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Volumn 296, Issue 3, 2002, Pages 507-514

Human α-fetoprotein binds to primary macrophages

Author keywords

Fetoprotein; CCR5; Glycans; Macrophages

Indexed keywords

ALPHA FETOPROTEIN; CARBOHYDRATE; CHEMOKINE RECEPTOR CCR5; GLYCOPROTEIN GP 120; LECTIN; MACROPHAGE INFLAMMATORY PROTEIN 1BETA; SIALIDASE;

EID: 0036382920     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)00909-9     Document Type: Article
Times cited : (30)

References (42)
  • 1
    • 0034059192 scopus 로고    scopus 로고
    • HIV-1 co-receptor expression on trophoblastic cells from early placentas and permissivity to infection by several HIV-1 primary isolates
    • B. Mognetti, M. Moussa, J. Croitoru, E. Menu, D. Dormont, P. Roques, G. Chaouat, HIV-1 co-receptor expression on trophoblastic cells from early placentas and permissivity to infection by several HIV-1 primary isolates, Clin. Exp. Immunol. 199 (2000) 486-492.
    • (2000) Clin. Exp. Immunol. , vol.199 , pp. 486-492
    • Mognetti, B.1    Moussa, M.2    Croitoru, J.3    Menu, E.4    Dormont, D.5    Roques, P.6    Chaouat, G.7
  • 2
    • 0025318735 scopus 로고
    • HIV-1 in trophoblastic and villous Hofbauer cells, and haematological precursors in eight-week fetuses
    • S. H. Lewis, C. Reynolds-Kohler, H.E. Fox, J.A. Nelson, HIV-1 in trophoblastic and villous Hofbauer cells, and haematological precursors in eight-week fetuses, Lancet 335 (1990) 565-568.
    • (1990) Lancet , vol.335 , pp. 565-568
    • Lewis, S.H.1    Reynolds-Kohler, C.2    Fox, H.E.3    Nelson, J.A.4
  • 5
    • 0030018156 scopus 로고    scopus 로고
    • CC Ckr-5: RANTES MIP-1α, MIP-1β receptor as a function cofactor for macrophage-tropic HIV-1
    • G. Alkhatib, C. Combadiere, C.C. Broder, Y. Feng, P.E. Kennedy, P.M. Murphy, E.A. Berger, CC CKR-5: A RANTES, MIP-1α, MIP-1β receptor as a function cofactor for macrophage-tropic HIV-1, Science 272 (1996) 1955-1958.
    • (1996) Science , vol.272 , pp. 1955-1958
    • Alkhatib, G.1    Combadiere, C.2    Broder, C.C.3    Feng, Y.4    Kennedy, P.E.5    Murphy, P.M.6    Berger, E.A.7
  • 6
    • 0030745286 scopus 로고    scopus 로고
    • Arenzada-Seisdedos HIV coreceptor downregulation as antiviral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication
    • A. Amara, S. Le Gall, O. Schwartz, J. Salamero, M. Montes, P. Loetscher, M. Baggiolini, J.L. Virelizier, F. Arenzada-Seisdedos, HIV coreceptor downregulation as antiviral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication, J. Exp. Med. 186 (1997) 139-146.
    • (1997) J. Exp. Med. , vol.186 , pp. 139-146
    • Amara, A.1    Le, S.2    Gall, O.3    Schwartz, J.4    Salamero, M.5    Montes, P.6    Loetscher, M.7    Baggiolini, J.L.8    Virelizier, F.9
  • 10
    • 0031575431 scopus 로고    scopus 로고
    • Change in coreceptor use correlates with disease progression in HIV-1 infected individuals
    • R.I. Connor, K.E. Sheridan, D. Ceradini, S. Choe, N.R. Landau, Change in coreceptor use correlates with disease progression in HIV-1 infected individuals, J. Exp. Med. 185 (1997) 625-628.
    • (1997) J. Exp. Med. , vol.185 , pp. 625-628
    • Connor, R.I.1    Sheridan, K.E.2    Ceradini, D.3    Choe, S.4    Landau, N.R.5
  • 11
    • 0024549386 scopus 로고
    • Role of N-linked glycans in the interaction between the envelope glycoprotein of human immunodeficiency virus and its CD4 cellular receptor. Structural enzymatic analysis
    • E. Fenouillet, B. Clerget-Raslain, J.C. Gluckman, D. Guétard, L. Montagnier, E. Bahraoui, Role of N-linked glycans in the interaction between the envelope glycoprotein of human immunodeficiency virus and its CD4 cellular receptor. Structural enzymatic analysis, J. Exp. Med. 3 (1989) 807-821.
    • (1989) J. Exp. Med. , vol.3 , pp. 807-821
    • Fenouillet, E.1    Clerget-Raslain, B.2    Gluckman, J.C.3    Guétard, D.4    Montagnier, L.5    Bahraoui, E.6
  • 12
    • 0025331559 scopus 로고
    • Role of N-linked glycans of envelope glycoproteins in infectivity of human immunodeficiency virus type 1
    • E. Fenouillet, J.C. Gluckman, E.M.J. Bahraoui, Role of N-linked glycans of envelope glycoproteins in infectivity of human immunodeficiency virus type 1, J. Virol. 64 (1990) 2841-2848.
    • (1990) J. Virol. , vol.64 , pp. 2841-2848
    • Fenouillet, E.1    Gluckman, J.C.2    Bahraoui, E.M.J.3
  • 15
    • 0027095766 scopus 로고
    • Carbohydrate binding properties of the envelope glycoproteins of human immunodeficiency virus type 1
    • M. Haidar, N. Seddiki, J.C. Gluckman, L. Gattegno, Carbohydrate binding properties of the envelope glycoproteins of human immunodeficiency virus type 1, Glycoconj. J. 9 (1992) 315-323.
    • (1992) Glycoconj. J. , vol.9 , pp. 315-323
    • Haidar, M.1    Seddiki, N.2    Gluckman, J.C.3    Gattegno, L.4
  • 16
    • 0028987366 scopus 로고
    • Specific interaction between HIV-1 major envelope glycoprotein and orosomucoid
    • L. Rabehi, F. Ferrìere, L. Gattegno, Specific interaction between HIV-1 major envelope glycoprotein and orosomucoid, Glycoconj. J. 12 (1995) 7-16.
    • (1995) Glycoconj. J. , vol.12 , pp. 7-16
    • Rabehi, L.1    Ferrière, F.2    Gattegno, L.3
  • 18
    • 0026794398 scopus 로고
    • Mannosyl/N-acetyl-β-D-glucosaminyl binding properties of the envelope glycoproteins of human immunodeficiency virus type 2
    • M. Haidar, J.C. Gluckman, L. Gattegno, Mannosyl/N-acetyl-β-D-glucosaminyl binding properties of the envelope glycoproteins of human immunodeficiency virus type 2, Glycobiology 2 (1992) 429-435.
    • (1992) Glycobiology , vol.2 , pp. 429-435
    • Haidar, M.1    Gluckman, J.C.2    Gattegno, L.3
  • 20
    • 0016586599 scopus 로고
    • Normal biology of α-fetoprotein
    • D. Gitlin, Normal biology of α-fetoprotein, Ann. NY Acad. Sci. 259 (1975) 7-16.
    • (1975) Ann. NY Acad. Sci. , vol.259 , pp. 7-16
    • Gitlin, D.1
  • 21
    • 0024361373 scopus 로고
    • α-Fetoprotein: 25 years of study
    • G.I. Abelev, α-Fetoprotein: 25 years of study, Tumor. Biol. 10 (1989) 63-74.
    • (1989) Tumor. Biol. , vol.10 , pp. 63-74
    • Abelev, G.I.1
  • 22
    • 0030601058 scopus 로고    scopus 로고
    • Lectin affinity electrophoretic demonstration of tissue specificity and malignant alteration of human α-fetoprotein isoforms produced transgenic mice
    • Y. Koyama, M. Sakai, T. Kitagaawa, K. Taketa, S. Nishi, Lectin affinity electrophoretic demonstration of tissue specificity and malignant alteration of human α-fetoprotein isoforms produced transgenic mice, Biochem. Biophys. Res. Commun. 233 (1996) 757-761.
    • (1996) Biochem. Biophys. Res. Commun. , vol.233 , pp. 757-761
    • Koyama, Y.1    Sakai, M.2    Kitagaawa, T.3    Taketa, K.4    Nishi, S.5
  • 23
    • 0028124236 scopus 로고
    • Biochemical characterization of bovine α-fetoprotein and comparison with human α-fetoprotein
    • Y. He, B.A. Keel, Biochemical characterization of bovine a-fetoprotein and comparison with human α-fetoprotein, Comp. Biochem. Physiol. Biochem. Mol. Biol. 108 (1994) 327-336.
    • (1994) Comp. Biochem. Physiol. Biochem. Mol. Biol. , vol.108 , pp. 327-336
    • He, Y.1    Keel, B.A.2
  • 24
    • 0015814369 scopus 로고
    • Increased α-fetoprotein in amniotic fluid associated with congenital oesophagial atresia
    • M. Seppala, Increased α-fetoprotein in amniotic fluid associated with congenital oesophagial atresia, Obstet. Gynecol. 42 (1973) 613-624.
    • (1973) Obstet. Gynecol. , vol.42 , pp. 613-624
    • Seppala, M.1
  • 25
    • 0016606444 scopus 로고
    • Maternal serum α-fetoprotein levels in multiple pregnancy
    • N. Wald, S. Barker, R. Peto, D.J.H. Brock, J. Bonnar, Maternal serum α-fetoprotein levels in multiple pregnancy, Br. Med. J. 1 (1975) 651-652.
    • (1975) Br. Med. J. , vol.1 , pp. 651-652
    • Wald, N.1    Barker, S.2    Peto, R.3    Brock, D.J.H.4    Bonnar, J.5
  • 27
    • 0028014379 scopus 로고
    • A monoclonal antibody directed to sulfatides inhibits the binding of human immunodeficiency virus (HIV-1) envelope glycoprotein to macrophages but not their infectivity by the virus
    • N. Seddiki, A. Ramdani, L. Saffar, J. Portoukalian, J.C. Gluckman, L. Gattegno, A monoclonal antibody directed to sulfatides inhibits the binding of human immunodeficiency virus (HIV-1) envelope glycoprotein to macrophages but not their infectivity by the virus, Biochem. Biophys. Acta 1225 (1994) 289-296.
    • (1994) Biochem. Biophys. Acta , vol.1225 , pp. 289-296
    • Seddiki, N.1    Ramdani, A.2    Saffar, L.3    Portoukalian, J.4    Gluckman, J.C.5    Gattegno, L.6
  • 30
    • 0031646364 scopus 로고    scopus 로고
    • Interactions of human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein V3 loop with CCR5 and CD4 at the membrane of human primary macrophages
    • L. Rabehi, N. Seddiki, A. Benjouad, J.C. Gluckman, L. Gattegno, Interactions of human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein V3 loop with CCR5 and CD4 at the membrane of human primary macrophages, AIDS Res. Hum. Retroviruses 18 (1998) 1605-1615.
    • (1998) AIDS Res. Hum. Retroviruses , vol.18 , pp. 1605-1615
    • Rabehi, L.1    Seddiki, N.2    Benjouad, A.3    Gluckman, J.C.4    Gattegno, L.5
  • 31
    • 0015694574 scopus 로고
    • Structure of α-1 acid glycoprotein: The complete amino acid sequence, multiple amino acid substitutions and homology with the immunoglobulins
    • K. Schmidt, H. Kaufmann, F. Isemura, J. Emura, T. Motuyama, M. Ishiguro, S. Nanno, Structure of α-1 acid glycoprotein: the complete amino acid sequence, multiple amino acid substitutions and homology with the immunoglobulins, Biochemistry 12 (1973) 2711-2724.
    • (1973) Biochemistry , vol.12 , pp. 2711-2724
    • Schmidt, K.1    Kaufmann, H.2    Isemura, F.3    Emura, J.4    Motuyama, T.5    Ishiguro, M.6    Nanno, S.7
  • 36
    • 0017564026 scopus 로고
    • The effect of α-fetoprotein on the immune response. III. Diminution of the phagocytic capacity of macrophages cultures in vitro in the presence of mouse amniotic fluid or α-fetoprotein
    • A. Olinescu, M. Laky, D.E. Pofescu, A. Dumitrescu, D. Ganea, The effect of α-fetoprotein on the immune response. III. Diminution of the phagocytic capacity of macrophages cultures in vitro in the presence of mouse amniotic fluid or α-fetoprotein, Arch. Roum. athol. Exp. Microbiol. 36 (1978) 247-253.
    • (1978) Arch. Roum. athol. Exp. Microbiol. , vol.36 , pp. 247-253
    • Olinescu, A.1    Laky, M.2    Pofescu, D.E.3    Dumitrescu, A.4    Ganea, D.5
  • 37
    • 0026440453 scopus 로고
    • Isolation and partial characterization of a specific α-fetoprotein receptor on human monocytes
    • Y. Suzuki, Q.Y. Carl, Y. Zeng, E. Alpert, Isolation and partial characterization of a specific α-fetoprotein receptor on human monocytes, J. Clin. Invest. 90 (1992) 1530-1536.
    • (1992) J. Clin. Invest. , vol.90 , pp. 1530-1536
    • Suzuki, Y.1    Carl, Q.Y.2    Zeng, Y.3    Alpert, E.4
  • 38
    • 0021816248 scopus 로고
    • Cell-type specific receptors for α-fetoprotein in mouse T-lymphoma cell line
    • J. Naval, M. Villacampa, A. Guoguel, J. Uriel, Cell-type specific receptors for α-fetoprotein in mouse T-lymphoma cell line, Proc. Natl. Acad. Sci. USA 82 (1985) 3301-3305.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3301-3305
    • Naval, J.1    Villacampa, M.2    Guoguel, A.3    Uriel, J.4
  • 40
    • 0032488240 scopus 로고    scopus 로고
    • The inhibitory effect of RANTES on infection of primary macrophages by R5 human immunodeficiency virus type-1 depends on macrophage activation state
    • S. Azamzi, L. Ylisastigui, Y. Bakri, L. Rabehi, L. Gattegno, M. Parmentier, J.C. Gluckman, A. Benjouad, The inhibitory effect of RANTES on infection of primary macrophages by R5 human immunodeficiency virus type-1 depends on macrophage activation state, Virology 252 (1998) 96-105.
    • (1998) Virology , vol.252 , pp. 96-105
    • Azamzi, S.1    Ylisastigui, L.2    Bakri, Y.3    Rabehi, L.4    Gattegno, L.5    Parmentier, M.6    Gluckman, J.C.7    Benjouad, A.8
  • 41
    • 0034697016 scopus 로고    scopus 로고
    • Examination of the function of RANTES, MIP-1α, and MIP-1α following interaction with heparin-like glycosaminoglycans
    • S. Ali, A.C. Palmer, B. Banerjee, S.J. Fritchley, J.A. Kirby, Examination of the function of RANTES, MIP-1α, and MIP-1α following interaction with heparin-like glycosaminoglycans, J. Biol. Chem. 275 (2000) 11721-11727.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11721-11727
    • Ali, S.1    Palmer, A.C.2    Banerjee, B.3    Fritchley, S.J.4    Kirby, J.A.5
  • 42
    • 0033942750 scopus 로고    scopus 로고
    • V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies
    • A. Ly, L. Stamatatos, V2 loop glycosylation of the human immunodeficiency virus type 1 SF162 envelope facilitates interaction of this protein with CD4 and CCR5 receptors and protects the virus from neutralization by anti-V3 loop and anti-CD4 binding site antibodies, J. Virol. 74 (2000) 6769-6776.
    • (2000) J. Virol. , vol.74 , pp. 6769-6776
    • Ly, A.1    Stamatatos, L.2


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