메뉴 건너뛰기




Volumn 187, Issue 2, 2011, Pages 748-759

Protein kinase C and NF-κB-dependent CD4 downregulation in macrophages induced by T cell-derived soluble factors: Consequences for HIV-1 infection

Author keywords

[No Author keywords available]

Indexed keywords

ATTRACTIN; CD4 ANTIGEN; CHEMOKINE RECEPTOR CCR5; CHEMOKINE RECEPTOR CXCR4; FIBRONECTIN; GALECTIN 3; GAMMA INTERFERON; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 13; INTERLEUKIN 16; INTERLEUKIN 5; INTERLEUKIN 8; MACROPHAGE INFLAMMATORY PROTEIN 1ALPHA; MACROPHAGE INFLAMMATORY PROTEIN 1BETA; MACROPHAGE MIGRATION INHIBITION FACTOR; PROTEASOME; PROTEIN KINASE C; RANTES; SERINE; SERINE PROTEINASE INHIBITOR; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING 1; TUMOR NECROSIS FACTOR ALPHA;

EID: 79960510967     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1003678     Document Type: Article
Times cited : (13)

References (75)
  • 2
    • 33644783594 scopus 로고    scopus 로고
    • Marked differences in the structures and protein associations of lymphocyte and monocyte CD4: Resolution of a novel CD4 isoform
    • Lynch, G. W., S. Turville, B. Carter, A. J. Sloane, A. Chan, N. Muljadi, S. Li, L. Low, P. Armati, R. Raison, et al. 2006. Marked differences in the structures and protein associations of lymphocyte and monocyte CD4: resolution of a novel CD4 isoform. Immunol. Cell Biol. 84: 154-165.
    • (2006) Immunol. Cell Biol. , vol.84 , pp. 154-165
    • Lynch, G.W.1    Turville, S.2    Carter, B.3    Sloane, A.J.4    Chan, A.5    Muljadi, N.6    Li, S.7    Low, L.8    Armati, P.9    Raison, R.10
  • 3
    • 0035383817 scopus 로고    scopus 로고
    • Mast cells/basophils in the peripheral blood of allergic individuals who are HIV-1 susceptible due to their surface expression of CD4 and the chemokine receptors CCR3, CCR5, and CXCR4
    • Li, Y., L. Li, R. Wadley, S. W. Reddel, J. C. Qi, C. Archis, A. Collins, E. Clark, M. Cooley, S. Kouts, et al. 2001. Mast cells/basophils in the peripheral blood of allergic individuals who are HIV-1 susceptible due to their surface expression of CD4 and the chemokine receptors CCR3, CCR5, and CXCR4. Blood 97: 3484-3490.
    • (2001) Blood , vol.97 , pp. 3484-3490
    • Li, Y.1    Li, L.2    Wadley, R.3    Reddel, S.W.4    Qi, J.C.5    Archis, C.6    Collins, A.7    Clark, E.8    Cooley, M.9    Kouts, S.10
  • 5
    • 0035863718 scopus 로고    scopus 로고
    • Positive and negative selection of thymocytes depends on Lck interaction with the CD4 and CD8 coreceptors
    • Trobridge, P. A., K. A. Forbush, and S. D. Levin. 2001. Positive and negative selection of thymocytes depends on Lck interaction with the CD4 and CD8 coreceptors. J. Immunol. 166: 809-818.
    • (2001) J. Immunol. , vol.166 , pp. 809-818
    • Trobridge, P.A.1    Forbush, K.A.2    Levin, S.D.3
  • 6
    • 0023521229 scopus 로고
    • Interaction between CD4 and class II MHC molecules mediates cell adhesion
    • Doyle, C., and J. L. Strominger. 1987. Interaction between CD4 and class II MHC molecules mediates cell adhesion. Nature 330: 256-259.
    • (1987) Nature , vol.330 , pp. 256-259
    • Doyle, C.1    Strominger, J.L.2
  • 7
    • 0036382872 scopus 로고    scopus 로고
    • CD4 is active as a signaling molecule on the human monocytic cell line Thp-1
    • Graziani-Bowering, G. M., L. G. Filion, P. Thibault, and M. Kozlowski. 2002. CD4 is active as a signaling molecule on the human monocytic cell line Thp-1. Exp. Cell Res. 279: 141-152.
    • (2002) Exp. Cell Res. , vol.279 , pp. 141-152
    • Graziani-Bowering, G.M.1    Filion, L.G.2    Thibault, P.3    Kozlowski, M.4
  • 8
    • 0024385389 scopus 로고
    • Cell surface comodulation of CD4 and T cell receptor by anti-CD4 monoclonal antibody
    • Cole, J. A., S. A. McCarthy, M. A. Rees, S. O. Sharrow, and A. Singer. 1989. Cell surface comodulation of CD4 and T cell receptor by anti-CD4 monoclonal antibody. J. Immunol. 143: 397-402. (Pubitemid 19191528)
    • (1989) Journal of Immunology , vol.143 , Issue.2 , pp. 397-402
    • Cole, J.A.1    McCarthy, S.A.2    Rees, M.A.3    Sharrow, S.O.4    Singer, A.5
  • 9
    • 0029886827 scopus 로고    scopus 로고
    • HIV-1 envelope glycoprotein gp120 down-regulates CD4 expression in primary human macrophages through induction of endogenous tumour necrosis factor-α
    • Karsten, V., S. Gordon, A. Kirn, and G. Herbein. 1996. HIV-1 envelope glycoprotein gp120 down-regulates CD4 expression in primary human macrophages through induction of endogenous tumour necrosis factor-α. Immunology 88: 55-60. (Pubitemid 26166376)
    • (1996) Immunology , vol.88 , Issue.1 , pp. 55-60
    • Karsten, V.1    Gordon, S.2    Kirn, A.3    Herbein, G.4
  • 10
    • 0032567335 scopus 로고    scopus 로고
    • A novel mechanism of CD4 down-modulation induced by monosialoganglioside GM3: Involvement of serine phosphorylation and protein kinase Cδ translocation
    • Garofalo, T., M. Sorice, R. Misasi, B. Cinque, M. Giammatteo, G. M. Pontieri, M. G. Cifone, and A. Pavan. 1998. A novel mechanism of CD4 down-modulation induced by monosialoganglioside GM3: involvement of serine phosphorylation and protein kinase Cδ translocation. J. Biol. Chem. 273: 35153-35160.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35153-35160
    • Garofalo, T.1    Sorice, M.2    Misasi, R.3    Cinque, B.4    Giammatteo, M.5    Pontieri, G.M.6    Cifone, M.G.7    Pavan, A.8
  • 11
    • 0344286482 scopus 로고    scopus 로고
    • Cluster of differentiation antigen 4 (CD4) endocytosis and adaptor complex binding require activation of the CD4 endocytosis signal by serine phosphorylation
    • Pitcher, C., S. Höning, A. Fingerhut, K. Bowers, and M. Marsh. 1999. Cluster of differentiation antigen 4 (CD4) endocytosis and adaptor complex binding require activation of the CD4 endocytosis signal by serine phosphorylation. Mol. Biol. Cell 10: 677-691.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 677-691
    • Pitcher, C.1    Höning, S.2    Fingerhut, A.3    Bowers, K.4    Marsh, M.5
  • 12
    • 0029163314 scopus 로고
    • Phorbol ester-induced down modulation of tailless CD4 receptors requires prior binding of gp120 and suggests a role for accessory molecules
    • Golding, H., D. S. Dimitrov, J. Manischewitz, C. C. Broder, J. Robinson, S. Fabian, D. R. Littman, and C. K. Lapham. 1995. Phorbol ester-induced down modulation of tailless CD4 receptors requires prior binding of gp120 and suggests a role for accessory molecules. J. Virol. 69: 6140-6148.
    • (1995) J. Virol. , vol.69 , pp. 6140-6148
    • Golding, H.1    Dimitrov, D.S.2    Manischewitz, J.3    Broder, C.C.4    Robinson, J.5    Fabian, S.6    Littman, D.R.7    Lapham, C.K.8
  • 13
    • 0027321454 scopus 로고
    • Phorbol ester-induced downregulation of CD4 is a multistep process involving dissociation from p56lck, increased association with clathrin-coated pits, and altered endosomal sorting
    • Pelchen-Matthews, A., I. J. Parsons, and M. Marsh. 1993. Phorbol ester-induced downregulation of CD4 is a multistep process involving dissociation from p56lck, increased association with clathrin-coated pits, and altered endosomal sorting. J. Exp. Med. 178: 1209-1222.
    • (1993) J. Exp. Med. , vol.178 , pp. 1209-1222
    • Pelchen-Matthews, A.1    Parsons, I.J.2    Marsh, M.3
  • 14
    • 0023858345 scopus 로고
    • T4 endocytosis and phosphorylation induced by phorbol esters but not by mitogen or HIV infection
    • Hoxie, J. A., J. L. Rackowski, B. S. Haggarty, and G. N. Gaulton. 1988. T4 endocytosis and phosphorylation induced by phorbol esters but not by mitogen or HIV infection. J. Immunol. 140: 786-795.
    • (1988) J. Immunol. , vol.140 , pp. 786-795
    • Hoxie, J.A.1    Rackowski, J.L.2    Haggarty, B.S.3    Gaulton, G.N.4
  • 15
    • 0023036903 scopus 로고
    • Rapid phosphorylation and modulation of the T4 antigen on cloned helper T cells induced by phorbol myristate acetate or antigen
    • Acres, R. B., P. J. Conlon, D. Y. Mochizuki, and B. Gallis. 1986. Rapid phosphorylation and modulation of the T4 antigen on cloned helper T cells induced by phorbol myristate acetate or antigen. J. Biol. Chem. 261: 16210-16214.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16210-16214
    • Acres, R.B.1    Conlon, P.J.2    Mochizuki, D.Y.3    Gallis, B.4
  • 17
    • 0026032662 scopus 로고
    • Differential endocytosis of CD4 in lymphocytic and nonlymphocytic cells
    • Pelchen-Matthews, A., J. E. Armes, G. Griffiths, and M. Marsh. 1991. Differential endocytosis of CD4 in lymphocytic and nonlymphocytic cells. J. Exp. Med. 173: 575-587.
    • (1991) J. Exp. Med. , vol.173 , pp. 575-587
    • Pelchen-Matthews, A.1    Armes, J.E.2    Griffiths, G.3    Marsh, M.4
  • 18
    • 0344440968 scopus 로고    scopus 로고
    • + cell anti-HIV factor (CAF)
    • + cell anti-HIV factor (CAF). Trends Immunol. 24: 628-632.
    • (2003) Trends Immunol. , vol.24 , pp. 628-632
    • Levy, J.A.1
  • 19
    • 0028905265 scopus 로고
    • + T cells suppress human immunodeficiency virus replication by inhibiting viral transcription
    • + T cells suppress human immunodeficiency virus replication by inhibiting viral transcription. Proc. Natl. Acad. Sci. USA 92: 2308-2312.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2308-2312
    • Mackewicz, C.E.1    Blackbourn, D.J.2    Levy, J.A.3
  • 20
    • 0034062063 scopus 로고    scopus 로고
    • + cell noncytotoxic anti-human immunodeficiency virus response inhibits expression of viral RNA but not reverse transcription or provirus integration
    • + cell noncytotoxic anti-human immunodeficiency virus response inhibits expression of viral RNA but not reverse transcription or provirus integration. J. Gen. Virol. 81: 1261-1264.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1261-1264
    • Mackewicz, C.E.1    Patterson, B.K.2    Lee, S.A.3    Levy, J.A.4
  • 21
    • 0037097773 scopus 로고    scopus 로고
    • Inhibition of CXCR4-tropic HIV-1 infection by lipopolysaccharide: Evidence of different mechanisms in macrophages and T lymphocytes
    • Verani, A., F. Sironi, A. G. Siccardi, P. Lusso, and D. Vercelli. 2002. Inhibition of CXCR4-tropic HIV-1 infection by lipopolysaccharide: evidence of different mechanisms in macrophages and T lymphocytes. J. Immunol. 168: 6388-6395. (Pubitemid 34620063)
    • (2002) Journal of Immunology , vol.168 , Issue.12 , pp. 6388-6395
    • Verani, A.1    Sironi, F.2    Siccardi, A.G.3    Lusso, P.4    Vercelli, D.5
  • 22
    • 67649482340 scopus 로고    scopus 로고
    • Biological and physical characterization of the X4 HIV-1 suppressive factor secreted by LPS-stimulated human macrophages
    • Mikulak, J., M. Gianolini, P. Versmisse, G. Pancino, P. Lusso, and A. Verani. 2009. Biological and physical characterization of the X4 HIV-1 suppressive factor secreted by LPS-stimulated human macrophages. Virology 390: 37-44.
    • (2009) Virology , vol.390 , pp. 37-44
    • Mikulak, J.1    Gianolini, M.2    Versmisse, P.3    Pancino, G.4    Lusso, P.5    Verani, A.6
  • 23
    • 0029616489 scopus 로고
    • A resting cell assay for improved detection of antibody-mediated neutralization of HIV type 1 primary isolates
    • Zolla-Pazner, S., and S. Sharpe. 1995. A resting cell assay for improved detection of antibody-mediated neutralization of HIV type 1 primary isolates. AIDS Res. Hum. Retroviruses 11: 1449-1458.
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 1449-1458
    • Zolla-Pazner, S.1    Sharpe, S.2
  • 24
    • 33646712321 scopus 로고    scopus 로고
    • Macrophage activation and human immunodeficiency virus infection: HIV replication directs macrophages towards a pro-inflammatory phenotype while previous activation modulates macrophage susceptibility to infection and viral production
    • DOI 10.1016/j.virol.2006.02.031, PII S0042682206001346
    • Porcheray, F., B. Samah, C. Léone, N. Dereuddre-Bosquet, and G. Gras. 2006. Macrophage activation and human immunodeficiency virus infection: HIV replication directs macrophages towards a pro-inflammatory phenotype while previous activation modulates macrophage susceptibility to infection and viral production. Virology 349: 112-120. (Pubitemid 43732479)
    • (2006) Virology , vol.349 , Issue.1 , pp. 112-120
    • Porcheray, F.1    Samah, B.2    Leone, C.3    Dereuddre-Bosquet, N.4    Gras, G.5
  • 25
    • 84944282429 scopus 로고
    • Virus isolation from and identification of HTLV-III/LAV-producing cells in brain tissue from a patient with AIDS
    • DOI 10.1001/jama.256.17.2365
    • Gartner, S., P. Markovits, D. M. Markovitz, R. F. Betts, and M. Popovic. 1986. Virus isolation from and identification of HTLV-III/LAV - producing cells in brain tissue from a patient with AIDS. JAMA 256: 2365-2371. (Pubitemid 17174464)
    • (1986) Journal of the American Medical Association , vol.256 , Issue.17 , pp. 2365-2371
    • Gartner, S.1    Markovits, P.2    Markovitz, D.M.3
  • 26
    • 0035025888 scopus 로고    scopus 로고
    • A quantitative assay for HIV DNA integration in vivo
    • Butler, S. L., M. S. Hansen, and F. D. Bushman. 2001. A quantitative assay for HIV DNA integration in vivo. Nat. Med. 7: 631-634.
    • (2001) Nat. Med. , vol.7 , pp. 631-634
    • Butler, S.L.1    Hansen, M.S.2    Bushman, F.D.3
  • 27
    • 54049134705 scopus 로고    scopus 로고
    • An aptamer that neutralizes R5 strains of HIV-1 binds to core residues of gp120 in the CCR5 binding site
    • Cohen, C., M. Forzan, B. Sproat, R. Pantophlet, I. McGowan, D. Burton, and W. James. 2008. An aptamer that neutralizes R5 strains of HIV-1 binds to core residues of gp120 in the CCR5 binding site. Virology 381: 46-54.
    • (2008) Virology , vol.381 , pp. 46-54
    • Cohen, C.1    Forzan, M.2    Sproat, B.3    Pantophlet, R.4    McGowan, I.5    Burton, D.6    James, W.7
  • 29
    • 0030049410 scopus 로고    scopus 로고
    • Comparison of p24 measurement by ELISA versus indicator cells for detecting residual HIV infectivity in vitro
    • DOI 10.1016/0166-0934(96)02007-1
    • Herbein, G., P. Illei, L. J. Montaner, W. James, and S. Gordon. 1996. Comparison of p24 measurement by ELISA versus indicator cells for detecting residual HIV infectivity in vitro. J. Virol. Methods 58: 167-173. (Pubitemid 26000599)
    • (1996) Journal of Virological Methods , vol.58 , Issue.1-2 , pp. 167-173
    • Herbein, G.1    Illei, P.2    Montaner, L.J.3    James, W.4    Gordon, S.5
  • 30
    • 0033028054 scopus 로고    scopus 로고
    • Recombinant interleukin-16 selectively modulates surface receptor expression and cytokine release in macrophages and dendritic cells
    • Hermann, E., E. Darcissac, T. Idziorek, A. Capron, and G. M. Bahr. 1999. Recombinant interleukin-16 selectively modulates surface receptor expression and cytokine release in macrophages and dendritic cells. Immunology 97: 241-248.
    • (1999) Immunology , vol.97 , pp. 241-248
    • Hermann, E.1    Darcissac, E.2    Idziorek, T.3    Capron, A.4    Bahr, G.M.5
  • 32
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox, J., I. Matic, M. Hilger, N. Nagaraj, M. Selbach, J. V. Olsen, and M. Mann. 2009. A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4: 698-705.
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6    Mann, M.7
  • 33
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and M. Mann. 2008. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26: 1367-1372.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 34
    • 74049132731 scopus 로고    scopus 로고
    • Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis
    • Griffin, N. M., J. Yu, F. Long, P. Oh, S. Shore, Y. Li, J. A. Koziol, and J. E. Schnitzer. 2010. Label-free, normalized quantification of complex mass spectrometry data for proteomic analysis. Nat. Biotechnol. 28: 83-89.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 83-89
    • Griffin, N.M.1    Yu, J.2    Long, F.3    Oh, P.4    Shore, S.5    Li, Y.6    Koziol, J.A.7    Schnitzer, J.E.8
  • 37
    • 0034672211 scopus 로고    scopus 로고
    • Association of immunoproteasomes with the endoplasmic reticulum
    • Brooks, P., R. Z. Murray, G. G. Mason, K. B. Hendil, and A. J. Rivett. 2000. Association of immunoproteasomes with the endoplasmic reticulum. Biochem. J. 352: 611-615.
    • (2000) Biochem. J. , vol.352 , pp. 611-615
    • Brooks, P.1    Murray, R.Z.2    Mason, G.G.3    Hendil, K.B.4    Rivett, A.J.5
  • 38
    • 31944432777 scopus 로고    scopus 로고
    • Proteasome subunit LMP2 is required for matrix metalloproteinase-2 and -9 expression and activities in human invasive extravillous trophoblast cell line
    • Wang, H. X., H. M. Wang, H. Y. Lin, Q. Yang, H. Zhang, B. K. Tsang, and C. Zhu. 2006. Proteasome subunit LMP2 is required for matrix metalloproteinase-2 and -9 expression and activities in human invasive extravillous trophoblast cell line. J. Cell. Physiol. 206: 616-623.
    • (2006) J. Cell. Physiol. , vol.206 , pp. 616-623
    • Wang, H.X.1    Wang, H.M.2    Lin, H.Y.3    Yang, Q.4    Zhang, H.5    Tsang, B.K.6    Zhu, C.7
  • 39
    • 0028927841 scopus 로고
    • Coordinate regulation of the human TAP1 and LMP2 genes from a shared bidirectional promoter
    • Wright, K. L., L. C. White, A. Kelly, S. Beck, J. Trowsdale, and J. P. Ting. 1995. Coordinate regulation of the human TAP1 and LMP2 genes from a shared bidirectional promoter. J. Exp. Med. 181: 1459-1471.
    • (1995) J. Exp. Med. , vol.181 , pp. 1459-1471
    • Wright, K.L.1    White, L.C.2    Kelly, A.3    Beck, S.4    Trowsdale, J.5    Ting, J.P.6
  • 40
    • 0036721164 scopus 로고    scopus 로고
    • Bay 11-7082 inhibits transcription factor NF-κB and induces apoptosis of HTVL-I-infected T-cell lines and primary adult T-cell leukemia cells
    • DOI 10.1182/blood-2002-01-0151
    • Mori, N., Y. Yamada, S. Ikeda, Y. Yamasaki, K. Tsukasaki, Y. Tanaka, M. Tomonaga, N. Yamamoto, and M. Fujii. 2002. Bay 11-7082 inhibits transcription factor NF-κB and induces apoptosis of HTLV-I - infected T-cell lines and primary adult T-cell leukemia cells. Blood 100: 1828-1834. (Pubitemid 34925163)
    • (2002) Blood , vol.100 , Issue.5 , pp. 1828-1834
    • Mori, N.1    Yamada, Y.2    Ikeda, S.3    Yamasaki, Y.4    Tsukasaki, K.5    Tanaka, Y.6    Tomonaga, M.7    Yamamoto, N.8    Fujii, M.9
  • 41
    • 0023922690 scopus 로고
    • Human immunodeficiency virus induces phosphorylation of its cell surface receptor
    • Fields, A. P., D. P. Bednarik, A. Hess, and W. S. May. 1988. Human immunodeficiency virus induces phosphorylation of its cell surface receptor. Nature 333: 278-280.
    • (1988) Nature , vol.333 , pp. 278-280
    • Fields, A.P.1    Bednarik, D.P.2    Hess, A.3    May, W.S.4
  • 42
    • 0024427545 scopus 로고
    • Variations in CD4 expression by human monocytes and macrophages and their relationships to infection with the human immunodeficiency virus
    • Kazazi, F., J.-M. Mathijs, P. Foley, and A. L. Cunningham. 1989. Variations in CD4 expression by human monocytes and macrophages and their relationships to infection with the human immunodeficiency virus. J. Gen. Virol. 70: 2661-2672.
    • (1989) J. Gen. Virol. , vol.70 , pp. 2661-2672
    • Kazazi, F.1    Mathijs, J.-M.2    Foley, P.3    Cunningham, A.L.4
  • 43
    • 0025779089 scopus 로고
    • Phosphorylation-dependent down-modulation of CD4 requires a specific structure within the cytoplasmic domain of CD4
    • Shin, J., R. L. Dunbrack, Jr., S. Lee, and J. L. Strominger. 1991. Phosphorylation-dependent down-modulation of CD4 requires a specific structure within the cytoplasmic domain of CD4. J. Biol. Chem. 266: 10658-10665.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10658-10665
    • Shin, J.1    Dunbrack Jr., R.L.2    Lee, S.3    Strominger, J.L.4
  • 44
    • 0025089942 scopus 로고
    • Structural features of the cytoplasmic region of CD4 required for internalization
    • Shin, J., C. Doyle, Z. Yang, D. Kappes, and J. L. Strominger. 1990. Structural features of the cytoplasmic region of CD4 required for internalization. EMBO J. 9: 425-434.
    • (1990) EMBO J. , vol.9 , pp. 425-434
    • Shin, J.1    Doyle, C.2    Yang, Z.3    Kappes, D.4    Strominger, J.L.5
  • 45
    • 0027336298 scopus 로고
    • Gö6976, a selective inhibitor of protein kinase C, is a potent antagonist of human immunodeficiency virus 1 induction from latent/low-level - Producing reservoir cells in vitro
    • Qatsha, K. A., C. Rudolph, D. Marmé, C. Schächtele, and W. S. May. 1993. Gö6976, a selective inhibitor of protein kinase C, is a potent antagonist of human immunodeficiency virus 1 induction from latent/low-level - producing reservoir cells in vitro. Proc. Natl. Acad. Sci. USA 90: 4674-4678.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4674-4678
    • Qatsha, K.A.1    Rudolph, C.2    Marmé, D.3    Schächtele, C.4    May, W.S.5
  • 47
    • 67650152516 scopus 로고    scopus 로고
    • M1 and M2a polarization of human monocyte-derived macrophages inhibits HIV-1 replication by distinct mechanisms
    • Cassol, E., L. Cassetta, C. Rizzi, M. Alfano, and G. Poli. 2009. M1 and M2a polarization of human monocyte-derived macrophages inhibits HIV-1 replication by distinct mechanisms. J. Immunol. 182: 6237-6246.
    • (2009) J. Immunol. , vol.182 , pp. 6237-6246
    • Cassol, E.1    Cassetta, L.2    Rizzi, C.3    Alfano, M.4    Poli, G.5
  • 48
    • 48849086000 scopus 로고    scopus 로고
    • The ProteoMiner and the FortyNiners: Searching for gold nuggets in the proteomic arena
    • Righetti, P. G., and E. Boschetti. 2008. The ProteoMiner and the FortyNiners: searching for gold nuggets in the proteomic arena. Mass Spectrom. Rev. 27: 596-608.
    • (2008) Mass Spectrom. Rev. , vol.27 , pp. 596-608
    • Righetti, P.G.1    Boschetti, E.2
  • 49
    • 48849098966 scopus 로고    scopus 로고
    • The ProteoMiner in the proteomic arena: A non-depleting tool for discovering low-abundance species
    • Boschetti, E., and P. G. Righetti. 2008. The ProteoMiner in the proteomic arena: a non-depleting tool for discovering low-abundance species. J. Proteomics 71: 255-264.
    • (2008) J. Proteomics , vol.71 , pp. 255-264
    • Boschetti, E.1    Righetti, P.G.2
  • 52
    • 0034470259 scopus 로고    scopus 로고
    • Attractin: A cub-family protease involved in T cell-monocyte/macrophage interactions
    • Duke-Cohan, J. S., W. Tang, and S. F. Schlossman. 2000. Attractin: a cub-family protease involved in T cell-monocyte/macrophage interactions. Adv. Exp. Med. Biol. 477: 173-185.
    • (2000) Adv. Exp. Med. Biol. , vol.477 , pp. 173-185
    • Duke-Cohan, J.S.1    Tang, W.2    Schlossman, S.F.3
  • 54
    • 0032530558 scopus 로고    scopus 로고
    • Attractin (DPPT-L), a member of the CUB family of cell adhesion and guidance proteins, is secreted by activated human T lymphocytes and modulates immune cell interactions
    • Duke-Cohan, J. S., J. Gu, D. F. McLaughlin, Y. Xu, G. J. Freeman, and S. F. Schlossman. 1998. Attractin (DPPT-L), a member of the CUB family of cell adhesion and guidance proteins, is secreted by activated human T lymphocytes and modulates immune cell interactions. Proc. Natl. Acad. Sci. USA 95: 11336-11341.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11336-11341
    • Duke-Cohan, J.S.1    Gu, J.2    McLaughlin, D.F.3    Xu, Y.4    Freeman, G.J.5    Schlossman, S.F.6
  • 55
    • 0032536822 scopus 로고    scopus 로고
    • Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds b1 integrins, collagens and fibronectin
    • DOI 10.1093/emboj/17.6.1606
    • Sasaki, T., C. Brakebusch, J. Engel, and R. Timpl. 1998. Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds b1 integrins, collagens and fibronectin. EMBO J. 17: 1606-1613. (Pubitemid 28119114)
    • (1998) EMBO Journal , vol.17 , Issue.6 , pp. 1606-1613
    • Sasaki, T.1    Brakebusch, C.2    Engel, J.3    Timpl, R.4
  • 57
    • 0025292792 scopus 로고
    • T cell fibronectin: An unexpected inflammatory lymphokine
    • Godfrey, H. P. 1990. T cell fibronectin: an unexpected inflammatory lymphokine. Lymphokine Res. 9: 435-447. (Pubitemid 20240115)
    • (1990) Lymphokine Research , vol.9 , Issue.3 , pp. 435-447
    • Godfrey, H.P.1
  • 58
    • 79954594132 scopus 로고    scopus 로고
    • Proteomic-based identification of CD4-interacting proteins in human primary macrophages
    • Raposo, R. A. S., B. Thomas, G. Ridlova, and W. James. 2011. Proteomic-based identification of CD4-interacting proteins in human primary macrophages. PLoS One 6: e18690.
    • (2011) PLoS One , vol.6
    • Raposo, R.A.S.1    Thomas, B.2    Ridlova, G.3    James, W.4
  • 59
    • 0026654595 scopus 로고
    • Internalization, lysosomal degradation and new synthesis of surface membrane CD4 in phorbol ester-activated T-lymphocytes and U-937 cells
    • Petersen, C. M., E. I. Christensen, B. S. Andresen, and B. K. Møller. 1992. Internalization, lysosomal degradation and new synthesis of surface membrane CD4 in phorbol ester-activated T-lymphocytes and U-937 cells. Exp. Cell Res. 201: 160-173.
    • (1992) Exp. Cell Res. , vol.201 , pp. 160-173
    • Petersen, C.M.1    Christensen, E.I.2    Andresen, B.S.3    Møller, B.K.4
  • 60
    • 0347986633 scopus 로고    scopus 로고
    • Emerging and diverse roles of protein kinase C in immune cell signalling
    • Tan, S. L., and P. J. Parker. 2003. Emerging and diverse roles of protein kinase C in immune cell signalling. Biochem. J. 376: 545-552.
    • (2003) Biochem. J. , vol.376 , pp. 545-552
    • Tan, S.L.1    Parker, P.J.2
  • 61
    • 0028911139 scopus 로고
    • Analysis of the role of protein kinase C-α, -ε, and -ζ in T cell activation
    • Genot, E. M., P. J. Parker, and D. A. Cantrell. 1995. Analysis of the role of protein kinase C-α, -ε, and -ζ in T cell activation. J. Biol. Chem. 270: 9833-9839.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9833-9839
    • Genot, E.M.1    Parker, P.J.2    Cantrell, D.A.3
  • 62
    • 4444245423 scopus 로고    scopus 로고
    • Protein kinase C and beyond
    • Spitaler, M., and D. A. Cantrell. 2004. Protein kinase C and beyond. Nat. Immunol. 5: 785-790.
    • (2004) Nat. Immunol. , vol.5 , pp. 785-790
    • Spitaler, M.1    Cantrell, D.A.2
  • 63
    • 0037124307 scopus 로고    scopus 로고
    • Protein kinase Cβ controls nuclear factor κB activation in B cells through selective regulation of the IkB kinase a
    • Saijo, K., I. Mecklenbräuker, A. Santana, M. Leitger, C. Schmedt, and A. Tarakhovsky. 2002. Protein kinase Cβ controls nuclear factor κB activation in B cells through selective regulation of the IkB kinase a. J. Exp. Med. 195: 1647-1652.
    • (2002) J. Exp. Med. , vol.195 , pp. 1647-1652
    • Saijo, K.1    Mecklenbräuker, I.2    Santana, A.3    Leitger, M.4    Schmedt, C.5    Tarakhovsky, A.6
  • 66
    • 0030053057 scopus 로고    scopus 로고
    • Serum high molecular weight dipeptidyl peptidase IV (CD26) is similar to a novel antigen DPPT-L released from activated T cells
    • Duke-Cohan, J. S., C. Morimoto, J. A. Rocker, and S. F. Schlossman. 1996. Serum high molecular weight dipeptidyl peptidase IV (CD26) is similar to a novel antigen DPPT-L released from activated T cells. J. Immunol. 156: 1714-1721.
    • (1996) J. Immunol. , vol.156 , pp. 1714-1721
    • Duke-Cohan, J.S.1    Morimoto, C.2    Rocker, J.A.3    Schlossman, S.F.4
  • 67
    • 1642315558 scopus 로고    scopus 로고
    • The intricate interface between immune system and metabolism
    • DOI 10.1016/j.it.2004.02.009, PII S1471490604000596
    • Matarese, G., and A. La Cava. 2004. The intricate interface between immune system and metabolism. Trends Immunol. 25: 193-200. (Pubitemid 38368167)
    • (2004) Trends in Immunology , vol.25 , Issue.4 , pp. 193-200
    • Matarese, G.1    La, C.A.2
  • 68
    • 16344377897 scopus 로고    scopus 로고
    • Fibronectin on activated T lymphocytes is bound to gangliosides and is present in detergent insoluble microdomains
    • Blum, S., F. Hug, G. M. Hänsch, and C. Wagner. 2005. Fibronectin on activated T lymphocytes is bound to gangliosides and is present in detergent insoluble microdomains. Immunol. Cell Biol. 83: 167-174.
    • (2005) Immunol. Cell Biol. , vol.83 , pp. 167-174
    • Blum, S.1    Hug, F.2    Hänsch, G.M.3    Wagner, C.4
  • 71
    • 0036141244 scopus 로고    scopus 로고
    • Human macrophage adhesion on fibronectin: The role of substratum and intracellular signalling kinases
    • Liu, Y., and W. J. Kao. 2002. Human macrophage adhesion on fibronectin: the role of substratum and intracellular signalling kinases. Cell. Signal. 14: 145-152.
    • (2002) Cell. Signal. , vol.14 , pp. 145-152
    • Liu, Y.1    Kao, W.J.2
  • 72
    • 0030845282 scopus 로고    scopus 로고
    • Dissection of pathways implicated in integrin-mediated actin cytoskeleton assembly. Involvement of protein kinase C, Rho GTPase, and tyrosine phosphorylation
    • Defilippi, P., M. Venturino, D. Gulino, A. Duperray, P. Boquet, C. Fiorentini, G. Volpe, M. Palmieri, L. Silengo, and G. Tarone. 1997. Dissection of pathways implicated in integrin-mediated actin cytoskeleton assembly. Involvement of protein kinase C, Rho GTPase, and tyrosine phosphorylation. J. Biol. Chem. 272: 21726-21734.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21726-21734
    • Defilippi, P.1    Venturino, M.2    Gulino, D.3    Duperray, A.4    Boquet, P.5    Fiorentini, C.6    Volpe, G.7    Palmieri, M.8    Silengo, L.9    Tarone, G.10
  • 73
    • 0031696891 scopus 로고    scopus 로고
    • The integrin avb6 is critical for keratinocyte migration on both its known ligand, fibronectin, and on vitronectin
    • Huang, X., J. Wu, S. Spong, and D. Sheppard. 1998. The integrin avb6 is critical for keratinocyte migration on both its known ligand, fibronectin, and on vitronectin. J. Cell Sci. 111: 2189-2195. (Pubitemid 28403697)
    • (1998) Journal of Cell Science , vol.111 , Issue.15 , pp. 2189-2195
    • Huanq, X.1    Wu, J.2    Spong, S.3    Sheppard, D.4
  • 74
    • 0029759727 scopus 로고    scopus 로고
    • vβ5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation
    • vβ5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation. J. Cell Biol. 134: 1323-1332.
    • (1996) J. Cell Biol. , vol.134 , pp. 1323-1332
    • Lewis, J.M.1    Cheresh, D.A.2    Schwartz, M.A.3
  • 75
    • 0027585507 scopus 로고
    • Effect of a-protein kinase C neutralizing antibodies and the pseudosubstrate peptide on phosphorylation, migration, and growth of REF52 cells
    • Liao, L., and S. Jaken. 1993. Effect of a-protein kinase C neutralizing antibodies and the pseudosubstrate peptide on phosphorylation, migration, and growth of REF52 cells. Cell Growth Differ. 4: 309-316.
    • (1993) Cell Growth Differ. , vol.4 , pp. 309-316
    • Liao, L.1    Jaken, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.