메뉴 건너뛰기




Volumn 23, Issue 6, 2016, Pages 962-978

Phosphatidylserine is a global immunosuppressive signal in efferocytosis, infectious disease, and cancer

Author keywords

[No Author keywords available]

Indexed keywords

LIPOCORTIN 5; MONOCLONAL ANTIBODY; OPSONIN; PHOSPHATIDYLSERINE; PLASMA PROTEIN; PROTEIN; SCRAMBLASE; ANTIBODY; APOPTOSIS REGULATORY PROTEIN; CELL SURFACE RECEPTOR; MEMBRANE PROTEIN; PHOSPHATIDYLSERINE RECEPTOR;

EID: 84959222190     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2016.11     Document Type: Review
Times cited : (506)

References (135)
  • 1
    • 77952944942 scopus 로고    scopus 로고
    • The distribution and function of phosphatidylserine in cellular membranes
    • Leventis PA, Grinstein S. The distribution and function of phosphatidylserine in cellular membranes. Annu Rev Biophys 2010; 39: 407-427
    • (2010) Annu Rev Biophys , vol.39 , pp. 407-427
    • Leventis, P.A.1    Grinstein, S.2
  • 2
    • 0021828779 scopus 로고
    • In vivo recognition and clearance of red blood cells containing phosphatidylserine in their plasma membranes
    • Schroit AJ, Madsen JW, Tanaka Y. In vivo recognition and clearance of red blood cells containing phosphatidylserine in their plasma membranes. J Biol Chem 1985; 260: 5131-5138
    • (1985) J Biol Chem , vol.260 , pp. 5131-5138
    • Schroit, A.J.1    Madsen, J.W.2    Tanaka, Y.3
  • 4
    • 0034602158 scopus 로고    scopus 로고
    • Phosphatidylserine synthase-1 and -2 are localized to mitochondriaassociated membranes
    • Stone SJ, Vance JE. Phosphatidylserine synthase-1 and -2 are localized to mitochondriaassociated membranes. J Biol Chem 2000; 275: 34534-34540
    • (2000) J Biol Chem , vol.275 , pp. 34534-34540
    • Stone, S.J.1    Vance, J.E.2
  • 5
    • 45149090469 scopus 로고    scopus 로고
    • Defining the importance of phosphatidylserine synthase-1 (PSS1): Unexpected viability of PSS1-deficient mice
    • Arikketh D, Nelson R, Vance JE. Defining the importance of phosphatidylserine synthase-1 (PSS1): unexpected viability of PSS1-deficient mice. J Biol Chem 2008; 283: 12888-12897
    • (2008) J Biol Chem , vol.283 , pp. 12888-12897
    • Arikketh, D.1    Nelson, R.2    Vance, J.E.3
  • 6
    • 84885006979 scopus 로고    scopus 로고
    • Phosphatidylserine-mediated cellular signaling
    • Kay JG, Grinstein S. Phosphatidylserine-mediated cellular signaling. Adv Exp Med Biol 2013; 991: 177-193
    • (2013) Adv Exp Med Biol , vol.991 , pp. 177-193
    • Kay, J.G.1    Grinstein, S.2
  • 7
    • 0019487669 scopus 로고
    • Characterization of phosphatidylserine synthase from Saccharomyces cerevisiae and a mutant defective in the enzyme
    • Nikawa JI, Yamashita S. Characterization of phosphatidylserine synthase from Saccharomyces cerevisiae and a mutant defective in the enzyme. Biochim Biophys Acta 1981; 665: 420-426
    • (1981) Biochim Biophys Acta , vol.665 , pp. 420-426
    • Nikawa, J.I.1    Yamashita, S.2
  • 8
    • 84891373792 scopus 로고    scopus 로고
    • Gain-of-function mutations in the phosphatidylserine synthase 1 (PTDSS1) gene cause Lenz-Majewski syndrome
    • Sousa SB, Jenkins D, Chanudet E, Tasseva G, Ishida M, Anderson G., et al. Gain-of-function mutations in the phosphatidylserine synthase 1 (PTDSS1) gene cause Lenz-Majewski syndrome. Nat Genet 2014; 46: 70-76
    • (2014) Nat Genet , vol.46 , pp. 70-76
    • Sousa, S.B.1    Jenkins, D.2    Chanudet, E.3    Tasseva, G.4    Ishida, M.5    Anderson, G.6
  • 9
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon M.A. Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 2008; 9: 99-111
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 10
    • 0020052831 scopus 로고
    • Generation of prothrombinconverting activity and the exposure of phosphatidylserine at the outer surface of platelets
    • Bevers EM, Comfurius P, Van Rijn JL, Hemker HC, Zwaal RF. Generation of prothrombinconverting activity and the exposure of phosphatidylserine at the outer surface of platelets. Eur J Biochem 1982; 122: 429-436
    • (1982) Eur J Biochem , vol.122 , pp. 429-436
    • Bevers, E.M.1    Comfurius, P.2    Van Rijn, J.L.3    Hemker, H.C.4    Zwaal, R.F.5
  • 11
    • 13544276524 scopus 로고    scopus 로고
    • Viable, apoptotic and necrotic monocytes expose phosphatidylserine: Cooperative binding of the ligand Annexin v to dying but not viable cells and implications for PS-dependent clearance
    • Appelt U, Sheriff A, Gaipl US, Kalden JR, Voll RE, Herrmann M. Viable, apoptotic and necrotic monocytes expose phosphatidylserine: cooperative binding of the ligand Annexin V to dying but not viable cells and implications for PS-dependent clearance. Cell Death Differ 2005; 12: 194-196
    • (2005) Cell Death Differ , vol.12 , pp. 194-196
    • Appelt, U.1    Sheriff, A.2    Gaipl, U.S.3    Kalden, J.R.4    Voll, R.E.5    Herrmann, M.6
  • 12
    • 0033937485 scopus 로고    scopus 로고
    • Surface expression of phosphatidylserine on macrophages is required for phagocytosis of apoptotic thymocytes
    • Callahan MK, Williamson P, Schlegel RA. Surface expression of phosphatidylserine on macrophages is required for phagocytosis of apoptotic thymocytes. Cell Death Differ 2000; 7: 645-653
    • (2000) Cell Death Differ , vol.7 , pp. 645-653
    • Callahan, M.K.1    Williamson, P.2    Schlegel, R.A.3
  • 14
    • 26944463126 scopus 로고    scopus 로고
    • Phosphatidylserinedependent engulfment by macrophages of nuclei from erythroid precursor cells
    • Yoshida H, Kawane K, Koike M, Mori Y, Uchiyama Y, Nagata S. Phosphatidylserinedependent engulfment by macrophages of nuclei from erythroid precursor cells. Nature 2005; 437: 754-758
    • (2005) Nature , vol.437 , pp. 754-758
    • Yoshida, H.1    Kawane, K.2    Koike, M.3    Mori, Y.4    Uchiyama, Y.5    Nagata, S.6
  • 15
    • 0034142375 scopus 로고    scopus 로고
    • Annexin v binds to viable B cells and colocalizes with a marker of lipid rafts upon B cell receptor activation
    • Dillon SR, Mancini M, Rosen A, Schlissel MS. Annexin V binds to viable B cells and colocalizes with a marker of lipid rafts upon B cell receptor activation. J Immunol 2000; 164: 1322-1332
    • (2000) J Immunol , vol.164 , pp. 1322-1332
    • Dillon, S.R.1    Mancini, M.2    Rosen, A.3    Schlissel, M.S.4
  • 16
    • 0025743796 scopus 로고
    • Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes
    • Utsugi T, Schroit AJ, Connor J, Bucana CD, Fidler IJ. Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes. Cancer Res 1991; 51: 3062-3066
    • (1991) Cancer Res , vol.51 , pp. 3062-3066
    • Utsugi, T.1    Schroit, A.J.2    Connor, J.3    Bucana, C.D.4    Fidler, I.J.5
  • 17
    • 27744528518 scopus 로고    scopus 로고
    • Cancer cell immune escape and tumor progression by exploitation of anti-inflammatory and pro-inflammatory responses
    • Kim R, Emi M, Tanabe K. Cancer cell immune escape and tumor progression by exploitation of anti-inflammatory and pro-inflammatory responses. Cancer Biol Ther 2005; 4: 924-933
    • (2005) Cancer Biol Ther , vol.4 , pp. 924-933
    • Kim, R.1    Emi, M.2    Tanabe, K.3
  • 18
    • 85028098813 scopus 로고    scopus 로고
    • Exosomes/microvesicles: Mediators of cancer-Associated immunosuppressive microenvironments
    • Taylor DD, Gercel-Taylor C. Exosomes/microvesicles: mediators of cancer-Associated immunosuppressive microenvironments. Semin Immunopathol 2011; 33: 441-454
    • (2011) Semin Immunopathol , vol.33 , pp. 441-454
    • Taylor, D.D.1    Gercel-Taylor, C.2
  • 19
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • Suzuki J, Umeda M, Sims PJ, Nagata S. Calcium-dependent phospholipid scrambling by TMEM16F. Nature 2010; 468: 834-838
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 20
    • 84880758440 scopus 로고    scopus 로고
    • Xk-related protein 8 and CED-8 promote phosphatidylserine exposure in apoptotic cells
    • Suzuki J, Denning DP, Imanishi E, Horvitz HR, Nagata S. Xk-related protein 8 and CED-8 promote phosphatidylserine exposure in apoptotic cells. Science 2013; 341: 403-406
    • (2013) Science , vol.341 , pp. 403-406
    • Suzuki, J.1    Denning, D.P.2    Imanishi, E.3    Horvitz, H.R.4    Nagata, S.5
  • 21
    • 84871860558 scopus 로고    scopus 로고
    • TMEM16F forms a Ca2+-Activated cation channel required for lipid scrambling in platelets during blood coagulation
    • Yang H, Kim A, David T, Palmer D, Jin T, Tien J., et al. TMEM16F forms a Ca2+-Activated cation channel required for lipid scrambling in platelets during blood coagulation. Cell 2012; 151: 111-122
    • (2012) Cell , vol.151 , pp. 111-122
    • Yang, H.1    Kim, A.2    David, T.3    Palmer, D.4    Jin, T.5    Tien, J.6
  • 22
    • 84877709762 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members
    • Suzuki J, Fujii T, Imao T, Ishihara K, Kuba H, Nagata S. Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members. J Biol Chem 2013; 288: 13305-13316
    • (2013) J Biol Chem , vol.288 , pp. 13305-13316
    • Suzuki, J.1    Fujii, T.2    Imao, T.3    Ishihara, K.4    Kuba, H.5    Nagata, S.6
  • 23
    • 0033680282 scopus 로고    scopus 로고
    • The ced-8 gene controls the timing of programmed cell deaths in C elegans
    • Stanfield GM, Horvitz HR. The ced-8 gene controls the timing of programmed cell deaths in C. elegans. Mol Cell 2000; 5: 423-433
    • (2000) Mol Cell , vol.5 , pp. 423-433
    • Stanfield, G.M.1    Horvitz, H.R.2
  • 24
    • 84908638686 scopus 로고    scopus 로고
    • Exposure of phosphatidylserine by Xk-related protein family members during apoptosis
    • Suzuki J, Imanishi E, Nagata S. Exposure of phosphatidylserine by Xk-related protein family members during apoptosis. J Biol Chem 2014; 289: 30257-30267
    • (2014) J Biol Chem , vol.289 , pp. 30257-30267
    • Suzuki, J.1    Imanishi, E.2    Nagata, S.3
  • 25
    • 82755163551 scopus 로고    scopus 로고
    • Constitutive exposure of phosphatidylserine on viable cells
    • Segawa K, Suzuki J, Nagata S. Constitutive exposure of phosphatidylserine on viable cells. Proc Natl Acad Sci USA 2011; 108: 19246-19251
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 19246-19251
    • Segawa, K.1    Suzuki, J.2    Nagata, S.3
  • 26
    • 84901849205 scopus 로고    scopus 로고
    • Caspasemediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure
    • Segawa K, Kurata S, Yanagihashi Y, Brummelkamp TR, Matsuda F, Nagata S. Caspasemediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure. Science 2014; 344: 1164-1168
    • (2014) Science , vol.344 , pp. 1164-1168
    • Segawa, K.1    Kurata, S.2    Yanagihashi, Y.3    Brummelkamp, T.R.4    Matsuda, F.5    Nagata, S.6
  • 27
    • 4544231736 scopus 로고    scopus 로고
    • The molecular arrangement of membrane-bound annexin A2-S100A10 tetramer as revealed by scanning force microscopy
    • Menke M, Ross M, Gerke V, Steinem C. The molecular arrangement of membrane-bound annexin A2-S100A10 tetramer as revealed by scanning force microscopy. Chembiochem 2004; 5: 1003-1006
    • (2004) Chembiochem , vol.5 , pp. 1003-1006
    • Menke, M.1    Ross, M.2    Gerke, V.3    Steinem, C.4
  • 28
    • 0033927556 scopus 로고    scopus 로고
    • Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- And tumor necrosis factor receptor-mediated apoptosis
    • Stegh AH, Herrmann H, Lampel S, Weisenberger D, Andra K, Seper M., et al. Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- And tumor necrosis factor receptor-mediated apoptosis. Mol Cell Biol 2000; 20: 5665-5679
    • (2000) Mol Cell Biol , vol.20 , pp. 5665-5679
    • Stegh, A.H.1    Herrmann, H.2    Lampel, S.3    Weisenberger, D.4    Andra, K.5    Seper, M.6
  • 29
    • 11144223256 scopus 로고    scopus 로고
    • Distinct localization of lipid rafts and externalized phosphatidylserine at the surface of apoptotic cells
    • Ishii H, Mori T, Shiratsuchi A, Nakai Y, Shimada Y, Ohno-Iwashita Y., et al. Distinct localization of lipid rafts and externalized phosphatidylserine at the surface of apoptotic cells. Biochem Biophys Res Commun 2005; 327: 94-99
    • (2005) Biochem Biophys Res Commun , vol.327 , pp. 94-99
    • Ishii, H.1    Mori, T.2    Shiratsuchi, A.3    Nakai, Y.4    Shimada, Y.5    Ohno-Iwashita, Y.6
  • 30
    • 84938406332 scopus 로고    scopus 로고
    • The AXL receptor is a sensor of ligand spatial heterogeneity
    • Meyer AS, Zweemer AJ, Lauffenburger DA. The AXL receptor is a sensor of ligand spatial heterogeneity. Cell Syst 2015; 1: 25-36
    • (2015) Cell Syst , vol.1 , pp. 25-36
    • Meyer, A.S.1    Zweemer, A.J.2    Lauffenburger, D.A.3
  • 31
    • 0033776534 scopus 로고    scopus 로고
    • ABC1 promotes engulfment of apoptotic cells and transbilayer redistribution of phosphatidylserine
    • Hamon Y, Broccardo C, Chambenoit O, Luciani MF, Toti F, Chaslin S., et al. ABC1 promotes engulfment of apoptotic cells and transbilayer redistribution of phosphatidylserine. Nat Cell Biol 2000; 2: 399-406
    • (2000) Nat Cell Biol , vol.2 , pp. 399-406
    • Hamon, Y.1    Broccardo, C.2    Chambenoit, O.3    Luciani, M.F.4    Toti, F.5    Chaslin, S.6
  • 32
    • 84870997563 scopus 로고    scopus 로고
    • Phosphatidylserine exposure during apoptosis reflects bidirectional trafficking between plasma membrane and cytoplasm
    • Lee SH, Meng XW, Flatten KS, Loegering DA, Kaufmann SH. Phosphatidylserine exposure during apoptosis reflects bidirectional trafficking between plasma membrane and cytoplasm. Cell Death Differ 2013; 20: 64-76
    • (2013) Cell Death Differ , vol.20 , pp. 64-76
    • Lee, S.H.1    Meng, X.W.2    Flatten, K.S.3    Loegering, D.A.4    Kaufmann, S.H.5
  • 33
    • 79952074327 scopus 로고    scopus 로고
    • Sensing phosphatidylserine in cellular membranes
    • Kay JG, Grinstein S. Sensing phosphatidylserine in cellular membranes. Sensors (Basel) 2011 11 1744-1755
    • (2011) Sensors (Basel) , vol.11 , pp. 1744-1755
    • Kay, J.G.1    Grinstein, S.2
  • 34
    • 84898053295 scopus 로고    scopus 로고
    • Oxidatively modified phosphatidylserines on the surface of apoptotic cells are essential phagocytic 'eat-me' signals: Cleavage and inhibition of phagocytosis by Lp-PLA2
    • Tyurin VA, Balasubramanian K, Winnica D, Tyurina YY, Vikulina AS, He RR., et al. Oxidatively modified phosphatidylserines on the surface of apoptotic cells are essential phagocytic 'eat-me' signals: cleavage and inhibition of phagocytosis by Lp-PLA2. Cell Death Differ 2014; 21: 825-835
    • (2014) Cell Death Differ , vol.21 , pp. 825-835
    • Tyurin, V.A.1    Balasubramanian, K.2    Winnica, D.3    Tyurina, Y.Y.4    Vikulina, A.S.5    He, R.R.6
  • 35
    • 12344303128 scopus 로고    scopus 로고
    • Cytochrome c release is required for phosphatidylserine peroxidation during Fas-triggered apoptosis in lung epithelial A549 cells
    • Jiang J, Kini V, Belikova N, Serinkan BF, Borisenko GG, Tyurina YY., et al. Cytochrome c release is required for phosphatidylserine peroxidation during Fas-triggered apoptosis in lung epithelial A549 cells. Lipids 2004; 39: 1133-1142
    • (2004) Lipids , vol.39 , pp. 1133-1142
    • Jiang, J.1    Kini, V.2    Belikova, N.3    Serinkan, B.F.4    Borisenko, G.G.5    Tyurina, Y.Y.6
  • 36
  • 38
    • 0036164008 scopus 로고    scopus 로고
    • Impaired uptake of apoptotic cells into tingible body macrophages in germinal centers of patients with systemic lupus erythematosus
    • Baumann I, Kolowos W, Voll RE, Manger B, Gaipl U, Neuhuber WL., et al. Impaired uptake of apoptotic cells into tingible body macrophages in germinal centers of patients with systemic lupus erythematosus. Arthritis Rheum 2002; 46: 191-201
    • (2002) Arthritis Rheum , vol.46 , pp. 191-201
    • Baumann, I.1    Kolowos, W.2    Voll, R.E.3    Manger, B.4    Gaipl, U.5    Neuhuber, W.L.6
  • 39
    • 0142072318 scopus 로고    scopus 로고
    • Increased apoptotic neutrophils and macrophages and impaired macrophage phagocytic clearance of apoptotic neutrophils in systemic lupus erythematosus
    • Ren Y, Tang J, Mok MY, Chan AW, Wu A, Lau CS. Increased apoptotic neutrophils and macrophages and impaired macrophage phagocytic clearance of apoptotic neutrophils in systemic lupus erythematosus. Arthritis Rheum 2003; 48: 2888-2897
    • (2003) Arthritis Rheum , vol.48 , pp. 2888-2897
    • Ren, Y.1    Tang, J.2    Mok, M.Y.3    Chan, A.W.4    Wu, A.5    Lau, C.S.6
  • 41
    • 80755180853 scopus 로고    scopus 로고
    • Beginnings of a good apoptotic meal: The find-me and eat-me signaling pathways
    • Ravichandran KS. Beginnings of a good apoptotic meal: the find-me and eat-me signaling pathways. Immunity 2011; 35: 445-455
    • (2011) Immunity , vol.35 , pp. 445-455
    • Ravichandran, K.S.1
  • 43
    • 77956941695 scopus 로고    scopus 로고
    • Decrease of sialic acid residues as an eat-me signal on the surface of apoptotic lymphocytes
    • Meesmann HM, Fehr EM, Kierschke S, Herrmann M, Bilyy R, Heyder P., et al. Decrease of sialic acid residues as an eat-me signal on the surface of apoptotic lymphocytes. J Cell Sci 2010; 123: 3347-3356
    • (2010) J Cell Sci , vol.123 , pp. 3347-3356
    • Meesmann, H.M.1    Fehr, E.M.2    Kierschke, S.3    Herrmann, M.4    Bilyy, R.5    Heyder, P.6
  • 45
    • 0036143018 scopus 로고    scopus 로고
    • Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation
    • Huynh ML, Fadok VA, Henson PM. Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation. J Clin Invest 2002; 109: 41-50
    • (2002) J Clin Invest , vol.109 , pp. 41-50
    • Huynh, M.L.1    Fadok, V.A.2    Henson, P.M.3
  • 46
    • 0031838606 scopus 로고    scopus 로고
    • Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus
    • Herrmann M, Voll RE, Zoller OM, Hagenhofer M, Ponner BB, Kalden JR. Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus. Arthritis Rheum 1998; 41: 1241-1250
    • (1998) Arthritis Rheum , vol.41 , pp. 1241-1250
    • Herrmann, M.1    Voll, R.E.2    Zoller, O.M.3    Hagenhofer, M.4    Ponner, B.B.5    Kalden, J.R.6
  • 47
    • 66449089455 scopus 로고    scopus 로고
    • Remnants of secondarily necrotic cells fuel inflammation in systemic lupus erythematosus
    • Munoz LE, Janko C, Grossmayer GE, Frey B, Voll RE, Kern P., et al. Remnants of secondarily necrotic cells fuel inflammation in systemic lupus erythematosus. Arthritis Rheum 2009; 60: 1733-1742
    • (2009) Arthritis Rheum , vol.60 , pp. 1733-1742
    • Munoz, L.E.1    Janko, C.2    Grossmayer, G.E.3    Frey, B.4    Voll, R.E.5    Kern, P.6
  • 48
    • 84919400992 scopus 로고    scopus 로고
    • Contribution of defective ps recognition and efferocytosis to chronic inflammation and autoimmunity
    • Kimani SG, Geng K, Kasikara C, Kumar S, Sriram G, Wu Y., et al. Contribution of defective ps recognition and efferocytosis to chronic inflammation and autoimmunity. Front Immunol 2014; 5: 566
    • (2014) Front Immunol , vol.5 , pp. 566
    • Kimani, S.G.1    Geng, K.2    Kasikara, C.3    Kumar, S.4    Sriram, G.5    Wu, Y.6
  • 49
    • 0036645294 scopus 로고    scopus 로고
    • Delayed apoptotic cell clearance and lupus-like autoimmunity in mice lacking the c-mer membrane tyrosine kinase
    • Cohen PL, Caricchio R, Abraham V, Camenisch TD, Jennette JC, Roubey RA., et al. Delayed apoptotic cell clearance and lupus-like autoimmunity in mice lacking the c-mer membrane tyrosine kinase. J Exp Med 2002; 196: 135-140
    • (2002) J Exp Med , vol.196 , pp. 135-140
    • Cohen, P.L.1    Caricchio, R.2    Abraham, V.3    Camenisch, T.D.4    Jennette, J.C.5    Roubey, R.A.6
  • 50
    • 41249092199 scopus 로고    scopus 로고
    • Autophosphorylation docking site Tyr-867 in Mer receptor tyrosine kinase allows for dissociation of multiple signaling pathways for phagocytosis of apoptotic cells and down-modulation of lipopolysaccharideinducible NF-kappaB transcriptional activation
    • Tibrewal N, Wu Y, D'Mello V, Akakura R, George TC, Varnum B., et al. Autophosphorylation docking site Tyr-867 in Mer receptor tyrosine kinase allows for dissociation of multiple signaling pathways for phagocytosis of apoptotic cells and down-modulation of lipopolysaccharideinducible NF-kappaB transcriptional activation. J Biol Chem 2008; 283: 3618-3627
    • (2008) J Biol Chem , vol.283 , pp. 3618-3627
    • Tibrewal, N.1    Wu, Y.2    D'Mello, V.3    Akakura, R.4    George, T.C.5    Varnum, B.6
  • 51
    • 1642536490 scopus 로고    scopus 로고
    • Innate immune discrimination of apoptotic cells: Repression of proinflammatory macrophage transcription is coupled directly to specific recognition
    • Cvetanovic M, Ucker DS. Innate immune discrimination of apoptotic cells: repression of proinflammatory macrophage transcription is coupled directly to specific recognition. J Immunol 2004; 172: 880-889
    • (2004) J Immunol , vol.172 , pp. 880-889
    • Cvetanovic, M.1    Ucker, D.S.2
  • 52
    • 36849033963 scopus 로고    scopus 로고
    • TAM receptors are pleiotropic inhibitors of the innate immune response
    • Rothlin CV, Ghosh S, Zuniga EI, Oldstone MB, Lemke G. TAM receptors are pleiotropic inhibitors of the innate immune response. Cell 2007; 131: 1124-1136
    • (2007) Cell , vol.131 , pp. 1124-1136
    • Rothlin, C.V.1    Ghosh, S.2    Zuniga, E.I.3    Oldstone, M.B.4    Lemke, G.5
  • 53
    • 84880730041 scopus 로고    scopus 로고
    • T cell-derived protein S engages TAM receptor signaling in dendritic cells to control the magnitude of the immune response.
    • Carrera Silva EA, Chan PY, Joannas L, Errasti AE, Gagliani N, Bosurgi L., et al. T cell-derived protein S engages TAM receptor signaling in dendritic cells to control the magnitude of the immune response. Immunity 2013; 39: 160-170
    • (2013) Immunity , vol.39 , pp. 160-170
    • Carrera Silva, E.A.1    Chan, P.Y.2    Joannas, L.3    Errasti, A.E.4    Gagliani, N.5    Bosurgi, L.6
  • 54
    • 78650661684 scopus 로고    scopus 로고
    • TIM-4, a receptor for phosphatidylserine, controls adaptive immunity by regulating the removal of antigenspecific T cells
    • Albacker LA, Karisola P, Chang YJ, Umetsu SE, Zhou M, Akbari O., et al. TIM-4, a receptor for phosphatidylserine, controls adaptive immunity by regulating the removal of antigenspecific T cells. J Immunol 2010; 185: 6839-6849
    • (2010) J Immunol , vol.185 , pp. 6839-6849
    • Albacker, L.A.1    Karisola, P.2    Chang, Y.J.3    Umetsu, S.E.4    Zhou, M.5    Akbari, O.6
  • 55
    • 77949900365 scopus 로고    scopus 로고
    • T cell/transmembrane, Ig, and mucin-3 allelic variants differentially recognize phosphatidylserine and mediate phagocytosis of apoptotic cells
    • DeKruyff RH, Bu X, Ballesteros A, Santiago C, Chim YL, Lee HH., et al. T cell/transmembrane, Ig, and mucin-3 allelic variants differentially recognize phosphatidylserine and mediate phagocytosis of apoptotic cells. J Immunol 2010; 184: 1918-1930
    • (2010) J Immunol , vol.184 , pp. 1918-1930
    • DeKruyff, R.H.1    Bu, X.2    Ballesteros, A.3    Santiago, C.4    Chim, Y.L.5    Lee, H.H.6
  • 57
    • 37049039277 scopus 로고    scopus 로고
    • Structures of T cell immunoglobulin mucin protein 4 show a metal-Ion-dependent ligand binding site where phosphatidylserine binds
    • Santiago C, Ballesteros A, Martinez-Munoz L, Mellado M, Kaplan GG, Freeman GJ., et al. Structures of T cell immunoglobulin mucin protein 4 show a metal-Ion-dependent ligand binding site where phosphatidylserine binds. Immunity 2007; 27: 941-951
    • (2007) Immunity , vol.27 , pp. 941-951
    • Santiago, C.1    Ballesteros, A.2    Martinez-Munoz, L.3    Mellado, M.4    Kaplan, G.G.5    Freeman, G.J.6
  • 58
    • 33947113954 scopus 로고    scopus 로고
    • Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family
    • Santiago C, Ballesteros A, Tami C, Martinez-Munoz L, Kaplan GG, Casasnovas JM. Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family. Immunity 2007; 26: 299-310
    • (2007) Immunity , vol.26 , pp. 299-310
    • Santiago, C.1    Ballesteros, A.2    Tami, C.3    Martinez-Munoz, L.4    Kaplan, G.G.5    Casasnovas, J.M.6
  • 59
    • 77951673268 scopus 로고    scopus 로고
    • TIM genes: A family of cell surface phosphatidylserine receptors that regulate innate and adaptive immunity
    • Freeman GJ, Casasnovas JM, Umetsu DT, DeKruyff RH. TIM genes: a family of cell surface phosphatidylserine receptors that regulate innate and adaptive immunity. Immunol Rev 2010; 235: 172-189
    • (2010) Immunol Rev , vol.235 , pp. 172-189
    • Freeman, G.J.1    Casasnovas, J.M.2    Umetsu, D.T.3    DeKruyff, R.H.4
  • 60
    • 84905967067 scopus 로고    scopus 로고
    • Too much of a good thing?. Tim-3 and TCR signaling in T cell exhaustion
    • Ferris RL, Lu B, Kane LP. Too much of a good thing?. Tim-3 and TCR signaling in T cell exhaustion. J Immunol 2014; 193: 1525-1530
    • (2014) J Immunol , vol.193 , pp. 1525-1530
    • Ferris, R.L.1    Lu, B.2    Kane, L.P.3
  • 61
    • 84868669212 scopus 로고    scopus 로고
    • Bat3 promotes T cell responses and autoimmunity by repressing Tim-3-mediated cell death and exhaustion
    • Rangachari M, Zhu C, Sakuishi K, Xiao S, Karman J, Chen A., et al. Bat3 promotes T cell responses and autoimmunity by repressing Tim-3-mediated cell death and exhaustion. Nat Med 2012; 18: 1394-1400
    • (2012) Nat Med , vol.18 , pp. 1394-1400
    • Rangachari, M.1    Zhu, C.2    Sakuishi, K.3    Xiao, S.4    Karman, J.5    Chen, A.6
  • 62
    • 80053608320 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent coupling of Tim-3 to T-cell receptor signaling pathways
    • Lee J, Su EW, Zhu C, Hainline S, Phuah J, Moroco JA., et al. Phosphotyrosine-dependent coupling of Tim-3 to T-cell receptor signaling pathways. Mol Cell Biol 2011; 31: 3963-3974
    • (2011) Mol Cell Biol , vol.31 , pp. 3963-3974
    • Lee, J.1    Su, E.W.2    Zhu, C.3    Hainline, S.4    Phuah, J.5    Moroco, J.A.6
  • 63
    • 84865422909 scopus 로고    scopus 로고
    • Tumorinfiltrating DCs suppress nucleic acid-mediated innate immune responses through interactions between the receptor TIM-3 and the alarmin HMGB1
    • Chiba S, Baghdadi M, Akiba H, Yoshiyama H, Kinoshita I, Dosaka-Akita H., et al. Tumorinfiltrating DCs suppress nucleic acid-mediated innate immune responses through interactions between the receptor TIM-3 and the alarmin HMGB1. Nat Immunol 2012; 13: 832-842
    • (2012) Nat Immunol , vol.13 , pp. 832-842
    • Chiba, S.1    Baghdadi, M.2    Akiba, H.3    Yoshiyama, H.4    Kinoshita, I.5    Dosaka-Akita, H.6
  • 64
  • 65
    • 84896955320 scopus 로고    scopus 로고
    • Role of phosphatidylserine receptors in enveloped virus infection
    • Morizono K, Chen IS. Role of phosphatidylserine receptors in enveloped virus infection. J Virol 2014; 88: 4275-4290
    • (2014) J Virol , vol.88 , pp. 4275-4290
    • Morizono, K.1    Chen, I.S.2
  • 66
    • 84922748055 scopus 로고    scopus 로고
    • Phosphatidylserine vesicles enable efficient en bloc transmission of enteroviruses
    • Chen YH, Du W, Hagemeijer MC, Takvorian PM, Pau C, Cali A., et al. Phosphatidylserine vesicles enable efficient en bloc transmission of enteroviruses. Cell 2015; 160: 619-630
    • (2015) Cell , vol.160 , pp. 619-630
    • Chen, Y.H.1    Du, W.2    Hagemeijer, M.C.3    Takvorian, P.M.4    Pau, C.5    Cali, A.6
  • 67
    • 84876287430 scopus 로고    scopus 로고
    • A pathogenic picornavirus acquires an envelope by hijacking cellular membranes
    • Feng Z, Hensley L, McKnight KL, Hu F, Madden V, Ping L., et al. A pathogenic picornavirus acquires an envelope by hijacking cellular membranes. Nature 2013; 496: 367-371
    • (2013) Nature , vol.496 , pp. 367-371
    • Feng, Z.1    Hensley, L.2    McKnight, K.L.3    Hu, F.4    Madden, V.5    Ping, L.6
  • 68
    • 84886252917 scopus 로고    scopus 로고
    • Direct formation of vaccinia virus membranes from the endoplasmic reticulum in the absence of the newly characterized L2-interacting protein A30.5
    • Maruri-Avidal L, Weisberg AS, Moss B. Direct formation of vaccinia virus membranes from the endoplasmic reticulum in the absence of the newly characterized L2-interacting protein A30.5. J Virol 2013; 87: 12313-12326
    • (2013) J Virol , vol.87 , pp. 12313-12326
    • Maruri-Avidal, L.1    Weisberg, A.S.2    Moss, B.3
  • 69
    • 84872610774 scopus 로고    scopus 로고
    • Comparative lipidomics analysis of HIV-1 particles and their producer cell membrane in different cell lines
    • Lorizate M, Sachsenheimer T, Glass B, Habermann A, Gerl MJ, Krausslich HG., et al. Comparative lipidomics analysis of HIV-1 particles and their producer cell membrane in different cell lines. Cell Microbiol 2013; 15: 292-304
    • (2013) Cell Microbiol , vol.15 , pp. 292-304
    • Lorizate, M.1    Sachsenheimer, T.2    Glass, B.3    Habermann, A.4    Gerl, M.J.5    Krausslich, H.G.6
  • 70
    • 79961113678 scopus 로고    scopus 로고
    • High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine
    • Fairn GD, Schieber NL, Ariotti N, Murphy S, Kuerschner L, Webb RI., et al. High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine. J Cell Biol 2011; 194: 257-275
    • (2011) J Cell Biol , vol.194 , pp. 257-275
    • Fairn, G.D.1    Schieber, N.L.2    Ariotti, N.3    Murphy, S.4    Kuerschner, L.5    Webb, R.I.6
  • 71
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer J, Helenius A. Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 2008; 320: 531-535
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 72
    • 78049493045 scopus 로고    scopus 로고
    • Apoptotic mimicry: Phosphatidylserine-mediated macropinocytosis of vaccinia virus
    • Mercer J, Helenius A. Apoptotic mimicry: phosphatidylserine-mediated macropinocytosis of vaccinia virus. Ann NY Acad Sci 2010; 1209: 49-55
    • (2010) Ann NY Acad Sci , vol.1209 , pp. 49-55
    • Mercer, J.1    Helenius, A.2
  • 73
    • 84882338751 scopus 로고    scopus 로고
    • Enveloped viruses disable innate immune responses in dendritic cells by direct activation of TAM receptors
    • Bhattacharyya S, Zagorska A, Lew ED, Shrestha B, Rothlin CV, Naughton J., et al. Enveloped viruses disable innate immune responses in dendritic cells by direct activation of TAM receptors. Cell Host Microbe 2013; 14: 136-147
    • (2013) Cell Host Microbe , vol.14 , pp. 136-147
    • Bhattacharyya, S.1    Zagorska, A.2    Lew, E.D.3    Shrestha, B.4    Rothlin, C.V.5    Naughton, J.6
  • 74
    • 19944412730 scopus 로고    scopus 로고
    • Vaccinia virus induces strong immunoregulatory cytokine production in healthy human epidermal keratinocytes: A novel strategy for immune evasion
    • Liu L, Xu Z, Fuhlbrigge RC, Pena-Cruz V, Lieberman J, Kupper TS. Vaccinia virus induces strong immunoregulatory cytokine production in healthy human epidermal keratinocytes: a novel strategy for immune evasion. J Virol 2005; 79: 7363-7370
    • (2005) J Virol , vol.79 , pp. 7363-7370
    • Liu, L.1    Xu, Z.2    Fuhlbrigge, R.C.3    Pena-Cruz, V.4    Lieberman, J.5    Kupper, T.S.6
  • 75
    • 84925307941 scopus 로고    scopus 로고
    • Effective binding of a phosphatidylserine-targeting antibody to Ebola virus infected cells and purified virions
    • Dowall SD, Graham VA, Corbin-Lickfett K, Empig C, Schlunegger K, Bruce CB., et al. Effective binding of a phosphatidylserine-targeting antibody to Ebola virus infected cells and purified virions. J Immunol Res 2015; 2015: 347903
    • (2015) J Immunol Res , vol.2015 , pp. 347903
    • Dowall, S.D.1    Graham, V.A.2    Corbin-Lickfett, K.3    Empig, C.4    Schlunegger, K.5    Bruce, C.B.6
  • 76
    • 57349140230 scopus 로고    scopus 로고
    • Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases
    • Soares MM, King SW, Thorpe PE. Targeting inside-out phosphatidylserine as a therapeutic strategy for viral diseases. Nat Med 2008; 14: 1357-1362
    • (2008) Nat Med , vol.14 , pp. 1357-1362
    • Soares, M.M.1    King, S.W.2    Thorpe, P.E.3
  • 77
    • 77951080820 scopus 로고    scopus 로고
    • Anti-phospholipid human monoclonal antibodies inhibit CCR5-tropic HIV-1 and induce beta-chemokines
    • Moody MA, Liao HX, Alam SM, Scearce RM, Plonk MK, Kozink DM., et al. Anti-phospholipid human monoclonal antibodies inhibit CCR5-tropic HIV-1 and induce beta-chemokines. J Exp Med 2010; 207: 763-776
    • (2010) J Exp Med , vol.207 , pp. 763-776
    • Ma, M.1    Liao, H.X.2    Alam, S.M.3    Scearce, R.M.4    Plonk, M.K.5    Kozink, D.M.6
  • 78
    • 84898632757 scopus 로고    scopus 로고
    • Axl receptor blockade ameliorates pulmonary pathology resulting from primary viral infection and viral exacerbation of asthma
    • Shibata T, Habiel DM, Coelho AL, Kunkel SL, Lukacs NW, Hogaboam CM. Axl receptor blockade ameliorates pulmonary pathology resulting from primary viral infection and viral exacerbation of asthma. J Immunol 2014; 192: 3569-3581
    • (2014) J Immunol , vol.192 , pp. 3569-3581
    • Shibata, T.1    Habiel, D.M.2    Coelho, A.L.3    Kunkel, S.L.4    Lukacs, N.W.5    Hogaboam, C.M.6
  • 79
    • 84899912557 scopus 로고    scopus 로고
    • Listeria monocytogenes exploits efferocytosis to promote cell-to-cell spread
    • Czuczman MA, Fattouh R, Van Rijn JM, Canadien V, Osborne S, Muise AM., et al. Listeria monocytogenes exploits efferocytosis to promote cell-to-cell spread. Nature 2014; 509: 230-234
    • (2014) Nature , vol.509 , pp. 230-234
    • Ma, C.1    Fattouh, R.2    Van Rijn, J.M.3    Canadien, V.4    Osborne, S.5    Muise, A.M.6
  • 81
    • 0028817287 scopus 로고
    • Apoptosis in a unicellular eukaryote (Trypanosoma cruzi): Implications for the evolutionary origin and role of programmed cell death in the control of cell proliferation, differentiation and survival
    • Ameisen JC, Idziorek T, Billaut-Mulot O, Loyens M, Tissier JP, Potentier A., et al. Apoptosis in a unicellular eukaryote (Trypanosoma cruzi): implications for the evolutionary origin and role of programmed cell death in the control of cell proliferation, differentiation and survival. Cell Death Differ 1995; 2: 285-300
    • (1995) Cell Death Differ , vol.2 , pp. 285-300
    • Ameisen, J.C.1    Idziorek, T.2    Billaut-Mulot, O.3    Loyens, M.4    Tissier, J.P.5    Potentier, A.6
  • 83
    • 77956882084 scopus 로고    scopus 로고
    • Programmed cell death in unicellular parasites: A prerequisite for sustained infection?
    • Van Zandbergen G, Luder CG, Heussler V, Duszenko M. Programmed cell death in unicellular parasites: a prerequisite for sustained infection?. Trends Parasitol 2010; 26: 477-483
    • (2010) Trends Parasitol , vol.26 , pp. 477-483
    • Van Zandbergen, G.1    Luder, C.G.2    Heussler, V.3    Duszenko, M.4
  • 84
    • 46549086296 scopus 로고    scopus 로고
    • Programmed cell death in protists
    • Deponte M. Programmed cell death in protists. Biochim Biophys Acta 2008; 1783: 1396-1405
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1396-1405
    • Deponte, M.1
  • 85
    • 84900336254 scopus 로고    scopus 로고
    • The calpain inhibitor MDL28170 induces the expression of apoptotic markers in Leishmania amazonensis promastigotes
    • Marinho FA, Goncalves KC, Oliveira SS, Goncalves DS, Matteoli FP, Seabra SH., et al. The calpain inhibitor MDL28170 induces the expression of apoptotic markers in Leishmania amazonensis promastigotes. PLoS One 2014; 9: e87659
    • (2014) PLoS One , vol.9 , pp. e87659
    • Marinho, F.A.1    Goncalves, K.C.2    Oliveira, S.S.3    Goncalves, D.S.4    Matteoli, F.P.5    Seabra, S.H.6
  • 88
    • 79953111659 scopus 로고    scopus 로고
    • Evolution of apoptosis-like programmed cell death in unicellular protozoan parasites
    • Kaczanowski S, Sajid M, Reece SE. Evolution of apoptosis-like programmed cell death in unicellular protozoan parasites. Parasit Vectors 2011; 4: 44
    • (2011) Parasit Vectors , vol.4 , pp. 44
    • Kaczanowski, S.1    Sajid, M.2    Reece, S.E.3
  • 89
    • 3142686069 scopus 로고    scopus 로고
    • Programmed cell death in trypanosomatids: A way to maximize their biological fitness?
    • Nguewa PA, Fuertes MA, Valladares B, Alonso C, Perez JM. Programmed cell death in trypanosomatids: a way to maximize their biological fitness?. Trends Parasitol 2004; 20: 375-380
    • (2004) Trends Parasitol , vol.20 , pp. 375-380
    • Nguewa, P.A.1    Ma, F.2    Valladares, B.3    Alonso, C.4    Perez, J.M.5
  • 90
    • 31144454859 scopus 로고    scopus 로고
    • Mimicry of apoptotic cells by exposing phosphatidylserine participates in the establishment of amastigotes of Leishmania L) amazonensis in mammalian hosts
    • Wanderley JL, Moreira ME, Benjamin A, Bonomo AC, Barcinski M.A. Mimicry of apoptotic cells by exposing phosphatidylserine participates in the establishment of amastigotes of Leishmania (L) amazonensis in mammalian hosts. J Immunol 2006; 176: 1834-1839
    • (2006) J Immunol , vol.176 , pp. 1834-1839
    • Wanderley, J.L.1    Moreira, M.E.2    Benjamin, A.3    Bonomo, A.C.4    Barcinski, M.A.5
  • 92
    • 82255195421 scopus 로고    scopus 로고
    • Phosphatidylserine exposure by Toxoplasma gondii is fundamental to balance the immune response granting survival of the parasite and of the host
    • Santos TA, Portes Jde A, Damasceno-Sa JC, Caldas LA, Souza W, Damatta RA., et al. Phosphatidylserine exposure by Toxoplasma gondii is fundamental to balance the immune response granting survival of the parasite and of the host. PLoS One 2011; 6: e27867
    • (2011) PLoS One , vol.6 , pp. e27867
    • Santos, T.A.1    Portes Jde, A.2    Damasceno-Sa, J.C.3    Caldas, L.A.4    Souza, W.5    Damatta, R.A.6
  • 94
    • 84876831551 scopus 로고    scopus 로고
    • LABCG2, a new ABC transporter implicated in phosphatidylserine exposure, is involved in the infectivity and pathogenicity of Leishmania
    • Campos-Salinas J, Leon-Guerrero D, Gonzalez-Rey E, Delgado M, Castanys S, Perez- Victoria JM., et al. LABCG2, a new ABC transporter implicated in phosphatidylserine exposure, is involved in the infectivity and pathogenicity of Leishmania. PLoS Negl Trop Dis 2013; 7: e2179
    • (2013) PLoS Negl Trop Dis , vol.7 , pp. e2179
    • Campos-Salinas, J.1    Leon-Guerrero, D.2    Gonzalez-Rey, E.3    Delgado, M.4    Castanys, S.5    Perez- Victoria, J.M.6
  • 95
    • 33748808057 scopus 로고    scopus 로고
    • Leishmania disease development depends on the presence of apoptotic promastigotes in the virulent inoculum
    • Van Zandbergen G, Bollinger A, Wenzel A, Kamhawi S, Voll R, Klinger M., et al. Leishmania disease development depends on the presence of apoptotic promastigotes in the virulent inoculum. Proc Natl Acad Sci USA 2006; 103: 13837-13842
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13837-13842
    • Van Zandbergen, G.1    Bollinger, A.2    Wenzel, A.3    Kamhawi, S.4    Voll, R.5    Klinger, M.6
  • 96
    • 0036829110 scopus 로고    scopus 로고
    • Increased exposure of anionic phospholipids on the surface of tumor blood vessels
    • Ran S, Downes A, Thorpe PE. Increased exposure of anionic phospholipids on the surface of tumor blood vessels. Cancer Res 2002; 62: 6132-6140
    • (2002) Cancer Res , vol.62 , pp. 6132-6140
    • Ran, S.1    Downes, A.2    Thorpe, P.E.3
  • 97
    • 8644274867 scopus 로고    scopus 로고
    • Inhibition of phosphatidylserine recognition heightens the immunogenicity of irradiated lymphoma cells in vivo
    • Bondanza A, Zimmermann VS, Rovere-Querini P, Turnay J, Dumitriu IE, Stach CM., et al. Inhibition of phosphatidylserine recognition heightens the immunogenicity of irradiated lymphoma cells in vivo. J Exp Med 2004; 200: 1157-1165
    • (2004) J Exp Med , vol.200 , pp. 1157-1165
    • Bondanza, A.1    Zimmermann, V.S.2    Rovere-Querini, P.3    Turnay, J.4    Dumitriu, I.E.5    Stach, C.M.6
  • 98
    • 84948181477 scopus 로고    scopus 로고
    • Extracellular vesicles present in human ovarian tumor microenvironments induce a phosphatidylserine dependent arrest in the T cell signaling cascade
    • Kelleher RJ, Balu-Iyer S, Loyall JL, Sacca AJ, Shenoy GN, Peng P., et al. Extracellular vesicles present in human ovarian tumor microenvironments induce a phosphatidylserine dependent arrest in the T cell signaling cascade. Cancer Immunol Res 2015; 3: 1269-1278
    • (2015) Cancer Immunol Res , vol.3 , pp. 1269-1278
    • Kelleher, R.J.1    Balu-Iyer, S.2    Loyall, J.L.3    Sacca, A.J.4    Shenoy, G.N.5    Peng, P.6
  • 99
    • 84922481128 scopus 로고    scopus 로고
    • The TAM family: Phosphatidylserine sensing receptor tyrosine kinases gone awry in cancer
    • Graham DK, DeRyckere D, Davies KD, Earp HS. The TAM family: phosphatidylserine sensing receptor tyrosine kinases gone awry in cancer. Nat Rev Cancer 2014; 14: 769-785
    • (2014) Nat Rev Cancer , vol.14 , pp. 769-785
    • Graham, D.K.1    DeRyckere, D.2    Davies, K.D.3    Earp, H.S.4
  • 101
    • 84908637378 scopus 로고    scopus 로고
    • Efferocytosis produces a prometastatic landscape during postpartum mammary gland involution
    • Stanford JC, Young C, Hicks D, Owens P, Williams A, Vaught DB., et al. Efferocytosis produces a prometastatic landscape during postpartum mammary gland involution. J Clin Invest 2014; 124: 4737-4752
    • (2014) J Clin Invest , vol.124 , pp. 4737-4752
    • Stanford, J.C.1    Young, C.2    Hicks, D.3    Owens, P.4    Williams, A.5    Vaught, D.B.6
  • 102
    • 84897954522 scopus 로고    scopus 로고
    • The E3 ligase Cblb and TAM receptors regulate cancer metastasis via natural killer cells
    • Paolino M, Choidas A, Wallner S, Pranjic B, Uribesalgo I, Loeser S., et al. The E3 ligase Cblb and TAM receptors regulate cancer metastasis via natural killer cells. Nature 2014; 507: 508-512
    • (2014) Nature , vol.507 , pp. 508-512
    • Paolino, M.1    Choidas, A.2    Wallner, S.3    Pranjic, B.4    Uribesalgo, I.5    Loeser, S.6
  • 103
    • 84938350452 scopus 로고    scopus 로고
    • Combination cancer immunotherapy and new immunomodulatory targets
    • Mahoney KM, Rennert PD, Freeman GJ. Combination cancer immunotherapy and new immunomodulatory targets. Nat Rev Drug Discov 2015; 14: 561-584
    • (2015) Nat Rev Drug Discov , vol.14 , pp. 561-584
    • Mahoney, K.M.1    Rennert, P.D.2    Freeman, G.J.3
  • 104
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: Linking Ca2+ signalling to membrane dynamics
    • Gerke V, Creutz CE, Moss SE. Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol 2005; 6: 449-461
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 105
    • 69849100452 scopus 로고    scopus 로고
    • Tumor-derived microvesicles modulate the establishment of metastatic melanoma in a phosphatidylserinedependent manner
    • Lima LG, Chammas R, Monteiro RQ, Moreira ME, Barcinski M.A. Tumor-derived microvesicles modulate the establishment of metastatic melanoma in a phosphatidylserinedependent manner. Cancer Lett 2009; 283: 168-175
    • (2009) Cancer Lett , vol.283 , pp. 168-175
    • Lima, L.G.1    Chammas, R.2    Monteiro, R.Q.3    Moreira, M.E.4    Barcinski, M.A.5
  • 106
    • 33845877452 scopus 로고    scopus 로고
    • The influence on the immunomodulatory effects of dying and dead cells of Annexin V
    • Munoz LE, Franz S, Pausch F, Furnrohr B, Sheriff A, Vogt B., et al. The influence on the immunomodulatory effects of dying and dead cells of Annexin V. J Leukoc Biol 2007; 81: 6-14
    • (2007) J Leukoc Biol , vol.81 , pp. 6-14
    • Munoz, L.E.1    Franz, S.2    Pausch, F.3    Furnrohr, B.4    Sheriff, A.5    Vogt, B.6
  • 107
    • 0033778724 scopus 로고    scopus 로고
    • Treatment with annexin v increases immunogenicity of apoptotic human T-cells in Balb/c mice
    • Stach CM, Turnay X, Voll RE, Kern PM, Kolowos W, Beyer TD., et al. Treatment with annexin V increases immunogenicity of apoptotic human T-cells in Balb/c mice. Cell Death Differ 2000; 7: 911-915
    • (2000) Cell Death Differ , vol.7 , pp. 911-915
    • Stach, C.M.1    Turnay, X.2    Voll, R.E.3    Kern, P.M.4    Kolowos, W.5    Beyer, T.D.6
  • 108
    • 70450219473 scopus 로고    scopus 로고
    • AnnexinA5 renders dead tumor cells immunogenic-implications for multimodal cancer therapies
    • Frey B, Schildkopf P, Rodel F, Weiss EM, Munoz LE, Herrmann M., et al. AnnexinA5 renders dead tumor cells immunogenic-implications for multimodal cancer therapies. J Immunotoxicol 2009; 6: 209-216
    • (2009) J Immunotoxicol , vol.6 , pp. 209-216
    • Frey, B.1    Schildkopf, P.2    Rodel, F.3    Weiss, E.M.4    Munoz, L.E.5    Herrmann, M.6
  • 110
    • 0032739985 scopus 로고    scopus 로고
    • Involvement of phosphatidylserine and non-phospholipid components of the hepatitis B virus envelope in human Annexin v binding and in HBV infection in vitro
    • De Meyer S, Gong Z, Depla E, Maertens G, Yap SH. Involvement of phosphatidylserine and non-phospholipid components of the hepatitis B virus envelope in human Annexin V binding and in HBV infection in vitro. J Hepatol 1999; 31: 783-790
    • (1999) J Hepatol , vol.31 , pp. 783-790
    • De Meyer, S.1    Gong, Z.2    Depla, E.3    Maertens, G.4    Yap, S.H.5
  • 111
    • 80051890661 scopus 로고    scopus 로고
    • Development of bavituximab, a vascular targeting agent with immune-modulating properties, for lung cancer treatment
    • DeRose P, Thorpe PE, Gerber DE. Development of bavituximab, a vascular targeting agent with immune-modulating properties, for lung cancer treatment. Immunotherapy 2011; 3: 933-944
    • (2011) Immunotherapy , vol.3 , pp. 933-944
    • DeRose, P.1    Thorpe, P.E.2    Gerber, D.E.3
  • 112
    • 20144374032 scopus 로고    scopus 로고
    • A monoclonal antibody that binds anionic phospholipids on tumor blood vessels enhances the antitumor effect of docetaxel on human breast tumors in mice
    • Huang X, Bennett M, Thorpe PE. A monoclonal antibody that binds anionic phospholipids on tumor blood vessels enhances the antitumor effect of docetaxel on human breast tumors in mice. Cancer Res 2005; 65: 4408-4416
    • (2005) Cancer Res , vol.65 , pp. 4408-4416
    • Huang, X.1    Bennett, M.2    Thorpe, P.E.3
  • 113
    • 33646420098 scopus 로고    scopus 로고
    • Combination of a monoclonal anti-phosphatidylserine antibody with gemcitabine strongly inhibits the growth and metastasis of orthotopic pancreatic tumors in mice
    • Beck AW, Luster TA, Miller AF, Holloway SE, Conner CR, Barnett CC., et al. Combination of a monoclonal anti-phosphatidylserine antibody with gemcitabine strongly inhibits the growth and metastasis of orthotopic pancreatic tumors in mice. Int J Cancer 2006; 118: 2639-2643
    • (2006) Int J Cancer , vol.118 , pp. 2639-2643
    • Beck, A.W.1    Luster, T.A.2    Miller, A.F.3    Holloway, S.E.4    Conner, C.R.5    Barnett, C.C.6
  • 114
    • 72549108621 scopus 로고    scopus 로고
    • Antiphosphatidylserine antibody combined with irradiation damages tumor blood vessels and induces tumor immunity in a rat model of glioblastoma
    • He J, Yin Y, Luster TA, Watkins L, Thorpe PE. Antiphosphatidylserine antibody combined with irradiation damages tumor blood vessels and induces tumor immunity in a rat model of glioblastoma. Clin Cancer Res 2009; 15: 6871-6880
    • (2009) Clin Cancer Res , vol.15 , pp. 6871-6880
    • He, J.1    Yin, Y.2    Luster, T.A.3    Watkins, L.4    Thorpe, P.E.5
  • 115
    • 84890933692 scopus 로고    scopus 로고
    • Phosphatidylserine-targeting antibody induces M1 macrophage polarization and promotes myeloid-derived suppressor cell differentiation
    • Yin Y, Huang X, Lynn KD, Thorpe PE. Phosphatidylserine-targeting antibody induces M1 macrophage polarization and promotes myeloid-derived suppressor cell differentiation. Cancer immunol Res 2013; 1: 256-268
    • (2013) Cancer Immunol Res , vol.1 , pp. 256-268
    • Yin, Y.1    Huang, X.2    Lynn, K.D.3    Thorpe, P.E.4
  • 116
    • 85006216584 scopus 로고    scopus 로고
    • A phase i clinical trial of bavituximab and paclitaxel in patients with HER2 negative metastatic breast cancer
    • Chalasani P, Marron M, Roe D, Clarke K, Iannone M, Livingston RB., et al. A phase I clinical trial of bavituximab and paclitaxel in patients with HER2 negative metastatic breast cancer. Cancer Med 2015; 4: 1051-1059
    • (2015) Cancer Med , vol.4 , pp. 1051-1059
    • Chalasani, P.1    Marron, M.2    Roe, D.3    Clarke, K.4    Iannone, M.5    Livingston, R.B.6
  • 117
    • 84908404361 scopus 로고    scopus 로고
    • Bavituximab plus paclitaxel and carboplatin for the treatment of advanced non-small-cell lung cancer
    • Digumarti R, Bapsy PP, Suresh AV, Bhattacharyya GS, Dasappa L, Shan JS., et al. Bavituximab plus paclitaxel and carboplatin for the treatment of advanced non-small-cell lung cancer. Lung Cancer 2014; 86: 231-236
    • (2014) Lung Cancer , vol.86 , pp. 231-236
    • Digumarti, R.1    Bapsy, P.P.2    Suresh, A.V.3    Bhattacharyya, G.S.4    Dasappa, L.5    Shan, J.S.6
  • 118
    • 80455127305 scopus 로고    scopus 로고
    • Phase i safety and pharmacokinetic study of bavituximab, a chimeric phosphatidylserine-targeting monoclonal antibody, in patients with advanced solid tumors
    • Gerber DE, Stopeck AT, Wong L, Rosen LS, Thorpe PE, Shan JS., et al. Phase I safety and pharmacokinetic study of bavituximab, a chimeric phosphatidylserine-targeting monoclonal antibody, in patients with advanced solid tumors. Clin Cancer Res 2011; 17: 6888-6896
    • (2011) Clin Cancer Res , vol.17 , pp. 6888-6896
    • De, G.1    Stopeck, A.T.2    Wong, L.3    Rosen, L.S.4    Thorpe, P.E.5    Shan, J.S.6
  • 120
    • 67651171188 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis evades macrophage defenses by inhibiting plasma membrane repair
    • Divangahi M, Chen M, Gan H, Desjardins D, Hickman TT, Lee DM., et al. Mycobacterium tuberculosis evades macrophage defenses by inhibiting plasma membrane repair. Nat Immunol 2009; 10: 899-906
    • (2009) Nat Immunol , vol.10 , pp. 899-906
    • Divangahi, M.1    Chen, M.2    Gan, H.3    Desjardins, D.4    Hickman, T.T.5    Lee, D.M.6
  • 121
    • 58149296186 scopus 로고    scopus 로고
    • Lipid mediators in innate immunity against tuberculosis: Opposing roles of PGE2 and LXA4 in the induction of macrophage death
    • Chen M, Divangahi M, Gan H, Shin DS, Hong S, Lee DM., et al. Lipid mediators in innate immunity against tuberculosis: opposing roles of PGE2 and LXA4 in the induction of macrophage death. J Exp Med 2008; 205: 2791-2801
    • (2008) J Exp Med , vol.205 , pp. 2791-2801
    • Chen, M.1    Divangahi, M.2    Gan, H.3    Shin, D.S.4    Hong, S.5    Lee, D.M.6
  • 122
    • 0036434149 scopus 로고    scopus 로고
    • Cytoadherence of malaria-infected red blood cells involves exposure of phosphatidylserine
    • Eda S, Sherman IW. Cytoadherence of malaria-infected red blood cells involves exposure of phosphatidylserine. Cell Physiol Biochem 2002; 12: 373-384
    • (2002) Cell Physiol Biochem , vol.12 , pp. 373-384
    • Eda, S.1    Sherman, I.W.2
  • 123
    • 0020363376 scopus 로고
    • Phospholipids in a measles virus persistent infection: Modification of fatty acid metabolism and fatty acid composition of released virus
    • Anderton P, Wild TF, Zwingelstein G. Phospholipids in a measles virus persistent infection: modification of fatty acid metabolism and fatty acid composition of released virus. J Gen Virol 1982; 62: 249-258
    • (1982) J Gen Virol , vol.62 , pp. 249-258
    • Anderton, P.1    Wild, T.F.2    Zwingelstein, G.3
  • 124
    • 0022336018 scopus 로고
    • Characteristic cellular fatty acid composition and an ornithine-containing lipid as a new type of hemagglutinin in Bordetella pertussis
    • Kawai Y. Characteristic cellular fatty acid composition and an ornithine-containing lipid as a new type of hemagglutinin in Bordetella pertussis. Dev Biol Stand 1985; 61: 249-254
    • (1985) Dev Biol Stand , vol.61 , pp. 249-254
    • Kawai, Y.1
  • 125
    • 0025300655 scopus 로고
    • Tetanus toxin channel in phosphatidylserine planar bilayers: Conductance states and pH dependence
    • Rauch G, Gambale F, Montal M. Tetanus toxin channel in phosphatidylserine planar bilayers: conductance states and pH dependence. Eur Biophys J 1990; 18: 79-83
    • (1990) Eur Biophys J , vol.18 , pp. 79-83
    • Rauch, G.1    Gambale, F.2    Montal, M.3
  • 126
    • 0028297815 scopus 로고
    • Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins
    • Belisle JT, Brandt ME, Radolf JD, Norgard MV. Fatty acids of Treponema pallidum and Borrelia burgdorferi lipoproteins. J Bacteriol 1994; 176: 2151-2157
    • (1994) J Bacteriol , vol.176 , pp. 2151-2157
    • Belisle, J.T.1    Brandt, M.E.2    Radolf, J.D.3    Norgard, M.V.4
  • 127
    • 84908025607 scopus 로고    scopus 로고
    • Lipid interactions during virus entry and infection
    • Mercer J, Mazzon M. Lipid interactions during virus entry and infection. Cell Microbiol 2014; 16: 1493-1502
    • (2014) Cell Microbiol , vol.16 , pp. 1493-1502
    • Mercer, J.1    Mazzon, M.2
  • 128
    • 9144220867 scopus 로고    scopus 로고
    • Cutting edge: Neutrophil granulocyte serves as a vector for Leishmania entry into macrophages
    • Van Zandbergen G, Klinger M, Mueller A, Dannenberg S, Gebert A, Solbach W., et al. Cutting edge: neutrophil granulocyte serves as a vector for Leishmania entry into macrophages. J Immunol 2004; 173: 6521-6525
    • (2004) J Immunol , vol.173 , pp. 6521-6525
    • Van Zandbergen, G.1    Klinger, M.2    Mueller, A.3    Dannenberg, S.4    Gebert, A.5    Solbach, W.6
  • 130
    • 59149103537 scopus 로고    scopus 로고
    • A Phase Ib safety and pharmacokinetic study of bavituximab plus chemotherapy in patients with refractory advanced solid tumor malignancies
    • Suppl Abstract 3038
    • Digumarti R, Bapsy PP, Shan JS. A Phase Ib safety and pharmacokinetic study of bavituximab plus chemotherapy in patients with refractory advanced solid tumor malignancies. J Clin Oncol 2008; 26(Suppl): Abstract 3038
    • (2008) J Clin Oncol , vol.26
    • Digumarti, R.1    Bapsy, P.P.2    Shan, J.S.3
  • 131
    • 80051869132 scopus 로고    scopus 로고
    • Phase II study of bavituximab plus docetaxel in locally advanced or metastatic breast cancer
    • Suppl Abstract 1042
    • Tabagari D, Nemsadze G, Janjalia M, Jincharadze M, Shan J. Phase II study of bavituximab plus docetaxel in locally advanced or metastatic breast cancer. J Clin Oncol 2010; 28 (Suppl): Abstract 1042
    • (2010) J Clin Oncol , vol.28
    • Tabagari, D.1    Nemsadze, G.2    Janjalia, M.3    Jincharadze, M.4    Shan, J.5
  • 132
    • 84880077570 scopus 로고    scopus 로고
    • Randomized, open-label, phase II trial of gemcitabine with or without bavituximab in patients with nonresectable stage IV pancreatic adenocarcinoma
    • Suppl: Abstract 4054
    • Pandya SS, Wong L, Bullock AJ, Grabelsky SA, Shum MK, Shan J., et al. Randomized, open-label, phase II trial of gemcitabine with or without bavituximab in patients with nonresectable stage IV pancreatic adenocarcinoma. J Clin Oncol 2013; 31(Suppl): Abstract 4054
    • (2013) J Clin Oncol , vol.31
    • Pandya, S.S.1    Wong, L.2    Bullock, A.J.3    Grabelsky, S.A.4    Shum, M.K.5    Shan, J.6
  • 133
    • 84938338794 scopus 로고    scopus 로고
    • Randomized, blinded, placebo-controlled phase II trial of docetaxel and bavituximab as second-line therapy in locally advanced or metastatic non-squamous non-small cell lung cancer
    • Suppl Abstract 8095
    • Shtivelband M, Spigel DR, Gerber DE, Jain MM, Ponomarova OV, Giorgadze D., et al. Randomized, blinded, placebo-controlled phase II trial of docetaxel and bavituximab as second-line therapy in locally advanced or metastatic non-squamous non-small cell lung cancer. J Clin Oncol 2013; 31(Suppl): Abstract 8095
    • (2013) J Clin Oncol , vol.31
    • Shtivelband, M.1    Spigel, D.R.2    De, G.3    Jain, M.M.4    Ponomarova, O.V.5    Giorgadze, D.6
  • 135
    • 84967274655 scopus 로고    scopus 로고
    • A phase II study of bavituximab and sorafenib in advanced hepatocellular carcinoma (HCC
    • Suppl): Abstract 4109
    • Yopp AC, Singal AG, Arriaga YE, Verma UN, Shan J, Kallinteris N., et al. A phase II study of bavituximab and sorafenib in advanced hepatocellular carcinoma (HCC). J Clin Oncol 2015; 33(Suppl): Abstract 4109
    • (2015) J Clin Oncol , vol.33
    • Yopp, A.C.1    Singal, A.G.2    Arriaga, Y.E.3    Verma, U.N.4    Shan, J.5    Kallinteris, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.