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Volumn 78, Issue 11, 2009, Pages 1382-1390

Photolabeling identifies transmembrane domain 4 of CXCR4 as a T140 binding site

Author keywords

CXCR4; GPCR; Ligand binding pocket; Molecular modeling; Photoaffinity labeling; T140

Indexed keywords

AMINO ACID P BENZOYL PHENYLALANINE; CHEMOKINE RECEPTOR CXCR4; GLUTAMINE; LYSINE; PHENYLALANINE DERIVATIVE; T 140; UNCLASSIFIED DRUG;

EID: 70349758088     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2009.07.007     Document Type: Article
Times cited : (18)

References (43)
  • 1
    • 0032499260 scopus 로고    scopus 로고
    • Chemokines and leukocyte traffic
    • Baggiolini M. Chemokines and leukocyte traffic. Nature 392 (1998) 565-568
    • (1998) Nature , vol.392 , pp. 565-568
    • Baggiolini, M.1
  • 2
    • 0031026475 scopus 로고    scopus 로고
    • The chemokine SDF-1 is a chemoattractant for human CD34+ hematopoietic progenitor cells and provides a new mechanism to explain the mobilization of CD34+ progenitors to peripheral blood
    • Aiuti A., Webb I.J., Bleul C., Springer T., and Gutierrez-Ramos J.C. The chemokine SDF-1 is a chemoattractant for human CD34+ hematopoietic progenitor cells and provides a new mechanism to explain the mobilization of CD34+ progenitors to peripheral blood. J Exp Med 185 (1997) 111-120
    • (1997) J Exp Med , vol.185 , pp. 111-120
    • Aiuti, A.1    Webb, I.J.2    Bleul, C.3    Springer, T.4    Gutierrez-Ramos, J.C.5
  • 4
    • 36549058333 scopus 로고    scopus 로고
    • Chemokines in hematopoiesis
    • Broxmeyer H.E. Chemokines in hematopoiesis. Curr Opin Hematol 15 (2008) 49-58
    • (2008) Curr Opin Hematol , vol.15 , pp. 49-58
    • Broxmeyer, H.E.1
  • 5
    • 33750212354 scopus 로고    scopus 로고
    • Stem cell homing
    • Chute J.P. Stem cell homing. Curr Opin Hematol 13 (2006) 399-406
    • (2006) Curr Opin Hematol , vol.13 , pp. 399-406
    • Chute, J.P.1
  • 6
    • 0142172456 scopus 로고    scopus 로고
    • Role of chemokines in angiogenesis: CXCL12/SDF-1 and CXCR4 interaction, a key regulator of endothelial cell responses
    • Salcedo R., and Oppenheim J.J. Role of chemokines in angiogenesis: CXCL12/SDF-1 and CXCR4 interaction, a key regulator of endothelial cell responses. Microcirculation 10 (2003) 359-370
    • (2003) Microcirculation , vol.10 , pp. 359-370
    • Salcedo, R.1    Oppenheim, J.J.2
  • 7
    • 50849144863 scopus 로고    scopus 로고
    • Molecular aspects of rheumatoid arthritis: chemokines in the joints of patients
    • Iwamoto T., Okamoto H., Toyama Y., and Momohara S. Molecular aspects of rheumatoid arthritis: chemokines in the joints of patients. FEBS J 275 (2008) 4448-4455
    • (2008) FEBS J , vol.275 , pp. 4448-4455
    • Iwamoto, T.1    Okamoto, H.2    Toyama, Y.3    Momohara, S.4
  • 8
    • 47749109823 scopus 로고    scopus 로고
    • The role of CXC chemokines and their receptors in cancer
    • Vandercappellen J., Van Damme J., and Struyf S. The role of CXC chemokines and their receptors in cancer. Cancer Lett 267 (2008) 226-244
    • (2008) Cancer Lett , vol.267 , pp. 226-244
    • Vandercappellen, J.1    Van Damme, J.2    Struyf, S.3
  • 9
    • 16044370087 scopus 로고    scopus 로고
    • The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1
    • Oberlin E., Amara A., Bachelerie F., Bessia C., Virelizier J.L., Arenzana-Seisdedos F., et al. The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1. Nature 382 (1996) 833-835
    • (1996) Nature , vol.382 , pp. 833-835
    • Oberlin, E.1    Amara, A.2    Bachelerie, F.3    Bessia, C.4    Virelizier, J.L.5    Arenzana-Seisdedos, F.6
  • 10
    • 27444443142 scopus 로고    scopus 로고
    • The chemokine SDF-1/CXCL12 binds to and signals through the orphan receptor RDC1 in T lymphocytes
    • Balabanian K., Lagane B., Infantino S., Chow K.Y., Harriague J., Moepps B., et al. The chemokine SDF-1/CXCL12 binds to and signals through the orphan receptor RDC1 in T lymphocytes. J Biol Chem 280 (2005) 35760-35766
    • (2005) J Biol Chem , vol.280 , pp. 35760-35766
    • Balabanian, K.1    Lagane, B.2    Infantino, S.3    Chow, K.Y.4    Harriague, J.5    Moepps, B.6
  • 11
    • 3142593911 scopus 로고    scopus 로고
    • Role of the CXCR4/SDF-1 chemokine axis in circulating neutrophil homeostasis
    • Suratt B.T., Petty J.M., Young S.K., Malcolm K.C., Lieber J.G., Nick J.A., et al. Role of the CXCR4/SDF-1 chemokine axis in circulating neutrophil homeostasis. Blood 104 (2004) 565-571
    • (2004) Blood , vol.104 , pp. 565-571
    • Suratt, B.T.1    Petty, J.M.2    Young, S.K.3    Malcolm, K.C.4    Lieber, J.G.5    Nick, J.A.6
  • 12
    • 7944236603 scopus 로고    scopus 로고
    • A new key in breast cancer metastasis
    • Benovic J.L., and Marchese A. A new key in breast cancer metastasis. Cancer Cell 6 (2004) 429-430
    • (2004) Cancer Cell , vol.6 , pp. 429-430
    • Benovic, J.L.1    Marchese, A.2
  • 14
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng Y., Broder C.C., Kennedy P.E., and Berger E.A. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272 (1996) 872-877
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 15
    • 32544446940 scopus 로고    scopus 로고
    • HIV and the chemokine system: 10 years later
    • Lusso P. HIV and the chemokine system: 10 years later. EMBO J 25 (2006) 447-456
    • (2006) EMBO J , vol.25 , pp. 447-456
    • Lusso, P.1
  • 17
    • 0032583575 scopus 로고    scopus 로고
    • A low-molecular-weight inhibitor against the chemokine receptor CXCR4: a strong anti-HIV peptide T140
    • Tamamura H., Xu Y., Hattori T., Zhang X., Arakaki R., Kanbara K., et al. A low-molecular-weight inhibitor against the chemokine receptor CXCR4: a strong anti-HIV peptide T140. Biochem Biophys Res Commun 253 (1998) 877-882
    • (1998) Biochem Biophys Res Commun , vol.253 , pp. 877-882
    • Tamamura, H.1    Xu, Y.2    Hattori, T.3    Zhang, X.4    Arakaki, R.5    Kanbara, K.6
  • 18
    • 0034835884 scopus 로고    scopus 로고
    • Peptide-lead CXCR4 antagonists with high anti-HIV activity
    • Fujii N., and Tamamura H. Peptide-lead CXCR4 antagonists with high anti-HIV activity. Curr Opin Investig Drugs 2 (2001) 1198-1202
    • (2001) Curr Opin Investig Drugs , vol.2 , pp. 1198-1202
    • Fujii, N.1    Tamamura, H.2
  • 19
    • 33745076246 scopus 로고    scopus 로고
    • Development of a linear type of low molecular weight CXCR4 antagonists based on T140 analogs
    • Tamamura H., Tsutsumi H., Masuno H., Mizokami S., Hiramatsu K., Wang Z., et al. Development of a linear type of low molecular weight CXCR4 antagonists based on T140 analogs. Org Biomol Chem 4 (2006) 2354-2357
    • (2006) Org Biomol Chem , vol.4 , pp. 2354-2357
    • Tamamura, H.1    Tsutsumi, H.2    Masuno, H.3    Mizokami, S.4    Hiramatsu, K.5    Wang, Z.6
  • 20
    • 3042593906 scopus 로고    scopus 로고
    • Identification of a CXCR4 antagonist, a T140 analog, as an anti-rheumatoid arthritis agent
    • Tamamura H., Fujisawa M., Hiramatsu K., Mizumoto M., Nakashima H., Yamamoto N., et al. Identification of a CXCR4 antagonist, a T140 analog, as an anti-rheumatoid arthritis agent. FEBS Lett 569 (2004) 99-104
    • (2004) FEBS Lett , vol.569 , pp. 99-104
    • Tamamura, H.1    Fujisawa, M.2    Hiramatsu, K.3    Mizumoto, M.4    Nakashima, H.5    Yamamoto, N.6
  • 21
    • 0142102523 scopus 로고    scopus 로고
    • T140 analogs as CXCR4 antagonists identified as anti-metastatic agents in the treatment of breast cancer
    • Tamamura H., Hori A., Kanzaki N., Hiramatsu K., Mizumoto M., Nakashima H., et al. T140 analogs as CXCR4 antagonists identified as anti-metastatic agents in the treatment of breast cancer. FEBS Lett 550 (2003) 79-83
    • (2003) FEBS Lett , vol.550 , pp. 79-83
    • Tamamura, H.1    Hori, A.2    Kanzaki, N.3    Hiramatsu, K.4    Mizumoto, M.5    Nakashima, H.6
  • 22
    • 0037025357 scopus 로고    scopus 로고
    • A point mutation that confers constitutive activity to CXCR4 reveals that T140 is an inverse agonist and that AMD3100 and ALX40-4C are weak partial agonists
    • Zhang W.B., Navenot J.M., Haribabu B., Tamamura H., Hiramatu K., Omagari A., et al. A point mutation that confers constitutive activity to CXCR4 reveals that T140 is an inverse agonist and that AMD3100 and ALX40-4C are weak partial agonists. J Biol Chem 277 (2002) 24515-24521
    • (2002) J Biol Chem , vol.277 , pp. 24515-24521
    • Zhang, W.B.1    Navenot, J.M.2    Haribabu, B.3    Tamamura, H.4    Hiramatu, K.5    Omagari, A.6
  • 23
    • 0034606466 scopus 로고    scopus 로고
    • Pharmacophore identification of a specific CXCR4 inhibitor, T140, leads to development of effective anti-HIV agents with very high selectivity indexes
    • Tamamura H., Omagari A., Oishi S., Kanamoto T., Yamamoto N., Peiper S.C., et al. Pharmacophore identification of a specific CXCR4 inhibitor, T140, leads to development of effective anti-HIV agents with very high selectivity indexes. Bioorg Med Chem Lett 10 (2000) 2633-2637
    • (2000) Bioorg Med Chem Lett , vol.10 , pp. 2633-2637
    • Tamamura, H.1    Omagari, A.2    Oishi, S.3    Kanamoto, T.4    Yamamoto, N.5    Peiper, S.C.6
  • 24
    • 0034604709 scopus 로고    scopus 로고
    • Identification of residues of CXCR4 critical for human immunodeficiency virus coreceptor and chemokine receptor activities
    • Brelot A., Heveker N., Montes M., and Alizon M. Identification of residues of CXCR4 critical for human immunodeficiency virus coreceptor and chemokine receptor activities. J Biol Chem 275 (2000) 23736-23744
    • (2000) J Biol Chem , vol.275 , pp. 23736-23744
    • Brelot, A.1    Heveker, N.2    Montes, M.3    Alizon, M.4
  • 25
    • 0035900771 scopus 로고    scopus 로고
    • Structural and functional characterization of human CXCR4 as a chemokine receptor and HIV-1 co-receptor by mutagenesis and molecular modeling studies
    • Zhou N., Luo Z., Luo J., Liu D., Hall J.W., Pomerantz R.J., et al. Structural and functional characterization of human CXCR4 as a chemokine receptor and HIV-1 co-receptor by mutagenesis and molecular modeling studies. J Biol Chem 276 (2001) 42826-42833
    • (2001) J Biol Chem , vol.276 , pp. 42826-42833
    • Zhou, N.1    Luo, Z.2    Luo, J.3    Liu, D.4    Hall, J.W.5    Pomerantz, R.J.6
  • 26
    • 0036838693 scopus 로고    scopus 로고
    • Identification of conserved and variable structures in the human immunodeficiency virus gp120 glycoprotein of importance for CXCR4 binding
    • Basmaciogullari S., Babcock G.J., Van Ryk D., Wojtowicz W., and Sodroski J. Identification of conserved and variable structures in the human immunodeficiency virus gp120 glycoprotein of importance for CXCR4 binding. J Virol 76 (2002) 10791-10800
    • (2002) J Virol , vol.76 , pp. 10791-10800
    • Basmaciogullari, S.1    Babcock, G.J.2    Van Ryk, D.3    Wojtowicz, W.4    Sodroski, J.5
  • 27
    • 0344012474 scopus 로고    scopus 로고
    • Lipid bilayer simulations of CXCR4 with inverse agonists and weak partial agonists
    • Trent J.O., Wang Z.X., Murray J.L., Shao W., Tamamura H., Fujii N., et al. Lipid bilayer simulations of CXCR4 with inverse agonists and weak partial agonists. J Biol Chem 278 (2003) 47136-47144
    • (2003) J Biol Chem , vol.278 , pp. 47136-47144
    • Trent, J.O.1    Wang, Z.X.2    Murray, J.L.3    Shao, W.4    Tamamura, H.5    Fujii, N.6
  • 28
    • 0028235205 scopus 로고
    • Benzophenone photophores in biochemistry
    • Dorman G., and Prestwich G.D. Benzophenone photophores in biochemistry. Biochemistry 33 (1994) 5661-5673
    • (1994) Biochemistry , vol.33 , pp. 5661-5673
    • Dorman, G.1    Prestwich, G.D.2
  • 29
    • 0034663965 scopus 로고    scopus 로고
    • Photolabeling identifies position 172 of the human AT(1) receptor as a ligand contact point: receptor-bound angiotensin II adopts an extended structure
    • Boucard A.A., Wilkes B.C., Laporte S.A., Escher E., Guillemette G., and Leduc R. Photolabeling identifies position 172 of the human AT(1) receptor as a ligand contact point: receptor-bound angiotensin II adopts an extended structure. Biochemistry 39 (2000) 9662-9670
    • (2000) Biochemistry , vol.39 , pp. 9662-9670
    • Boucard, A.A.1    Wilkes, B.C.2    Laporte, S.A.3    Escher, E.4    Guillemette, G.5    Leduc, R.6
  • 30
    • 0033324715 scopus 로고    scopus 로고
    • Determination of peptide contact points in the human angiotensin II type I receptor (AT1) with photosensitive analogs of angiotensin II
    • Laporte S.A., Boucard A.A., Servant G., Guillemette G., Leduc R., and Escher E. Determination of peptide contact points in the human angiotensin II type I receptor (AT1) with photosensitive analogs of angiotensin II. Mol Endocrinol 13 (1999) 578-586
    • (1999) Mol Endocrinol , vol.13 , pp. 578-586
    • Laporte, S.A.1    Boucard, A.A.2    Servant, G.3    Guillemette, G.4    Leduc, R.5    Escher, E.6
  • 31
    • 33846947213 scopus 로고    scopus 로고
    • Photolabelling the urotensin II receptor reveals distinct agonist- and partial-agonist-binding sites
    • Holleran B.J., Beaulieu M.E., Proulx C.D., Lavigne P., Escher E., and Leduc R. Photolabelling the urotensin II receptor reveals distinct agonist- and partial-agonist-binding sites. Biochem J 402 (2007) 51-61
    • (2007) Biochem J , vol.402 , pp. 51-61
    • Holleran, B.J.1    Beaulieu, M.E.2    Proulx, C.D.3    Lavigne, P.4    Escher, E.5    Leduc, R.6
  • 32
    • 0035929548 scopus 로고    scopus 로고
    • Identification of peptide ligand-binding domains within the human motilin receptor using photoaffinity labeling
    • Coulie B., Matsuura B., Dong M., Hadac E.M., Pinon D.I., Feighner S.D., et al. Identification of peptide ligand-binding domains within the human motilin receptor using photoaffinity labeling. J Biol Chem 276 (2001) 35518-35522
    • (2001) J Biol Chem , vol.276 , pp. 35518-35522
    • Coulie, B.1    Matsuura, B.2    Dong, M.3    Hadac, E.M.4    Pinon, D.I.5    Feighner, S.D.6
  • 33
    • 0017874586 scopus 로고
    • Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril
    • Fraker P.J., and Speck Jr. J.C. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril. Biochem Biophys Res Commun 80 (1978) 849-857
    • (1978) Biochem Biophys Res Commun , vol.80 , pp. 849-857
    • Fraker, P.J.1    Speck Jr., J.C.2
  • 35
    • 0036208960 scopus 로고    scopus 로고
    • Hemofiltrate CC chemokine 1[9-74] causes effective internalization of CCR5 and is a potent inhibitor of R5-tropic human immunodeficiency virus type 1 strains in primary T cells and macrophages
    • Munch J., Standker L., Pohlmann S., Baribaud F., Papkalla A., Rosorius O., et al. Hemofiltrate CC chemokine 1[9-74] causes effective internalization of CCR5 and is a potent inhibitor of R5-tropic human immunodeficiency virus type 1 strains in primary T cells and macrophages. Antimicrob Agents Chemother 46 (2002) 982-990
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 982-990
    • Munch, J.1    Standker, L.2    Pohlmann, S.3    Baribaud, F.4    Papkalla, A.5    Rosorius, O.6
  • 36
    • 0026442236 scopus 로고
    • An infectious molecular clone of an unusual macrophage-tropic and highly cytopathic strain of human immunodeficiency virus type 1
    • Collman R., Balliet J.W., Gregory S.A., Friedman H., Kolson D.L., Nathanson N., et al. An infectious molecular clone of an unusual macrophage-tropic and highly cytopathic strain of human immunodeficiency virus type 1. J Virol 66 (1992) 7517-7521
    • (1992) J Virol , vol.66 , pp. 7517-7521
    • Collman, R.1    Balliet, J.W.2    Gregory, S.A.3    Friedman, H.4    Kolson, D.L.5    Nathanson, N.6
  • 37
    • 52949102889 scopus 로고    scopus 로고
    • Crystal structure of opsin in its G-protein-interacting conformation
    • Scheerer P., Park J.H., Hildebrand P.W., Kim Y.J., Krauss N., Choe H.W., et al. Crystal structure of opsin in its G-protein-interacting conformation. Nature 455 (2008) 497-502
    • (2008) Nature , vol.455 , pp. 497-502
    • Scheerer, P.1    Park, J.H.2    Hildebrand, P.W.3    Kim, Y.J.4    Krauss, N.5    Choe, H.W.6
  • 38
    • 0035847678 scopus 로고    scopus 로고
    • Conformational study of a highly specific CXCR4 inhibitor, T140, disclosing the close proximity of its intrinsic pharmacophores associated with strong anti-HIV activity
    • Tamamura H., Sugioka M., Odagaki Y., Omagari A., Kan Y., Oishi S., et al. Conformational study of a highly specific CXCR4 inhibitor, T140, disclosing the close proximity of its intrinsic pharmacophores associated with strong anti-HIV activity. Bioorg Med Chem Lett 11 (2001) 359-362
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 359-362
    • Tamamura, H.1    Sugioka, M.2    Odagaki, Y.3    Omagari, A.4    Kan, Y.5    Oishi, S.6
  • 39
    • 35548996783 scopus 로고    scopus 로고
    • Disrupted cardiac development but normal hematopoiesis in mice deficient in the second CXCL12/SDF-1 receptor, CXCR7
    • Sierro F., Biben C., Martinez-Munoz L., Mellado M., Ransohoff R.M., Li M., et al. Disrupted cardiac development but normal hematopoiesis in mice deficient in the second CXCL12/SDF-1 receptor, CXCR7. Proc Natl Acad Sci USA 104 (2007) 14759-14764
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 14759-14764
    • Sierro, F.1    Biben, C.2    Martinez-Munoz, L.3    Mellado, M.4    Ransohoff, R.M.5    Li, M.6
  • 41
    • 0035423565 scopus 로고    scopus 로고
    • Pharmacological evidence for complex and multiple site interaction of CXCR4 with SDF-1alpha: implications for development of selective CXCR4 antagonists
    • Gupta S.K., Pillarisetti K., Thomas R.A., and Aiyar N. Pharmacological evidence for complex and multiple site interaction of CXCR4 with SDF-1alpha: implications for development of selective CXCR4 antagonists. Immunol Lett 78 (2001) 29-34
    • (2001) Immunol Lett , vol.78 , pp. 29-34
    • Gupta, S.K.1    Pillarisetti, K.2    Thomas, R.A.3    Aiyar, N.4
  • 42
    • 35348848462 scopus 로고    scopus 로고
    • Replication-competent variants of human immunodeficiency virus type 2 lacking the V3 loop exhibit resistance to chemokine receptor antagonists
    • Lin G., Bertolotti-Ciarlet A., Haggarty B., Romano J., Nolan K.M., Leslie G.J., et al. Replication-competent variants of human immunodeficiency virus type 2 lacking the V3 loop exhibit resistance to chemokine receptor antagonists. J Virol 81 (2007) 9956-9966
    • (2007) J Virol , vol.81 , pp. 9956-9966
    • Lin, G.1    Bertolotti-Ciarlet, A.2    Haggarty, B.3    Romano, J.4    Nolan, K.M.5    Leslie, G.J.6
  • 43
    • 33645658328 scopus 로고    scopus 로고
    • Stereospecific synthesis of a carbene-generating angiotensin II analogue for comparative photoaffinity labeling: improved incorporation and absence of methionine selectivity
    • Fillion D., Deraet M., Holleran B.J., and Escher E. Stereospecific synthesis of a carbene-generating angiotensin II analogue for comparative photoaffinity labeling: improved incorporation and absence of methionine selectivity. J Med Chem 49 (2006) 2200-2209
    • (2006) J Med Chem , vol.49 , pp. 2200-2209
    • Fillion, D.1    Deraet, M.2    Holleran, B.J.3    Escher, E.4


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