B.3    He, R.4    Phulsuksombati, M.5    Ye, R.D.6    Oppenheim, J.J.7
  • 80
    • 0035869443 scopus 로고    scopus 로고
    • Differential regulation of formyl peptide receptor-like 1 expression during the differentiation of monocytes to dendritic cells and macrophages
    • Yang D., Chen Q., Le Y., Wang J.M., and Oppenheim J.J. Differential regulation of formyl peptide receptor-like 1 expression during the differentiation of monocytes to dendritic cells and macrophages. J. Immunol. 166 (2001) 4092-4098
    • (2001) J. Immunol. , vol.166 , pp. 4092-4098
    • Yang, D.1    Chen, Q.2    Le, Y.3    Wang, J.M.4    Oppenheim, J.J.5
  • 81
    • 0028863749 scopus 로고
    • Identification and characterization of the complement C5a anaphylatoxin receptor on human astrocytes
    • Gasque P., Chan P., Fontaine M., Ischenko A., Lamacz M., Götze O., and Morgan B.P. Identification and characterization of the complement C5a anaphylatoxin receptor on human astrocytes. J. Immunol. 155 (1995) 4882-4889
    • (1995) J. Immunol. , vol.155 , pp. 4882-4889
    • Gasque, P.1    Chan, P.2    Fontaine, M.3    Ischenko, A.4    Lamacz, M.5    Götze, O.6    Morgan, B.P.7
  • 82
    • 0029119287 scopus 로고
    • Expression of the receptors for the C5a anaphylatoxin, interleukin-8 and FMLP by human astrocytes and microglia
    • Lacy M., Jones J., Whittemore S.R., Haviland D.L., Wetsel R.A., and Barnum S.R. Expression of the receptors for the C5a anaphylatoxin, interleukin-8 and FMLP by human astrocytes and microglia. J. Neuroimmunol. 61 (1995) 71-78
    • (1995) J. Neuroimmunol. , vol.61 , pp. 71-78
    • Lacy, M.1    Jones, J.2    Whittemore, S.R.3    Haviland, D.L.4    Wetsel, R.A.5    Barnum, S.R.6
  • 83
    • 6344241861 scopus 로고    scopus 로고
    • Characterization of C3a and C5a receptors in rat cerebellar granule neurons during maturation. Neuroprotective effect of C5a against apoptotic cell death
    • Benard M., Gonzalez B.J., Schouft M.T., Falluel-Morel A., Vaudry D., Chan P., Vaudry H., and Fontaine M. Characterization of C3a and C5a receptors in rat cerebellar granule neurons during maturation. Neuroprotective effect of C5a against apoptotic cell death. J. Biol. Chem. 279 (2004) 43487-43496
    • (2004) J. Biol. Chem. , vol.279 , pp. 43487-43496
    • Benard, M.1    Gonzalez, B.J.2    Schouft, M.T.3    Falluel-Morel, A.4    Vaudry, D.5    Chan, P.6    Vaudry, H.7    Fontaine, M.8
  • 85
    • 0037871469 scopus 로고    scopus 로고
    • Regulation by complement C3a and C5a anaphylatoxins of cytokine production in human umbilical vein endothelial cells
    • Monsinjon T., Gasque P., Chan P., Ischenko A., Brady J.J., and Fontaine M.C. Regulation by complement C3a and C5a anaphylatoxins of cytokine production in human umbilical vein endothelial cells. FASEB J. 17 (2003) 1003-1014
    • (2003) FASEB J. , vol.17 , pp. 1003-1014
    • Monsinjon, T.1    Gasque, P.2    Chan, P.3    Ischenko, A.4    Brady, J.J.5    Fontaine, M.C.6
  • 86
    • 0037103283 scopus 로고    scopus 로고
    • Complement c3a and c5a induce different signal transduction cascades in endothelial cells
    • Schraufstatter I.U., Trieu K., Sikora L., Sriramarao P., and DiScipio R. Complement c3a and c5a induce different signal transduction cascades in endothelial cells. J. Immunol. 169 (2002) 2102-2110
    • (2002) J. Immunol. , vol.169 , pp. 2102-2110
    • Schraufstatter, I.U.1    Trieu, K.2    Sikora, L.3    Sriramarao, P.4    DiScipio, R.5
  • 89
    • 4344686677 scopus 로고    scopus 로고
    • Expression of a functional C5a receptor in regenerating hepatocytes and its involvement in a proliferative signaling pathway in rat
    • Daveau M., Benard M., Scotte M., Schouft M.T., Hiron M., Francois A., Salier J.P., and Fontaine M. Expression of a functional C5a receptor in regenerating hepatocytes and its involvement in a proliferative signaling pathway in rat. J. Immunol. 173 (2004) 3418-3424
    • (2004) J. Immunol. , vol.173 , pp. 3418-3424
    • Daveau, M.1    Benard, M.2    Scotte, M.3    Schouft, M.T.4    Hiron, M.5    Francois, A.6    Salier, J.P.7    Fontaine, M.8
  • 92
    • 0029099616 scopus 로고
    • Chemoattractant signaling and leukocyte activation
    • Bokoch G.M. Chemoattractant signaling and leukocyte activation. Blood 86 (1995) 1649-1660
    • (1995) Blood , vol.86 , pp. 1649-1660
    • Bokoch, G.M.1
  • 93
    • 0024854386 scopus 로고
    • Two distinct Gi-proteins mediate formyl peptide receptor signal transduction in human leukemia (HL-60) cells
    • Gierschik P., Sidoropoulos D., and Jakobs K.H. Two distinct Gi-proteins mediate formyl peptide receptor signal transduction in human leukemia (HL-60) cells. J. Biol. Chem. 264 (1989) 21470-21473
    • (1989) J. Biol. Chem. , vol.264 , pp. 21470-21473
    • Gierschik, P.1    Sidoropoulos, D.2    Jakobs, K.H.3
  • 94
    • 0029077579 scopus 로고
    • Differential coupling of the formyl peptide receptor to adenylate cyclase and phospholipase C by the pertussis toxin-insensitive Gz protein
    • Tsu R.C., Lai H.W., Allen R.A., and Wong Y.H. Differential coupling of the formyl peptide receptor to adenylate cyclase and phospholipase C by the pertussis toxin-insensitive Gz protein. Biochem. J. 309 (1995) 331-339
    • (1995) Biochem. J. , vol.309 , pp. 331-339
    • Tsu, R.C.1    Lai, H.W.2    Allen, R.A.3    Wong, Y.H.4
  • 95
    • 0027310748 scopus 로고
    • Specific interactions of chemoattractant factor receptors with G-proteins
    • Amatruda T.D., Gerard N.P., Gerard C., and Simon M.I. Specific interactions of chemoattractant factor receptors with G-proteins. J. Biol. Chem. 268 (1993) 10139-10144
    • (1993) J. Biol. Chem. , vol.268 , pp. 10139-10144
    • Amatruda, T.D.1    Gerard, N.P.2    Gerard, C.3    Simon, M.I.4
  • 96
    • 0028988979 scopus 로고
    • Extensive contact between Gi2 and N-formyl peptide receptor of human neutrophils: mapping of binding sites using receptor-mimetic peptides
    • Bommakanti R.K., Dratz E.A., Siemsen D.W., and Jesaitis A.J. Extensive contact between Gi2 and N-formyl peptide receptor of human neutrophils: mapping of binding sites using receptor-mimetic peptides. Biochemistry 34 (1995) 6720-6728
    • (1995) Biochemistry , vol.34 , pp. 6720-6728
    • Bommakanti, R.K.1    Dratz, E.A.2    Siemsen, D.W.3    Jesaitis, A.J.4
  • 97
    • 0027248974 scopus 로고
    • The role of the third intracellular loop of the neutrophil N-formyl peptide receptor in G protein coupling
    • Prossnitz E.R., Quehenberger O., Cochrane C.G., and Ye R.D. The role of the third intracellular loop of the neutrophil N-formyl peptide receptor in G protein coupling. Biochem. J. 294 (1993) 581-587
    • (1993) Biochem. J. , vol.294 , pp. 581-587
    • Prossnitz, E.R.1    Quehenberger, O.2    Cochrane, C.G.3    Ye, R.D.4
  • 98
    • 0028916589 scopus 로고
    • Binding of low affinity N-formyl peptide receptors to G protein. Characterization of a novel inactive receptor intermediate
    • Prossnitz E.R., Schreiber R.E., Bokoch G.M., and Ye R.D. Binding of low affinity N-formyl peptide receptors to G protein. Characterization of a novel inactive receptor intermediate. J. Biol. Chem. 270 (1995) 10686-10694
    • (1995) J. Biol. Chem. , vol.270 , pp. 10686-10694
    • Prossnitz, E.R.1    Schreiber, R.E.2    Bokoch, G.M.3    Ye, R.D.4
  • 99
    • 0028013155 scopus 로고
    • Domains of the human neutrophil N-formyl peptide receptor involved in G protein coupling
    • Schreiber R.E., Prossnitz E.R., Ye R.D., Cochrane C.G., and Bokoch G.M. Domains of the human neutrophil N-formyl peptide receptor involved in G protein coupling. J. Biol. Chem. 269 (1994) 326-331
    • (1994) J. Biol. Chem. , vol.269 , pp. 326-331
    • Schreiber, R.E.1    Prossnitz, E.R.2    Ye, R.D.3    Cochrane, C.G.4    Bokoch, G.M.5
  • 100
    • 34047246323 scopus 로고    scopus 로고
    • A comprehensive structure-function map of the intracellular surface of the human C5a receptor: I. Identification of critical residues
    • Matsumoto M.L., Narzinski K., Kiser P.D., Nikiforovich G.V., and Baranski T.J. A comprehensive structure-function map of the intracellular surface of the human C5a receptor: I. Identification of critical residues. J. Biol. Chem. 282 (2007) 3105-3121
    • (2007) J. Biol. Chem. , vol.282 , pp. 3105-3121
    • Matsumoto, M.L.1    Narzinski, K.2    Kiser, P.D.3    Nikiforovich, G.V.4    Baranski, T.J.5
  • 101
    • 34047274266 scopus 로고    scopus 로고
    • A comprehensive structure-function map of the intracellular surface of the human C5a receptor: II. Elucidation of g protein specificity determinants
    • Matsumoto M.L., Narzinski K., Nikiforovich G.V., and Baranski T.J. A comprehensive structure-function map of the intracellular surface of the human C5a receptor: II. Elucidation of g protein specificity determinants. J. Biol. Chem. 282 (2007) 3122-3133
    • (2007) J. Biol. Chem. , vol.282 , pp. 3122-3133
    • Matsumoto, M.L.1    Narzinski, K.2    Nikiforovich, G.V.3    Baranski, T.J.4
  • 102
    • 0026676806 scopus 로고
    • Isozyme-selective stimulation of phospholipase C-b2 by G protein bg-subunits
    • Camps M., Carozzi A., Schnabel P., Scheer A., Parker P.J., and Gierschik P. Isozyme-selective stimulation of phospholipase C-b2 by G protein bg-subunits. Nature 360 (1992) 684-689
    • (1992) Nature , vol.360 , pp. 684-689
    • Camps, M.1    Carozzi, A.2    Schnabel, P.3    Scheer, A.4    Parker, P.J.5    Gierschik, P.6
  • 104
    • 0037133606 scopus 로고    scopus 로고
    • Neutrophils lacking phosphoinositide 3-kinase gamma show loss of directionality during N-formyl-Met-Leu-Phe-induced chemotaxis
    • Hannigan M., Zhan L., Li Z., Ai Y., Wu D., and Huang C.K. Neutrophils lacking phosphoinositide 3-kinase gamma show loss of directionality during N-formyl-Met-Leu-Phe-induced chemotaxis. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 3603-3608
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3603-3608
    • Hannigan, M.1    Zhan, L.2    Li, Z.3    Ai, Y.4    Wu, D.5    Huang, C.K.6
  • 107
    • 0032534597 scopus 로고    scopus 로고
    • Isolation and characterization of a variant HL60 cell line defective in the activation of the NADPH oxidase by phorbol myristate acetate
    • Tardif M., Rabiet M.-J., Christophe T., Milcent D., and Boulay F. Isolation and characterization of a variant HL60 cell line defective in the activation of the NADPH oxidase by phorbol myristate acetate. J. Immunol. 161 (1998) 6885-6895
    • (1998) J. Immunol. , vol.161 , pp. 6885-6895
    • Tardif, M.1    Rabiet, M.-J.2    Christophe, T.3    Milcent, D.4    Boulay, F.5
  • 108
    • 0031578232 scopus 로고    scopus 로고
    • Translocation of protein kinase C isoforms in rat neutrophils
    • Tsao L.-T., and Wang J.-P. Translocation of protein kinase C isoforms in rat neutrophils. Biochem. Biophys. Res. Commun. 234 (1997) 412-418
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 412-418
    • Tsao, L.-T.1    Wang, J.-P.2
  • 109
    • 0037129803 scopus 로고    scopus 로고
    • Phosphorylation of p47phox sites by PKC alpha, beta II, delta, and zeta: effect on binding to p22phox and on NADPH oxidase activation
    • Fontayne A., Dang P.M., Gougerot-Pocidalo M.A., and El-Benna J. Phosphorylation of p47phox sites by PKC alpha, beta II, delta, and zeta: effect on binding to p22phox and on NADPH oxidase activation. Biochemistry 41 (2002) 7743-7750
    • (2002) Biochemistry , vol.41 , pp. 7743-7750
    • Fontayne, A.1    Dang, P.M.2    Gougerot-Pocidalo, M.A.3    El-Benna, J.4
  • 111
    • 17044431078 scopus 로고    scopus 로고
    • Activation-induced depletion of protein kinase C alpha provokes desensitization of monocytes/macrophages in sepsis
    • von Knethen A., Tautenhahn A., Link H., Lindemann D., and Brune B. Activation-induced depletion of protein kinase C alpha provokes desensitization of monocytes/macrophages in sepsis. J. Immunol. 174 (2005) 4960-4965
    • (2005) J. Immunol. , vol.174 , pp. 4960-4965
    • von Knethen, A.1    Tautenhahn, A.2    Link, H.3    Lindemann, D.4    Brune, B.5
  • 112
    • 10344246590 scopus 로고    scopus 로고
    • Reconstitution of chemotactic peptide-induced nicotinamide adenine dinucleotide phosphate (reduced) oxidase activation in transgenic COS-phox cells
    • He R., Nanamori M., Sang H., Yin H., Dinauer M.C., and Ye R.D. Reconstitution of chemotactic peptide-induced nicotinamide adenine dinucleotide phosphate (reduced) oxidase activation in transgenic COS-phox cells. J. Immunol. 173 (2004) 7462-7470
    • (2004) J. Immunol. , vol.173 , pp. 7462-7470
    • He, R.1    Nanamori, M.2    Sang, H.3    Yin, H.4    Dinauer, M.C.5    Ye, R.D.6
  • 113
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase g
    • Lopez-Ilasaca M., Crespo P., Pellici P.G., Gutkind J.S., and Wetzker R. Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase g. Science 275 (1997) 394-397
    • (1997) Science , vol.275 , pp. 394-397
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.G.3    Gutkind, J.S.4    Wetzker, R.5
  • 114
    • 0031573210 scopus 로고    scopus 로고
    • Formyl peptide receptor are coupled to multiple mitogen-activated protein kinase cascades by distinct signal transduction pathways
    • Rane M.J., Carrithers S.L., Arthur J.M., Klein J.B., and McLeish K.R. Formyl peptide receptor are coupled to multiple mitogen-activated protein kinase cascades by distinct signal transduction pathways. J. Immunol. 159 (1997) 5070-5078
    • (1997) J. Immunol. , vol.159 , pp. 5070-5078
    • Rane, M.J.1    Carrithers, S.L.2    Arthur, J.M.3    Klein, J.B.4    McLeish, K.R.5
  • 115
    • 0027238929 scopus 로고
    • Stimulation of human neutrophils with formyl-methionyl-leucyl-phenylalanine induces tyrosine phosphorylation and activation of distinct mitogen-activated protein-kinases
    • Torres M., Hall F.L., and O'Neill K. Stimulation of human neutrophils with formyl-methionyl-leucyl-phenylalanine induces tyrosine phosphorylation and activation of distinct mitogen-activated protein-kinases. J. Immunol. 150 (1993) 1563-1578
    • (1993) J. Immunol. , vol.150 , pp. 1563-1578
    • Torres, M.1    Hall, F.L.2    O'Neill, K.3
  • 116
    • 0034268796 scopus 로고    scopus 로고
    • Src tyrosine kinase is a novel direct effector of G proteins
    • Ma Y.C., Huang J., Ali S., Lowry W., and Huang X.Y. Src tyrosine kinase is a novel direct effector of G proteins. Cell 102 (2000) 635-646
    • (2000) Cell , vol.102 , pp. 635-646
    • Ma, Y.C.1    Huang, J.2    Ali, S.3    Lowry, W.4    Huang, X.Y.5
  • 120
    • 0141889083 scopus 로고    scopus 로고
    • The hemopoietic Rho/Rac guanine nucleotide exchange factor Vav1 regulates N-formyl-methionyl-leucyl-phenylalanine-activated neutrophil functions
    • Kim C., Marchal C.C., Penninger J., and Dinauer M.C. The hemopoietic Rho/Rac guanine nucleotide exchange factor Vav1 regulates N-formyl-methionyl-leucyl-phenylalanine-activated neutrophil functions. J. Immunol. 171 (2003) 4425-4430
    • (2003) J. Immunol. , vol.171 , pp. 4425-4430
    • Kim, C.1    Marchal, C.C.2    Penninger, J.3    Dinauer, M.C.4
  • 122
    • 0242683360 scopus 로고    scopus 로고
    • Leukocyte polarization in cell migration and immune interactions
    • Sanchez-Madrid F., and del Pozo M.A. Leukocyte polarization in cell migration and immune interactions. EMBO J. 18 (1999) 501-511
    • (1999) EMBO J. , vol.18 , pp. 501-511
    • Sanchez-Madrid, F.1    del Pozo, M.A.2
  • 123
    • 0037215397 scopus 로고    scopus 로고
    • Regulation of neutrophil function by Rac GTPases
    • Dinauer M.C. Regulation of neutrophil function by Rac GTPases. Curr. Opin. Hematol. 10 (2003) 8-15
    • (2003) Curr. Opin. Hematol. , vol.10 , pp. 8-15
    • Dinauer, M.C.1
  • 124
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M., Derry J.M., Karlak B., Jiang S., Lemahieu V., McCormick F., Francke U., and Abo A. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84 (1996) 723-734
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 125
    • 0033040628 scopus 로고    scopus 로고
    • The Arp2/3 complex: a multifunctional actin organizer
    • Machesky L.M., and Gould K.L. The Arp2/3 complex: a multifunctional actin organizer. Curr. Opin. Cell Biol. 11 (1999) 117-121
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 117-121
    • Machesky, L.M.1    Gould, K.L.2
  • 126
    • 0038000556 scopus 로고    scopus 로고
    • Direct binding of a fragment of the Wiskott-Aldrich syndrome protein to the C-terminal end of the anaphylatoxin C5a receptor
    • Tardif M., Brouchon L., Rabiet M.J., and Boulay F. Direct binding of a fragment of the Wiskott-Aldrich syndrome protein to the C-terminal end of the anaphylatoxin C5a receptor. Biochem. J. 372 (2003) 453-463
    • (2003) Biochem. J. , vol.372 , pp. 453-463
    • Tardif, M.1    Brouchon, L.2    Rabiet, M.J.3    Boulay, F.4
  • 127
    • 23844500010 scopus 로고    scopus 로고
    • The immunostimulatory peptide WKYMVm-NH activates bone marrow mouse neutrophils via multiple signal transduction pathways
    • Boxio R., Bossenmeyer-Pourie C., Vanderesse R., Dournon C., and Nusse O. The immunostimulatory peptide WKYMVm-NH activates bone marrow mouse neutrophils via multiple signal transduction pathways. Scand. J. Immunol. 62 (2005) 140-147
    • (2005) Scand. J. Immunol. , vol.62 , pp. 140-147
    • Boxio, R.1    Bossenmeyer-Pourie, C.2    Vanderesse, R.3    Dournon, C.4    Nusse, O.5
  • 131
    • 0035033022 scopus 로고    scopus 로고
    • Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers
    • Lee H.C. Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers. Annu. Rev. Pharmacol. Toxicol. 41 (2001) 317-345
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 317-345
    • Lee, H.C.1
  • 132
    • 33646039372 scopus 로고    scopus 로고
    • The peptide Trp-Lys-Tyr-Met-Val-d-Met activates neutrophils through the formyl peptide receptor only when signaling through the formylpeptide receptor like 1 is blocked. A receptor switch with implications for signal transduction studies with inhibitors and receptor antagonists
    • Karlsson J., Fu H., Boulay F., Bylund J., and Dahlgren C. The peptide Trp-Lys-Tyr-Met-Val-d-Met activates neutrophils through the formyl peptide receptor only when signaling through the formylpeptide receptor like 1 is blocked. A receptor switch with implications for signal transduction studies with inhibitors and receptor antagonists. Biochem. Pharmacol. 71 (2006) 1488-1496
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 1488-1496
    • Karlsson, J.1    Fu, H.2    Boulay, F.3    Bylund, J.4    Dahlgren, C.5
  • 134
    • 33748042937 scopus 로고    scopus 로고
    • Differential production of leukotriene B4 or prostaglandin E2 by WKYMVm or serum amyloid A via formyl peptide receptor-like 1
    • Lee H.Y., Jo S.H., Lee C., Baek S.H., and Bae Y.S. Differential production of leukotriene B4 or prostaglandin E2 by WKYMVm or serum amyloid A via formyl peptide receptor-like 1. Biochem. Pharmacol. 72 (2006) 860-868
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 860-868
    • Lee, H.Y.1    Jo, S.H.2    Lee, C.3    Baek, S.H.4    Bae, Y.S.5
  • 136
    • 0035860802 scopus 로고    scopus 로고
    • The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states
    • Palanche T., Ilien B., Zoffmann S., Reck M.P., Bucher B., Edelstein S.J., and Galzi J.L. The neurokinin A receptor activates calcium and cAMP responses through distinct conformational states. J. Biol. Chem. 276 (2001) 34853-34861
    • (2001) J. Biol. Chem. , vol.276 , pp. 34853-34861
    • Palanche, T.1    Ilien, B.2    Zoffmann, S.3    Reck, M.P.4    Bucher, B.5    Edelstein, S.J.6    Galzi, J.L.7
  • 137
    • 0036463901 scopus 로고    scopus 로고
    • Efficacy at G-protein-coupled receptors
    • Kenakin T. Efficacy at G-protein-coupled receptors. Nat. Rev. Drug Discov. 1 (2002) 103-110
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 103-110
    • Kenakin, T.1
  • 138
    • 0036177114 scopus 로고    scopus 로고
    • Drug efficacy at G protein-coupled receptors
    • Kenakin T. Drug efficacy at G protein-coupled receptors. Annu. Rev. Pharmacol. Toxicol. 42 (2002) 349-379
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 349-379
    • Kenakin, T.1
  • 141
    • 0031862620 scopus 로고    scopus 로고
    • Complement C5a anaphylatoxin fragment causes apoptosis in TGW neuroblastoma cells
    • Farkas I., Baranyi L., Liposits Z.S., Yamamoto T., and Okada H. Complement C5a anaphylatoxin fragment causes apoptosis in TGW neuroblastoma cells. Neuroscience 86 (1998) 903-911
    • (1998) Neuroscience , vol.86 , pp. 903-911
    • Farkas, I.1    Baranyi, L.2    Liposits, Z.S.3    Yamamoto, T.4    Okada, H.5
  • 143
    • 0034717942 scopus 로고    scopus 로고
    • The role of complement anaphylatoxin C5a in neurodegeneration: implications in Alzheimer's disease
    • Mukherjee P., and Pasinetti G.M. The role of complement anaphylatoxin C5a in neurodegeneration: implications in Alzheimer's disease. J. Neuroimmunol. 105 (2000) 124-130
    • (2000) J. Neuroimmunol. , vol.105 , pp. 124-130
    • Mukherjee, P.1    Pasinetti, G.M.2
  • 144
    • 0035076597 scopus 로고    scopus 로고
    • Complement anaphylatoxin C5a neuroprotects through mitogen-activated protein kinase-dependent inhibition of caspase 3
    • Mukherjee P., and Pasinetti G.M. Complement anaphylatoxin C5a neuroprotects through mitogen-activated protein kinase-dependent inhibition of caspase 3. J. Neurochem. 77 (2001) 43-49
    • (2001) J. Neurochem. , vol.77 , pp. 43-49
    • Mukherjee, P.1    Pasinetti, G.M.2
  • 145
    • 0242572132 scopus 로고    scopus 로고
    • Dimerization of G-protein-coupled receptors: roles in signal transduction
    • Bai M. Dimerization of G-protein-coupled receptors: roles in signal transduction. Cell. Signal. 16 (2004) 175-186
    • (2004) Cell. Signal. , vol.16 , pp. 175-186
    • Bai, M.1
  • 146
    • 10844255797 scopus 로고    scopus 로고
    • Oligomerization of G protein-coupled receptors: past, present, and future
    • Park P.S., Filipek S., Wells J.W., and Palczewski K. Oligomerization of G protein-coupled receptors: past, present, and future. Biochemistry 43 (2004) 15643-15656
    • (2004) Biochemistry , vol.43 , pp. 15643-15656
    • Park, P.S.1    Filipek, S.2    Wells, J.W.3    Palczewski, K.4
  • 147
    • 0242289624 scopus 로고    scopus 로고
    • Homo- and hetero-oligomerization of G protein-coupled receptors
    • Lee S.P., O'Dowd B.F., and George S.R. Homo- and hetero-oligomerization of G protein-coupled receptors. Life Sci. 74 (2003) 173-180
    • (2003) Life Sci. , vol.74 , pp. 173-180
    • Lee, S.P.1    O'Dowd, B.F.2    George, S.R.3
  • 148
    • 0036174608 scopus 로고    scopus 로고
    • Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function
    • Angers S., Salahpour A., and Bouvier M. Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function. Annu. Rev. Pharmacol. Toxicol. 42 (2002) 409-435
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 409-435
    • Angers, S.1    Salahpour, A.2    Bouvier, M.3
  • 149
    • 0041315583 scopus 로고    scopus 로고
    • C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G protein-coupled receptor expressed in yeast
    • Floyd D.H., Geva A., Bruinsma S.P., Overton M.C., Blumer K.J., and Baranski T.J. C5a receptor oligomerization. II. Fluorescence resonance energy transfer studies of a human G protein-coupled receptor expressed in yeast. J. Biol. Chem. 278 (2003) 35354-35361
    • (2003) J. Biol. Chem. , vol.278 , pp. 35354-35361
    • Floyd, D.H.1    Geva, A.2    Bruinsma, S.P.3    Overton, M.C.4    Blumer, K.J.5    Baranski, T.J.6
  • 150
    • 0041331661 scopus 로고    scopus 로고
    • Experimental evidence for lack of homodimerization of the G protein-coupled human N-formyl peptide receptor
    • Gripentrog J.M., Kantele K.P., Jesaitis A.J., and Miettinen H.M. Experimental evidence for lack of homodimerization of the G protein-coupled human N-formyl peptide receptor. J. Immunol. 171 (2003) 3187-3193
    • (2003) J. Immunol. , vol.171 , pp. 3187-3193
    • Gripentrog, J.M.1    Kantele, K.P.2    Jesaitis, A.J.3    Miettinen, H.M.4
  • 151
    • 0035032316 scopus 로고    scopus 로고
    • Oligomerisation of G-protein-coupled receptors
    • Milligan G. Oligomerisation of G-protein-coupled receptors. J. Cell Sci. 114 (2001) 1265-1271
    • (2001) J. Cell Sci. , vol.114 , pp. 1265-1271
    • Milligan, G.1
  • 152
    • 27144548417 scopus 로고    scopus 로고
    • Dimerization of chemokine receptors and its functional consequences
    • Springael J.Y., Urizar E., and Parmentier M. Dimerization of chemokine receptors and its functional consequences. Cytokine Growth Factor Rev. 16 (2005) 611-623
    • (2005) Cytokine Growth Factor Rev. , vol.16 , pp. 611-623
    • Springael, J.Y.1    Urizar, E.2    Parmentier, M.3
  • 153
    • 0041315589 scopus 로고    scopus 로고
    • C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor
    • Klco J.M., Lassere T.B., and Baranski T.J. C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor. J. Biol. Chem. 278 (2003) 35345-35353
    • (2003) J. Biol. Chem. , vol.278 , pp. 35345-35353
    • Klco, J.M.1    Lassere, T.B.2    Baranski, T.J.3
  • 154
    • 0034634690 scopus 로고    scopus 로고
    • Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function
    • Geva A., Lassere T.B., Lichtarge O., Pollitt S.K., and Baranski T.J. Genetic mapping of the human C5a receptor. Identification of transmembrane amino acids critical for receptor function. J. Biol. Chem. 275 (2000) 35393-35401
    • (2000) J. Biol. Chem. , vol.275 , pp. 35393-35401
    • Geva, A.1    Lassere, T.B.2    Lichtarge, O.3    Pollitt, S.K.4    Baranski, T.J.5
  • 157
    • 27844541754 scopus 로고    scopus 로고
    • G protein-coupled receptor kinases promote phosphorylation and beta-arrestin-mediated internalization of CCR5 homo- and hetero-oligomers
    • Huttenrauch F., Pollok-Kopp B., and Oppermann M. G protein-coupled receptor kinases promote phosphorylation and beta-arrestin-mediated internalization of CCR5 homo- and hetero-oligomers. J. Biol. Chem. 280 (2005) 37503-37515
    • (2005) J. Biol. Chem. , vol.280 , pp. 37503-37515
    • Huttenrauch, F.1    Pollok-Kopp, B.2    Oppermann, M.3
  • 159
    • 0035874534 scopus 로고    scopus 로고
    • The synthetic peptide WKYMVm attenuates the function of the chemokine receptors CCR5 and CXCR4 through activation of formyl peptide receptor-like 1
    • Li B.Q., Wetzel M.A., Mikovits J.A., Henderson E.E., Rogers T.J., Gong W., Le Y., Ruscetti F.W., and Wang J.M. The synthetic peptide WKYMVm attenuates the function of the chemokine receptors CCR5 and CXCR4 through activation of formyl peptide receptor-like 1. Blood 97 (2001) 2941-2947
    • (2001) Blood , vol.97 , pp. 2941-2947
    • Li, B.Q.1    Wetzel, M.A.2    Mikovits, J.A.3    Henderson, E.E.4    Rogers, T.J.5    Gong, W.6    Le, Y.7    Ruscetti, F.W.8    Wang, J.M.9
  • 161
    • 0032911044 scopus 로고    scopus 로고
    • Dynamics of a chemoattractant receptor in living neutrophils during chemotaxis
    • Servant G., Weiner O.D., Neptune E.R., Sedat J.W., and Bourne H.R. Dynamics of a chemoattractant receptor in living neutrophils during chemotaxis. Mol. Biol. Cell 10 (1999) 1163-1178
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1163-1178
    • Servant, G.1    Weiner, O.D.2    Neptune, E.R.3    Sedat, J.W.4    Bourne, H.R.5
  • 162
    • 7244257487 scopus 로고    scopus 로고
    • N-formyl peptide receptors cluster in an active Raft-associated state prior to phosphorylation
    • Xue M., Vines C.M., Buranda T., Cimino D.F., Bennett T.A., and Prossnitz E.R. N-formyl peptide receptors cluster in an active Raft-associated state prior to phosphorylation. J. Biol. Chem. 279 (2004) 45175-45184
    • (2004) J. Biol. Chem. , vol.279 , pp. 45175-45184
    • Xue, M.1    Vines, C.M.2    Buranda, T.3    Cimino, D.F.4    Bennett, T.A.5    Prossnitz, E.R.6
  • 163
    • 0035966001 scopus 로고    scopus 로고
    • Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding
    • Bennett T.A., Foutz T.D., Gurevich V.V., Sklar L.A., and Prossnitz E.R. Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding. J. Biol. Chem. 276 (2001) 49195-49203
    • (2001) J. Biol. Chem. , vol.276 , pp. 49195-49203
    • Bennett, T.A.1    Foutz, T.D.2    Gurevich, V.V.3    Sklar, L.A.4    Prossnitz, E.R.5
  • 164
    • 0027722215 scopus 로고
    • Cytoskeletal regulation of chemotactic receptors: molecular complexation of N-formyl peptide receptors with G proteins and actin
    • Jesaitis A.J., and Klotz K.N. Cytoskeletal regulation of chemotactic receptors: molecular complexation of N-formyl peptide receptors with G proteins and actin. Eur. J. Haematol. 51 (1993) 288-293
    • (1993) Eur. J. Haematol. , vol.51 , pp. 288-293
    • Jesaitis, A.J.1    Klotz, K.N.2
  • 165
    • 20244365891 scopus 로고    scopus 로고
    • Reactivation of formyl peptide receptors triggers the neutrophil NADPH-oxidase but not a transient rise in intracellular calcium
    • Bylund J., Bjorstad A., Granfeldt D., Karlsson A., Woschnagg C., and Dahlgren C. Reactivation of formyl peptide receptors triggers the neutrophil NADPH-oxidase but not a transient rise in intracellular calcium. J. Biol. Chem. 278 (2003) 30578-30586
    • (2003) J. Biol. Chem. , vol.278 , pp. 30578-30586
    • Bylund, J.1    Bjorstad, A.2    Granfeldt, D.3    Karlsson, A.4    Woschnagg, C.5    Dahlgren, C.6
  • 166
    • 0027231533 scopus 로고
    • Agonist-dependent phosphorylation of N-formylpeptide and activation peptide from the fifth component of C (C5a) chemoattractant receptors in differentiated HL60 cells
    • Tardif M., Mery L., Brouchon L., and Boulay F. Agonist-dependent phosphorylation of N-formylpeptide and activation peptide from the fifth component of C (C5a) chemoattractant receptors in differentiated HL60 cells. J. Immunol. 150 (1993) 3534-3545
    • (1993) J. Immunol. , vol.150 , pp. 3534-3545
    • Tardif, M.1    Mery, L.2    Brouchon, L.3    Boulay, F.4
  • 167
    • 0027368179 scopus 로고
    • Differences in phosphorylation of formylpeptide and C5a chemoattractant receptors correlate with differences in desensitization
    • Ali H., Richardson R.M., Tomhave E.D., Didsbury J.R., and Snyderman R. Differences in phosphorylation of formylpeptide and C5a chemoattractant receptors correlate with differences in desensitization. J. Biol. Chem. 268 (1993) 24247-24254
    • (1993) J. Biol. Chem. , vol.268 , pp. 24247-24254
    • Ali, H.1    Richardson, R.M.2    Tomhave, E.D.3    Didsbury, J.R.4    Snyderman, R.5
  • 168
    • 14844356200 scopus 로고
    • Phosphorylation, dephosphorylation, and recycling of the C5a receptor in differentiated HL60 cells
    • Giannini E., and Boulay F. Phosphorylation, dephosphorylation, and recycling of the C5a receptor in differentiated HL60 cells. J. Immunol. 154 (1995) 4055-4064
    • (1995) J. Immunol. , vol.154 , pp. 4055-4064
    • Giannini, E.1    Boulay, F.2
  • 169
    • 0029021188 scopus 로고
    • Identification of the major phosphorylation sites in human C5a anaphylatoxin receptor in vivo
    • Giannini E., Brouchon L., and Boulay F. Identification of the major phosphorylation sites in human C5a anaphylatoxin receptor in vivo. J. Biol. Chem. 270 (1995) 19166-19172
    • (1995) J. Biol. Chem. , vol.270 , pp. 19166-19172
    • Giannini, E.1    Brouchon, L.2    Boulay, F.3
  • 170
    • 0033381145 scopus 로고    scopus 로고
    • Ligand-induced phosphorylation of anaphylatoxin receptors C3aR and C5aR is mediated by G protein-coupled receptor kinases
    • Langkabel P., Zwirner J., and Oppermann M. Ligand-induced phosphorylation of anaphylatoxin receptors C3aR and C5aR is mediated by G protein-coupled receptor kinases. Eur. J. Immunol. 29 (1999) 3035-3046
    • (1999) Eur. J. Immunol. , vol.29 , pp. 3035-3046
    • Langkabel, P.1    Zwirner, J.2    Oppermann, M.3
  • 171
    • 0033609360 scopus 로고    scopus 로고
    • Overexpression of wild-type and catalytically inactive forms of GRK2 and GRK6 fails to alter the agonist-induced phosphorylation of the C5a receptor (CD88): evidence that GRK6 is autophosphorylated in COS-7 cells
    • Milcent M.D., Christophe T., Rabiet M.-J., Tardif M., and Boulay F. Overexpression of wild-type and catalytically inactive forms of GRK2 and GRK6 fails to alter the agonist-induced phosphorylation of the C5a receptor (CD88): evidence that GRK6 is autophosphorylated in COS-7 cells. Biochem. Biophys. Res. Commun. 259 (1999) 224-229
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 224-229
    • Milcent, M.D.1    Christophe, T.2    Rabiet, M.-J.3    Tardif, M.4    Boulay, F.5
  • 172
    • 0034695490 scopus 로고    scopus 로고
    • Human complement 5a (C5a) anaphylatoxin receptor (CD88) phosphorylation sites and their specific role in receptor phosphorylation and attenuation of G protein-mediated responses
    • Christophe T., Rabiet M.-J., Tardif M., Milcent M.-D., and Boulay F. Human complement 5a (C5a) anaphylatoxin receptor (CD88) phosphorylation sites and their specific role in receptor phosphorylation and attenuation of G protein-mediated responses. J. Biol. Chem. 275 (2000) 1656-1664
    • (2000) J. Biol. Chem. , vol.275 , pp. 1656-1664
    • Christophe, T.1    Rabiet, M.-J.2    Tardif, M.3    Milcent, M.-D.4    Boulay, F.5
  • 173
    • 0000693801 scopus 로고    scopus 로고
    • Internalization and recycling of the C5a anaphylatoxin receptor: evidence that the agonist-mediated internalization is modulated by phosphorylation of the C-terminal domain
    • Naik N., Giannini E., Brouchon L., and Boulay F. Internalization and recycling of the C5a anaphylatoxin receptor: evidence that the agonist-mediated internalization is modulated by phosphorylation of the C-terminal domain. J. Cell Sci. 110 (1997) 2381-2390
    • (1997) J. Cell Sci. , vol.110 , pp. 2381-2390
    • Naik, N.1    Giannini, E.2    Brouchon, L.3    Boulay, F.4
  • 174
    • 0037423283 scopus 로고    scopus 로고
    • Phosphorylation of key serine residues is required for internalization of the complement 5a (C5a) anaphylatoxin receptor via a beta-arrestin, dynamin, and clathrin-dependent pathway
    • Braun L., Christophe T., and Boulay F. Phosphorylation of key serine residues is required for internalization of the complement 5a (C5a) anaphylatoxin receptor via a beta-arrestin, dynamin, and clathrin-dependent pathway. J. Biol. Chem. 278 (2003) 4277-4285
    • (2003) J. Biol. Chem. , vol.278 , pp. 4277-4285
    • Braun, L.1    Christophe, T.2    Boulay, F.3
  • 175
    • 0028809192 scopus 로고
    • Phosphorylation of the N-formyl peptide receptor carboxyl terminus by the G protein-coupled receptor kinase, GRK2
    • Prossnitz E.R., Kim C.M., Benovic J.L., and Ye R.D. Phosphorylation of the N-formyl peptide receptor carboxyl terminus by the G protein-coupled receptor kinase, GRK2. J. Biol. Chem. 270 (1995) 1130-1137
    • (1995) J. Biol. Chem. , vol.270 , pp. 1130-1137
    • Prossnitz, E.R.1    Kim, C.M.2    Benovic, J.L.3    Ye, R.D.4
  • 176
    • 0033569754 scopus 로고    scopus 로고
    • Differential phosphorylation paradigms dictate desensitization and internalization of the N-formyl peptide receptor
    • Maestes D.C., Potter R.M., and Prossnitz E.R. Differential phosphorylation paradigms dictate desensitization and internalization of the N-formyl peptide receptor. J. Biol. Chem. 274 (1999) 29791-29795
    • (1999) J. Biol. Chem. , vol.274 , pp. 29791-29795
    • Maestes, D.C.1    Potter, R.M.2    Prossnitz, E.R.3
  • 177
    • 0025742855 scopus 로고
    • Role of acidic amino acids in peptide substrates of the b-adrenergic receptor kinase and rhodopsin kinase
    • Onorato J.J., Palczewski K., Regan J.W., Caron M.G., Lefkowitz R.J., and Benovic J.L. Role of acidic amino acids in peptide substrates of the b-adrenergic receptor kinase and rhodopsin kinase. Biochemistry 30 (1991) 5118-5125
    • (1991) Biochemistry , vol.30 , pp. 5118-5125
    • Onorato, J.J.1    Palczewski, K.2    Regan, J.W.3    Caron, M.G.4    Lefkowitz, R.J.5    Benovic, J.L.6
  • 178
    • 33645970198 scopus 로고    scopus 로고
    • Regulation of N-formyl peptide receptor signaling and trafficking by individual carboxyl-terminal serine and threonine residues
    • Potter R.M., Maestas D.C., Cimino D.F., and Prossnitz E.R. Regulation of N-formyl peptide receptor signaling and trafficking by individual carboxyl-terminal serine and threonine residues. J. Immunol. 176 (2006) 5418-5425
    • (2006) J. Immunol. , vol.176 , pp. 5418-5425
    • Potter, R.M.1    Maestas, D.C.2    Cimino, D.F.3    Prossnitz, E.R.4
  • 179
    • 0037423307 scopus 로고    scopus 로고
    • N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity
    • Key T.A., Foutz T.D., Gurevich V.V., Sklar L.A., and Prossnitz E.R. N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity. J. Biol. Chem. 278 (2003) 4041-4047
    • (2003) J. Biol. Chem. , vol.278 , pp. 4041-4047
    • Key, T.A.1    Foutz, T.D.2    Gurevich, V.V.3    Sklar, L.A.4    Prossnitz, E.R.5
  • 180
    • 12744260243 scopus 로고    scopus 로고
    • Inhibition of chemoattractant N-formyl peptide receptor trafficking by active arrestins
    • Key T.A., Vines C.M., Wagener B.M., Gurevich V., Sklar L.A., and Prossnitz E. Inhibition of chemoattractant N-formyl peptide receptor trafficking by active arrestins. Traffic 6 (2005) 1-13
    • (2005) Traffic , vol.6 , pp. 1-13
    • Key, T.A.1    Vines, C.M.2    Wagener, B.M.3    Gurevich, V.4    Sklar, L.A.5    Prossnitz, E.6
  • 181
    • 0034802172 scopus 로고    scopus 로고
    • Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane translocation
    • Han M., Gurevich V.V., Vishnivetskiy S.A., Sigler P.B., and Schubert C. Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane translocation. Structure (Camb.) 9 (2001) 869-880
    • (2001) Structure (Camb.) , vol.9 , pp. 869-880
    • Han, M.1    Gurevich, V.V.2    Vishnivetskiy, S.A.3    Sigler, P.B.4    Schubert, C.5
  • 182
    • 0037066145 scopus 로고    scopus 로고
    • Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis
    • Milano S.K., Pace H.C., Kim Y.M., Brenner C., and Benovic J.L. Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis. Biochemistry 41 (2002) 3321-3328
    • (2002) Biochemistry , vol.41 , pp. 3321-3328
    • Milano, S.K.1    Pace, H.C.2    Kim, Y.M.3    Brenner, C.4    Benovic, J.L.5
  • 184
    • 0034725650 scopus 로고    scopus 로고
    • The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits
    • Laporte S.A., Oakley R.H., Holt J.A., Barak L.S., and Caron M.G. The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits. J. Biol. Chem. 275 (2000) 23120-23126
    • (2000) J. Biol. Chem. , vol.275 , pp. 23120-23126
    • Laporte, S.A.1    Oakley, R.H.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 185
    • 0036479228 scopus 로고    scopus 로고
    • Recruitment of activated G protein-coupled receptors to pre-existing clathrin-coated pits in living cells
    • Scott M.G., Benmerah A., Muntaner O., and Marullo S. Recruitment of activated G protein-coupled receptors to pre-existing clathrin-coated pits in living cells. J. Biol. Chem. 277 (2002) 3552-3559
    • (2002) J. Biol. Chem. , vol.277 , pp. 3552-3559
    • Scott, M.G.1    Benmerah, A.2    Muntaner, O.3    Marullo, S.4
  • 186
    • 0030600145 scopus 로고    scopus 로고
    • Dynamin and receptor-mediated endocytosis
    • Damke H. Dynamin and receptor-mediated endocytosis. FEBS Lett. 389 (1996) 48-51
    • (1996) FEBS Lett. , vol.389 , pp. 48-51
    • Damke, H.1
  • 187
    • 33646868636 scopus 로고    scopus 로고
    • Platelet-activating factor-induced clathrin-mediated endocytosis requires beta-arrestin-1 recruitment and activation of the p38 MAPK signalosome at the plasma membrane for actin bundle formation
    • McLaughlin N.J., Banerjee A., Kelher M.R., Gamboni-Robertson F., Hamiel C., Sheppard F.R., Moore E.E., and Silliman C.C. Platelet-activating factor-induced clathrin-mediated endocytosis requires beta-arrestin-1 recruitment and activation of the p38 MAPK signalosome at the plasma membrane for actin bundle formation. J. Immunol. 176 (2006) 7039-7050
    • (2006) J. Immunol. , vol.176 , pp. 7039-7050
    • McLaughlin, N.J.1    Banerjee, A.2    Kelher, M.R.3    Gamboni-Robertson, F.4    Hamiel, C.5    Sheppard, F.R.6    Moore, E.E.7    Silliman, C.C.8
  • 188
    • 0035957235 scopus 로고    scopus 로고
    • Internalization of the human N-formyl peptide and C5a chemoattractant receptors occurs via clathrin-independent mechanisms
    • Gilbert T.L., Bennett T.A., Maestas D.C., Cimino D.F., and Prossnitz E.R. Internalization of the human N-formyl peptide and C5a chemoattractant receptors occurs via clathrin-independent mechanisms. Biochemistry 40 (2001) 3467-3475
    • (2001) Biochemistry , vol.40 , pp. 3467-3475
    • Gilbert, T.L.1    Bennett, T.A.2    Maestas, D.C.3    Cimino, D.F.4    Prossnitz, E.R.5
  • 190
    • 0035852697 scopus 로고    scopus 로고
    • beta-Arrestin 1 and 2 differentially regulate heptahelical receptor signaling and trafficking
    • Kohout T.A., Lin F.S., Perry S.J., Conner D.A., and Lefkowitz R.J. beta-Arrestin 1 and 2 differentially regulate heptahelical receptor signaling and trafficking. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 1601-1606
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1601-1606
    • Kohout, T.A.1    Lin, F.S.2    Perry, S.J.3    Conner, D.A.4    Lefkowitz, R.J.5
  • 191
    • 3242787907 scopus 로고    scopus 로고
    • Agonist-induced trafficking of the low-affinity formyl peptide receptor FPRL1
    • Ernst S., Zobiack N., Boecker K., Gerke V., and Rescher U. Agonist-induced trafficking of the low-affinity formyl peptide receptor FPRL1. Cell. Mol. Life Sci. 61 (2004) 1684-1692
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1684-1692
    • Ernst, S.1    Zobiack, N.2    Boecker, K.3    Gerke, V.4    Rescher, U.5
  • 192
    • 2942618584 scopus 로고    scopus 로고
    • beta-Arrestins: traffic cops of cell signaling
    • Lefkowitz R.J., and Whalen E.J. beta-Arrestins: traffic cops of cell signaling. Curr. Opin. Cell Biol. 16 (2004) 162-168
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 162-168
    • Lefkowitz, R.J.1    Whalen, E.J.2
  • 193
    • 17144364766 scopus 로고    scopus 로고
    • Receptor-specific ubiquitination of beta-arrestin directs assembly and targeting of seven-transmembrane receptor signalosomes
    • Shenoy S.K., and Lefkowitz R.J. Receptor-specific ubiquitination of beta-arrestin directs assembly and targeting of seven-transmembrane receptor signalosomes. J. Biol. Chem. 280 (2005) 15315-15324
    • (2005) J. Biol. Chem. , vol.280 , pp. 15315-15324
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 194
    • 12744261611 scopus 로고    scopus 로고
    • Different endocytosis pathways of the C5a receptor and the N-formyl peptide receptor
    • Suvorova E.S., Gripentrog J.M., and Miettinen H.M. Different endocytosis pathways of the C5a receptor and the N-formyl peptide receptor. Traffic 6 (2005) 100-115
    • (2005) Traffic , vol.6 , pp. 100-115
    • Suvorova, E.S.1    Gripentrog, J.M.2    Miettinen, H.M.3
  • 195
    • 0035834428 scopus 로고    scopus 로고
    • Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin
    • Shenoy S.K., McDonald P.H., Kohout T.A., and Lefkowitz R.J. Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin. Science 294 (2001) 1307-1313
    • (2001) Science , vol.294 , pp. 1307-1313
    • Shenoy, S.K.1    McDonald, P.H.2    Kohout, T.A.3    Lefkowitz, R.J.4
  • 196
    • 0035985175 scopus 로고    scopus 로고
    • Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1
    • Wang Y., Zhou Y., Szabo K., Haft C.R., and Trejo J. Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1. Mol. Biol. Cell 13 (2002) 1965-1976
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1965-1976
    • Wang, Y.1    Zhou, Y.2    Szabo, K.3    Haft, C.R.4    Trejo, J.5
  • 199
    • 0029033888 scopus 로고
    • N-formylpeptide and complement C5a receptors are expressed in liver cells and mediate hepatic acute phase gene regulation
    • McCoy R., Haviland D.L., Molmenti E.P., Ziambaras T., Wetsel R.A., and Perlmutter D.H. N-formylpeptide and complement C5a receptors are expressed in liver cells and mediate hepatic acute phase gene regulation. J. Exp. Med. 182 (1995) 207-217
    • (1995) J. Exp. Med. , vol.182 , pp. 207-217
    • McCoy, R.1    Haviland, D.L.2    Molmenti, E.P.3    Ziambaras, T.4    Wetsel, R.A.5    Perlmutter, D.H.6
  • 200
    • 0031957984 scopus 로고    scopus 로고
    • Mucosal subepithelial binding sites for the bacterial chemotactic peptide, formyl-methionyl-leucyl-phenylanine (FMLP)
    • Anton P., O'Connell J., O'Connell D., Whitaker L., O'Sullivan G.C., Collins J.K., and Shanahan F. Mucosal subepithelial binding sites for the bacterial chemotactic peptide, formyl-methionyl-leucyl-phenylanine (FMLP). Gut 42 (1998) 374-379
    • (1998) Gut , vol.42 , pp. 374-379
    • Anton, P.1    O'Connell, J.2    O'Connell, D.3    Whitaker, L.4    O'Sullivan, G.C.5    Collins, J.K.6    Shanahan, F.7
  • 202
    • 0032550368 scopus 로고    scopus 로고
    • Identification of a human enterocyte lipoxin A4 receptor that is regulated by interleukin (IL)-13 and interferon g and inhibits tumor necrosis factor a-induced IL-8 release
    • Gronert K., Gewirtz A., Madara J.L., and Serhan C.N. Identification of a human enterocyte lipoxin A4 receptor that is regulated by interleukin (IL)-13 and interferon g and inhibits tumor necrosis factor a-induced IL-8 release. J. Exp. Med. 187 (1998) 1285-1294
    • (1998) J. Exp. Med. , vol.187 , pp. 1285-1294
    • Gronert, K.1    Gewirtz, A.2    Madara, J.L.3    Serhan, C.N.4
  • 205
    • 0032525008 scopus 로고    scopus 로고
    • Expression of receptors for C5a anaphylatoxin (CD88) on human bronchial epithelial cells: enhancement of C5a-mediated release of IL-8 upon exposure to cigarette smoke
    • Floreani A.A., Heires A.J., Welniak L.A., Miller-Lindholm A., Clark-Pierce L., Rennard S.I., Morgan E.L., and Sanderson S.D. Expression of receptors for C5a anaphylatoxin (CD88) on human bronchial epithelial cells: enhancement of C5a-mediated release of IL-8 upon exposure to cigarette smoke. J. Immunol. 160 (1998) 5073-5081
    • (1998) J. Immunol. , vol.160 , pp. 5073-5081
    • Floreani, A.A.1    Heires, A.J.2    Welniak, L.A.3    Miller-Lindholm, A.4    Clark-Pierce, L.5    Rennard, S.I.6    Morgan, E.L.7    Sanderson, S.D.8
  • 206
    • 0034052110 scopus 로고    scopus 로고
    • Expression of receptors for complement anaphylatoxins C3a and C5a following permanent focal cerebral ischemia in the mouse
    • Van Beek J., Bernaudin M., Petit E., Gasque P., Nouvelot A., MacKenzie E.T., and Fontaine M. Expression of receptors for complement anaphylatoxins C3a and C5a following permanent focal cerebral ischemia in the mouse. Exp. Neurol. 161 (2000) 373-382
    • (2000) Exp. Neurol. , vol.161 , pp. 373-382
    • Van Beek, J.1    Bernaudin, M.2    Petit, E.3    Gasque, P.4    Nouvelot, A.5    MacKenzie, E.T.6    Fontaine, M.7
  • 207
    • 34547883377 scopus 로고    scopus 로고
    • E. Huet, M.-J. Rabiet, S. Barral, F. Boulay, The role of beta-arrestins in the formyl peptide receptor-like 1 internalization and signaling, submitted for publication.
  • 208
    • 22144481017 scopus 로고    scopus 로고
    • Activation and nuclear translocation of ERK1/2 by the formyl peptide receptor is regulated by G protein and is not dependent on beta-arrestin translocation or receptor endocytosis
    • Gripentrog J.M., and Miettinen H.M. Activation and nuclear translocation of ERK1/2 by the formyl peptide receptor is regulated by G protein and is not dependent on beta-arrestin translocation or receptor endocytosis. Cell Signal 17 (2005) 1300-1311
    • (2005) Cell Signal , vol.17 , pp. 1300-1311
    • Gripentrog, J.M.1    Miettinen, H.M.2


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