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Volumn 14, Issue 12, 2009, Pages 4892-4914

Phospholipids: Key players in apoptosis and immune regulation

Author keywords

Apoptosis; Clearance; Immune modulation; Phagocytosis; Phosphatidylserine; Phospholipids

Indexed keywords

LIGAND; PHOSPHOLIPID;

EID: 73849105316     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules14124892     Document Type: Review
Times cited : (130)

References (136)
  • 1
    • 36549076985 scopus 로고    scopus 로고
    • On the origin of lipid asymmetry: The flip side of ion transport
    • Lenoir, G.; Williamson, P.; Holthuis, J.C. On the origin of lipid asymmetry: the flip side of ion transport. Curr. Opin. Chem. Biol. 2007, 11, 654-661.
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 654-661
    • Lenoir, G.1    Williamson, P.2    Holthuis, J.C.3
  • 2
    • 0027179487 scopus 로고
    • Phospholipids in animal eukaryotic membranes: Transverse asymmetry and movement
    • Zachowski, A. Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem. J. 1993, 294, 1-14.
    • (1993) Biochem. J , vol.294 , pp. 1-14
    • Zachowski, A.1
  • 3
    • 50949084838 scopus 로고    scopus 로고
    • Phosphatidylserine and phosphatidylethanolamine in mammalian cells: Two metabolically related aminophospholipids
    • Vance, J.E., Phosphatidylserine and phosphatidylethanolamine in mammalian cells: two metabolically related aminophospholipids. J. Lipid. Res. 2008, 49, 1377-1387.
    • (2008) J. Lipid. Res , vol.49 , pp. 1377-1387
    • Vance, J.E.1
  • 4
    • 0020052831 scopus 로고
    • Generation of prothrombin-converting activity and the exposure of phosphatidylserine at the outer surface of platelets
    • Bevers, E.M.; Comfurius, P.; van Rijn, J.L.; Hemker, H.C.; Zwaal, R.F. Generation of prothrombin-converting 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
  • 5
    • 0026423662 scopus 로고
    • Transbilayer movement of phospholipids in red cell and platelet membranes
    • Schroit, A.J.; Zwaal, R.F. Transbilayer movement of phospholipids in red cell and platelet membranes. Biochim. Biophys. Acta 1991, 1071, 313-329.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 313-329
    • Schroit, A.J.1    Zwaal, R.F.2
  • 6
    • 0036676445 scopus 로고    scopus 로고
    • Exosomes: Composition, biogenesis and function
    • Thery, C.; Zitvogel, L.; Amigorena, S. Exosomes: composition, biogenesis and function. Nat. Rev. Immunol. 2002, 2, 569-579.
    • (2002) Nat. Rev. Immunol , vol.2 , pp. 569-579
    • Thery, C.1    Zitvogel, L.2    Amigorena, S.3
  • 7
    • 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, U.S.; Kalden, J.R.; Voll, R.E.; 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
  • 8
    • 0033937485 scopus 로고    scopus 로고
    • Surface expression of phosphatidylserine on macrophages is required for phagocytosis of apoptotic thymocytes
    • Callahan, M. K.; Williamson, P.; Schlegel, R. A. 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
  • 9
    • 26944463126 scopus 로고    scopus 로고
    • Phosphatidylserine-dependent engulfment by macrophages of nuclei from erythroid precursor cells
    • Yoshida, H.; Kawane, K.; Koike, M.; Mori, Y.; Uchiyama, Y.; Nagata, S. Phosphatidylserine-dependent 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
  • 10
    • 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, S.R.; Mancini, M.; Rosen, A.; Schlissel, M.S. 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
  • 12
    • 34249829887 scopus 로고    scopus 로고
    • Interaction of histones with phospholipids-implications for the exposure of histones on apoptotic cells
    • Furnrohr, B.G.; Groer, G.J.; Sehnert, B.; Herrmann, M.; Voll, R.E. Interaction of histones with phospholipids-implications for the exposure of histones on apoptotic cells. Autoimmunity 2007, 40, 322-326.
    • (2007) Autoimmunity , vol.40 , pp. 322-326
    • Furnrohr, B.G.1    Groer, G.J.2    Sehnert, B.3    Herrmann, M.4    Voll, R.E.5
  • 13
    • 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
  • 15
    • 33745258657 scopus 로고    scopus 로고
    • Tumor-driven evolution of immunosuppressive networks during malignant progression
    • Kim, R.; Emi, M.; Tanabe, K.; Arihiro, K. Tumor-driven evolution of immunosuppressive networks during malignant progression. Cancer Res. 2006, 66, 5527-5536.
    • (2006) Cancer Res , vol.66 , pp. 5527-5536
    • Kim, R.1    Emi, M.2    Tanabe, K.3    Arihiro, K.4
  • 16
    • 0036891466 scopus 로고    scopus 로고
    • Phosphatidylserine is a marker of tumor vasculature and a potential target for cancer imaging and therapy
    • Ran, S.; Thorpe, P. E. Phosphatidylserine is a marker of tumor vasculature and a potential target for cancer imaging and therapy. Int. J. Radiat. Oncol. Biol. Phys. 2002, 54, 1479-1484.
    • (2002) Int. J. Radiat. Oncol. Biol. Phys , vol.54 , pp. 1479-1484
    • Ran, S.1    Thorpe, P.E.2
  • 17
    • 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, A.J.; Connor, J.; Bucana, C.D.; Fidler, I.J. 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
  • 18
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J.F.; Wyllie, A.H.; Currie, A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 1972, 26, 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 19
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • Martin, S.J.; Reutelingsperger, C.P.; McGahon, A.J.; Rader, J.A.; van Schie, R.C.; LaFace, D. M.; Green, D. R. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl. J. Exp. Med. 1995, 182, 1545-1556.
    • (1995) J. Exp. Med , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    McGahon, A.J.3    Rader, J.A.4    van Schie, R.C.5    LaFace, D.M.6    Green, D.R.7
  • 20
    • 0028820202 scopus 로고
    • Mechanisms of phosphatidylserine exposure, a phagocyte recognition signal, on apoptotic T lymphocytes
    • Verhoven, B.; Schlegel, R.A.; Williamson, P. Mechanisms of phosphatidylserine exposure, a phagocyte recognition signal, on apoptotic T lymphocytes. J. Exp. Med. 1995, 182, 1597-1601.
    • (1995) J. Exp. Med , vol.182 , pp. 1597-1601
    • Verhoven, B.1    Schlegel, R.A.2    Williamson, P.3
  • 21
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok, V.A.; Voelker, D.R.; Campbell, P.A.; Cohen, J.J.; Bratton, D.L.; Henson, P.M. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 1992, 148, 2207-2216.
    • (1992) J. Immunol , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 25
    • 33748300590 scopus 로고    scopus 로고
    • Phosphatidic acid- and phosphatidylserine- binding proteins
    • Stace, C.L.; Ktistakis, N.T. Phosphatidic acid- and phosphatidylserine- binding proteins. Biochim. Biophys. Acta 2006, 1761, 913-926.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 913-926
    • Stace, C.L.1    Ktistakis, N.T.2
  • 27
    • 33746721535 scopus 로고    scopus 로고
    • Asymmetric distribution of phospholipids in biomembranes
    • Yamaji-Hasegawa, A.; Tsujimoto, M. Asymmetric distribution of phospholipids in biomembranes. Biol. Pharm. Bull. 2006, 29, 1547-1553.
    • (2006) Biol. Pharm. Bull , vol.29 , pp. 1547-1553
    • Yamaji-Hasegawa, A.1    Tsujimoto, M.2
  • 28
    • 33748347104 scopus 로고    scopus 로고
    • Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria
    • Chen, D.; Zhang, X.Y.; Shi, Y. Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria. Biochem. J. 2006, 398, 169-176.
    • (2006) Biochem. J , vol.398 , pp. 169-176
    • Chen, D.1    Zhang, X.Y.2    Shi, Y.3
  • 29
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame, M.; Rua, D.; Greenberg, M.L. The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 2000, 39, 257-288.
    • (2000) Prog. Lipid Res , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 30
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M.O. The biochemistry of apoptosis. Nature 2000, 407, 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 31
    • 0029992825 scopus 로고    scopus 로고
    • A subfamily of P-type ATPases with aminophospholipid transporting activity
    • Tang, X.; Halleck, M.S.; Schlegel, R.A.; Williamson, P. A subfamily of P-type ATPases with aminophospholipid transporting activity. Science 1996, 272, 1495-1497.
    • (1996) Science , vol.272 , pp. 1495-1497
    • Tang, X.1    Halleck, M.S.2    Schlegel, R.A.3    Williamson, P.4
  • 32
    • 0037203341 scopus 로고    scopus 로고
    • Transbilayer phospholipid movement and the clearance of apoptotic cells
    • Williamson, P.; Schlegel, R.A. Transbilayer phospholipid movement and the clearance of apoptotic cells. Biochim. Biophys. Acta 2002, 1585, 53-63.
    • (2002) Biochim. Biophys. Acta , vol.1585 , pp. 53-63
    • Williamson, P.1    Schlegel, R.A.2
  • 34
    • 67649270577 scopus 로고    scopus 로고
    • Linking phospholipid flippases to vesicle-mediated protein transport
    • Muthusamy, B.P.; Natarajan, P.; Zhou, X.; Graham, T.R. Linking phospholipid flippases to vesicle-mediated protein transport. Biochim. Biophys. Acta 2009, 1791, 612-619.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 612-619
    • Muthusamy, B.P.1    Natarajan, P.2    Zhou, X.3    Graham, T.R.4
  • 35
    • 67649243778 scopus 로고    scopus 로고
    • The yeast plasma membrane P4-ATPases are major transporters for lysophospholipids
    • Riekhof, W.R.; Voelker, D.R. The yeast plasma membrane P4-ATPases are major transporters for lysophospholipids. Biochim. Biophys. Acta 2009, 1791, 620-627.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 620-627
    • Riekhof, W.R.1    Voelker, D.R.2
  • 37
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins, C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 1992, 8, 67-113.
    • (1992) Annu. Rev. Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 38
    • 2942750350 scopus 로고    scopus 로고
    • ATP-binding cassette (ABC) transporters in human metabolism and diseases
    • Stefkova, J.; Poledne, R.; Hubacek, J.A. ATP-binding cassette (ABC) transporters in human metabolism and diseases. Physiol. Res. 2004, 53, 235-243.
    • (2004) Physiol. Res , vol.53 , pp. 235-243
    • Stefkova, J.1    Poledne, R.2    Hubacek, J.A.3
  • 39
    • 69849099831 scopus 로고    scopus 로고
    • Lipid dependence of ABC transporter localization and function
    • Klappe, K.; Hummel, I.; Hoekstra, D.; Kok, J.W. Lipid dependence of ABC transporter localization and function. Chem. Phys. Lipids 2009, 161, 57-64.
    • (2009) Chem. Phys. Lipids , vol.161 , pp. 57-64
    • Klappe, K.1    Hummel, I.2    Hoekstra, D.3    Kok, J.W.4
  • 41
    • 0001001129 scopus 로고
    • The fine structure of mitochondria
    • Palade, G.E. The fine structure of mitochondria. Anat. Rec. 1952, 114, 427-451.
    • (1952) Anat. Rec , vol.114 , pp. 427-451
    • Palade, G.E.1
  • 42
    • 0345010008 scopus 로고
    • An electron microscope study of the mitochondrial structure
    • Palade, G.E. An electron microscope study of the mitochondrial structure. J. Histochem. Cytochem. 1953, 1, 188-211.
    • (1953) J. Histochem. Cytochem , vol.1 , pp. 188-211
    • Palade, G.E.1
  • 43
    • 34250691686 scopus 로고
    • Electron microscopy of mitochondria and cytoplasmic double membranes
    • Sjostrand, F.S. Electron microscopy of mitochondria and cytoplasmic double membranes. Nature 1953, 171, 30-32.
    • (1953) Nature , vol.171 , pp. 30-32
    • Sjostrand, F.S.1
  • 44
    • 1542457190 scopus 로고
    • Morphology of ordered biological structures
    • Sjostrand, F.S. Morphology of ordered biological structures. Radiat. Res. 1960, Suppl. 2, 349-386.
    • (1960) Radiat. Res , Issue.SUPPL. 2 , pp. 349-386
    • Sjostrand, F.S.1
  • 45
    • 0018399751 scopus 로고
    • Asymmetric distribution of phospholipids in the inner membrane of beef heart mitochondria
    • Krebs, J.J.; Hauser, H.; Carafoli, E. Asymmetric distribution of phospholipids in the inner membrane of beef heart mitochondria. J. Biol. Chem. 1979, 254, 5308-5316.
    • (1979) J. Biol. Chem , vol.254 , pp. 5308-5316
    • Krebs, J.J.1    Hauser, H.2    Carafoli, E.3
  • 46
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum, G. Lipids of mitochondria. Biochim. Biophys. Acta 1985, 822, 1-42.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 1-42
    • Daum, G.1
  • 47
    • 0025091897 scopus 로고
    • Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane
    • Hovius, R.; Lambrechts, H.; Nicolay, K.; de Kruijff, B. Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane. Biochim. Biophys. Acta 1990, 1021, 217-226.
    • (1990) Biochim. Biophys. Acta , vol.1021 , pp. 217-226
    • Hovius, R.1    Lambrechts, H.2    Nicolay, K.3    de Kruijff, B.4
  • 48
    • 0025871358 scopus 로고
    • Mitochondrial membrane contact sites of yeast. Characterization of lipid components and possible involvement in intramitochondrial translocation of phospholipids
    • Simbeni, R.; Pon, L.; Zinser, E.; Paltauf, F.; Daum, G. Mitochondrial membrane contact sites of yeast. Characterization of lipid components and possible involvement in intramitochondrial translocation of phospholipids. J. Biol. Chem. 1991, 266, 10047-10049.
    • (1991) J. Biol. Chem , vol.266 , pp. 10047-10049
    • Simbeni, R.1    Pon, L.2    Zinser, E.3    Paltauf, F.4    Daum, G.5
  • 49
    • 0026082909 scopus 로고
    • Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae
    • Zinser, E.; Sperka-Gottlieb, C.D.; Fasch, E.V.; Kohlwein, S.D.; Paltauf, F.; Daum, G. Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae. J. Bacteriol. 1991, 173, 2026-2034.
    • (1991) J. Bacteriol , vol.173 , pp. 2026-2034
    • Zinser, E.1    Sperka-Gottlieb, C.D.2    Fasch, E.V.3    Kohlwein, S.D.4    Paltauf, F.5    Daum, G.6
  • 50
    • 34247482333 scopus 로고    scopus 로고
    • Cardiolipin: Setting the beat of apoptosis
    • Gonzalvez, F.; Gottlieb, E. Cardiolipin: setting the beat of apoptosis. Apoptosis 2007, 12, 877-885.
    • (2007) Apoptosis , vol.12 , pp. 877-885
    • Gonzalvez, F.1    Gottlieb, E.2
  • 51
    • 0031551023 scopus 로고    scopus 로고
    • Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane?
    • de Kroon, A.I.; Dolis, D.; Mayer, A.; Lill, R.; de Kruijff, B. Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane? Biochim. Biophys. Acta 1997, 1325, 108-116.
    • (1997) Biochim. Biophys. Acta , vol.1325 , pp. 108-116
    • de Kroon, A.I.1    Dolis, D.2    Mayer, A.3    Lill, R.4    de Kruijff, B.5
  • 52
    • 0025534163 scopus 로고
    • Further characterization of mitochondrial contact sites: Effect of short-chain alcohols on membrane fluidity and activity
    • Ardail, D.; Lerme, F.; Louisot, P. Further characterization of mitochondrial contact sites: effect of short-chain alcohols on membrane fluidity and activity. Biochem. Biophys. Res. Commun. 1990, 173, 878-885.
    • (1990) Biochem. Biophys. Res. Commun , vol.173 , pp. 878-885
    • Ardail, D.1    Lerme, F.2    Louisot, P.3
  • 53
    • 48849108199 scopus 로고    scopus 로고
    • The mitochondrial gateway to cell death
    • Smith, D.J.; Ng, H.; Kluck, R.M.; Nagley, P. The mitochondrial gateway to cell death. IUBMB Life 2008, 60, 383-389.
    • (2008) IUBMB Life , vol.60 , pp. 383-389
    • Smith, D.J.1    Ng, H.2    Kluck, R.M.3    Nagley, P.4
  • 55
    • 70349524664 scopus 로고    scopus 로고
    • Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis
    • Schug, Z.T.; Gottlieb, E. Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis. Biochim. Biophys. Acta 2009, 1788, 2022-2031.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2022-2031
    • Schug, Z.T.1    Gottlieb, E.2
  • 56
    • 0037085029 scopus 로고    scopus 로고
    • Sequence and functional similarities between pro-apoptotic Bid and plant lipid transfer proteins
    • Degli Esposti, M. Sequence and functional similarities between pro-apoptotic Bid and plant lipid transfer proteins. Biochim. Biophys. Acta 2002, 1553, 331-340.
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 331-340
    • Degli Esposti, M.1
  • 57
    • 0034795258 scopus 로고    scopus 로고
    • Esposti, M.D.; Erler, J. T.; Hickman, J.A.; Dive, C. Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity. Mol. Cell Biol. 2001, 21, 7268-7276.
    • Esposti, M.D.; Erler, J. T.; Hickman, J.A.; Dive, C. Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity. Mol. Cell Biol. 2001, 21, 7268-7276.
  • 60
    • 0347481136 scopus 로고    scopus 로고
    • Transbilayer lipid diffusion promoted by Bax: Implications for apoptosis
    • Epand, R.F.; Martinou, J.C.; Montessuit, S.; Epand, R.M. Transbilayer lipid diffusion promoted by Bax: implications for apoptosis. Biochemistry 2003, 42, 14576-14582.
    • (2003) Biochemistry , vol.42 , pp. 14576-14582
    • Epand, R.F.1    Martinou, J.C.2    Montessuit, S.3    Epand, R.M.4
  • 62
    • 33846023675 scopus 로고    scopus 로고
    • Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes
    • Epand, R.F.; Schlattner, U.; Wallimann, T.; Lacombe, M.L.; Epand, R.M. Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes. Biophys. J. 2007, 92, 126-137.
    • (2007) Biophys. J , vol.92 , pp. 126-137
    • Epand, R.F.1    Schlattner, U.2    Wallimann, T.3    Lacombe, M.L.4    Epand, R.M.5
  • 63
    • 0037444392 scopus 로고    scopus 로고
    • Phospholipid scramblase 3 is the mitochondrial target of protein kinase C delta-induced apoptosis
    • Liu, J.; Chen, J.; Dai, Q.; Lee, R. M. Phospholipid scramblase 3 is the mitochondrial target of protein kinase C delta-induced apoptosis. Cancer Res. 2003, 63, 1153-1156.
    • (2003) Cancer Res , vol.63 , pp. 1153-1156
    • Liu, J.1    Chen, J.2    Dai, Q.3    Lee, R.M.4
  • 64
    • 0142156049 scopus 로고    scopus 로고
    • Phospholipid scramblase 3 controls mitochondrial structure, function, and apoptotic response
    • Liu, J.; Dai, Q.; Chen, J.; Durrant, D.; Freeman, A.; Liu, T.; Grossman, D.; Lee, R.M. Phospholipid scramblase 3 controls mitochondrial structure, function, and apoptotic response. Mol. Cancer Res. 2003, 1, 892-902.
    • (2003) Mol. Cancer Res , vol.1 , pp. 892-902
    • Liu, J.1    Dai, Q.2    Chen, J.3    Durrant, D.4    Freeman, A.5    Liu, T.6    Grossman, D.7    Lee, R.M.8
  • 65
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter, M.; Fang, M.; Luo, X.; Nishijima, M.; Xie, X.; Wang, X. Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat. Cell Biol. 2000, 2, 754-761.
    • (2000) Nat. Cell Biol , vol.2 , pp. 754-761
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.5    Wang, X.6
  • 66
    • 0034663829 scopus 로고    scopus 로고
    • Wei, M. C.; Lindsten, T.; Mootha, V. K.; Weiler, S.; Gross, A.; Ashiya, M.; Thompson, C. B.; Korsmeyer, S. J. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev. 2000, 14, 2060-2071.
    • Wei, M. C.; Lindsten, T.; Mootha, V. K.; Weiler, S.; Gross, A.; Ashiya, M.; Thompson, C. B.; Korsmeyer, S. J. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev. 2000, 14, 2060-2071.
  • 67
    • 3042723249 scopus 로고    scopus 로고
    • Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome C release
    • Kim, T.H.; Zhao, Y.; Ding, W.X.; Shin, J.N.; He, X.; Seo, Y.W.; Chen, J.; Rabinowich, H.; Amoscato, A.A.; Yin, X.M. Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome C release. Mol. Biol. Cell 2004, 15, 3061-3072.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3061-3072
    • Kim, T.H.1    Zhao, Y.2    Ding, W.X.3    Shin, J.N.4    He, X.5    Seo, Y.W.6    Chen, J.7    Rabinowich, H.8    Amoscato, A.A.9    Yin, X.M.10
  • 70
    • 67849133020 scopus 로고    scopus 로고
    • Cardiolipin-enriched raft-like microdomains are essential activating platforms for apoptotic signals on mitochondria
    • Sorice, M.; Manganelli, V.; Matarrese, P.; Tinari, A.; Misasi, R.; Malorni, W.; Garofalo, T. Cardiolipin-enriched raft-like microdomains are essential activating platforms for apoptotic signals on mitochondria. FEBS Lett. 2009, 583, 2447-2450.
    • (2009) FEBS Lett , vol.583 , pp. 2447-2450
    • Sorice, M.1    Manganelli, V.2    Matarrese, P.3    Tinari, A.4    Misasi, R.5    Malorni, W.6    Garofalo, T.7
  • 73
    • 34249818786 scopus 로고    scopus 로고
    • Attraction of phagocytes by apoptotic cells is mediated by lysophosphatidylcholine
    • Mueller, R.B.; Sheriff, A.; Gaipl, U.S.; Wesselborg, S.; Lauber, K. Attraction of phagocytes by apoptotic cells is mediated by lysophosphatidylcholine. Autoimmunity 2007, 40, 342-344.
    • (2007) Autoimmunity , vol.40 , pp. 342-344
    • Mueller, R.B.1    Sheriff, A.2    Gaipl, U.S.3    Wesselborg, S.4    Lauber, K.5
  • 74
    • 0038218405 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate: An enigmatic signalling lipid
    • Spiegel, S.; Milstien, S. Sphingosine-1-phosphate: an enigmatic signalling lipid. Nat. Rev. Mol. Cell Biol. 2003, 4, 397-407.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 397-407
    • Spiegel, S.1    Milstien, S.2
  • 75
    • 48749121214 scopus 로고    scopus 로고
    • Apoptosis induces expression of sphingosine kinase 1 to release sphingosine-1-phosphate as a "come-and-get-me" signal
    • Gude, D.R.; Alvarez, S. E.; Paugh, S.W.; Mitra, P.; Yu, J.; Griffiths, R.; Barbour, S.E.; Milstien, S.; Spiegel, S. Apoptosis induces expression of sphingosine kinase 1 to release sphingosine-1-phosphate as a "come-and-get-me" signal. FASEB J. 2008, 22, 2629-2638.
    • (2008) FASEB J , vol.22 , pp. 2629-2638
    • Gude, D.R.1    Alvarez, S.E.2    Paugh, S.W.3    Mitra, P.4    Yu, J.5    Griffiths, R.6    Barbour, S.E.7    Milstien, S.8    Spiegel, S.9
  • 77
    • 33644924588 scopus 로고    scopus 로고
    • Involvement of phosphatidylserine, alphavbeta3, CD14, CD36, and complement C1q in the phagocytosis of primary necrotic lymphocytes by macrophages
    • Bottcher, A.; Gaipl, U.S.; Furnrohr, B.G.; Herrmann, M.; Girkontaite, I.; Kalden, J.R.; Voll, R.E. Involvement of phosphatidylserine, alphavbeta3, CD14, CD36, and complement C1q in the phagocytosis of primary necrotic lymphocytes by macrophages. Arthritis Rheum. 2006, 54, 927-938.
    • (2006) Arthritis Rheum , vol.54 , pp. 927-938
    • Bottcher, A.1    Gaipl, U.S.2    Furnrohr, B.G.3    Herrmann, M.4    Girkontaite, I.5    Kalden, J.R.6    Voll, R.E.7
  • 78
    • 36448961645 scopus 로고    scopus 로고
    • Engulfment of apoptotic cells: Signals for a good meal
    • Ravichandran, K.S.; Lorenz, U. Engulfment of apoptotic cells: signals for a good meal. Nat. Rev. Immunol. 2007, 7, 964-974.
    • (2007) Nat. Rev. Immunol , vol.7 , pp. 964-974
    • Ravichandran, K.S.1    Lorenz, U.2
  • 79
    • 0024366194 scopus 로고
    • Effective production of monoclonal antibodies against phosphatidylserine: Stereo-specific recognition of phosphatidylserine by monoclonal antibody
    • Umeda, M.; Igarashi, K.; Nam, K.S.; Inoue, K. Effective production of monoclonal antibodies against phosphatidylserine: stereo-specific recognition of phosphatidylserine by monoclonal antibody. J. Immunol. 1989, 143, 2273-2279.
    • (1989) J. Immunol , vol.143 , pp. 2273-2279
    • Umeda, M.1    Igarashi, K.2    Nam, K.S.3    Inoue, K.4
  • 80
    • 0037046580 scopus 로고    scopus 로고
    • Identification of a factor that links apoptotic cells to phagocytes
    • Hanayama, R.; Tanaka, M.; Miwa, K.; Shinohara, A.; Iwamatsu, A.; Nagata, S. Identification of a factor that links apoptotic cells to phagocytes. Nature 2002, 417, 182-187.
    • (2002) Nature , vol.417 , pp. 182-187
    • Hanayama, R.1    Tanaka, M.2    Miwa, K.3    Shinohara, A.4    Iwamatsu, A.5    Nagata, S.6
  • 82
    • 0032582647 scopus 로고    scopus 로고
    • Characterization of phosphatidylserine-dependent beta2-glycoprotein I macrophage interactions. Implications for apoptotic cell clearance by phagocytes
    • Balasubramanian, K.; Schroit, A.J. Characterization of phosphatidylserine-dependent beta2-glycoprotein I macrophage interactions. Implications for apoptotic cell clearance by phagocytes. J. Biol. Chem. 1998, 273, 29272-29277.
    • (1998) J. Biol. Chem , vol.273 , pp. 29272-29277
    • Balasubramanian, K.1    Schroit, A.J.2
  • 83
    • 5444239857 scopus 로고    scopus 로고
    • Innate immune and non-immune mediators of erythrocyte clearance
    • Lutz, H.U. Innate immune and non-immune mediators of erythrocyte clearance. Cell. Mol. Biol. (Noisy-le-grand) 2004, 50, 107-116.
    • (2004) Cell. Mol. Biol. (Noisy-le-grand) , vol.50 , pp. 107-116
    • Lutz, H.U.1
  • 84
    • 20244362188 scopus 로고    scopus 로고
    • Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells
    • Anderson, H.A.; Maylock, C.A.; Williams, J.A.; Paweletz, C.P.; Shu, H.; Shacter, E. Serum-derived protein S binds to phosphatidylserine and stimulates the phagocytosis of apoptotic cells. Nat. Immunol. 2003, 4, 87-91.
    • (2003) Nat. Immunol , vol.4 , pp. 87-91
    • Anderson, H.A.1    Maylock, C.A.2    Williams, J.A.3    Paweletz, C.P.4    Shu, H.5    Shacter, E.6
  • 86
    • 0028997232 scopus 로고
    • The class B scavenger receptors SR-BI and CD36 are receptors for anionic phospholipids
    • Rigotti, A.; Acton, S.L.; Krieger, M. The class B scavenger receptors SR-BI and CD36 are receptors for anionic phospholipids. J. Biol. Chem. 1995, 270, 16221-16224.
    • (1995) J. Biol. Chem , vol.270 , pp. 16221-16224
    • Rigotti, A.1    Acton, S.L.2    Krieger, M.3
  • 92
    • 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, G.G.; Casasnovas, J.M. 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
  • 93
    • 0037072936 scopus 로고    scopus 로고
    • FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and angiogenesis-modulating activities
    • Adachi, H.; Tsujimoto, M. FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and angiogenesis-modulating activities. J. Biol. Chem. 2002, 277, 34264-34270.
    • (2002) J. Biol. Chem , vol.277 , pp. 34264-34270
    • Adachi, H.1    Tsujimoto, M.2
  • 95
    • 0346216136 scopus 로고    scopus 로고
    • Expression of stabilin-2, a novel fasciclin-like hyaluronan receptor protein, in murine sinusoidal endothelia, avascular tissues, and at solid/liquid interfaces
    • Falkowski, M.; Schledzewski, K.; Hansen, B.; Goerdt, S. Expression of stabilin-2, a novel fasciclin-like hyaluronan receptor protein, in murine sinusoidal endothelia, avascular tissues, and at solid/liquid interfaces. Histochem. Cell Biol. 2003, 120, 361-369.
    • (2003) Histochem. Cell Biol , vol.120 , pp. 361-369
    • Falkowski, M.1    Schledzewski, K.2    Hansen, B.3    Goerdt, S.4
  • 97
    • 50249133197 scopus 로고    scopus 로고
    • Epidermal growth factor-like domain repeat of stabilin-2 recognizes phosphatidylserine during cell corpse clearance
    • Park, S.Y.; Kim, S.Y.; Jung, M.Y.; Bae, D.J.; Kim, I.S. Epidermal growth factor-like domain repeat of stabilin-2 recognizes phosphatidylserine during cell corpse clearance. Mol. Cell. Biol. 2008, 28, 5288-5298.
    • (2008) Mol. Cell. Biol , vol.28 , pp. 5288-5298
    • Park, S.Y.1    Kim, S.Y.2    Jung, M.Y.3    Bae, D.J.4    Kim, I.S.5
  • 101
    • 32144441221 scopus 로고    scopus 로고
    • Dock180-ELMO cooperation in Rac activation
    • Lu, M.; Ravichandran, K.S. Dock180-ELMO cooperation in Rac activation. Methods Enzymol. 2006, 406, 388-402.
    • (2006) Methods Enzymol , vol.406 , pp. 388-402
    • Lu, M.1    Ravichandran, K.S.2
  • 106
    • 0036143018 scopus 로고    scopus 로고
    • Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation
    • Huynh, M.L.; Fadok, V.A.; Henson, P.M. 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
  • 109
    • 0031838606 scopus 로고    scopus 로고
    • Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus
    • Herrmann, M.; Voll, R.E.; Zoller, O.M.; Hagenhofer, M.; Ponner, B.B.; Kalden, J.R. 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
  • 110
    • 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, R.E.; Manger, B.; Gaipl, U.; Neuhuber, W.L.; Kirchner, T.; Kalden, J.R.; Herrmann, M. 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    Kirchner, T.7    Kalden, J.R.8    Herrmann, M.9
  • 113
    • 0029300651 scopus 로고
    • Annexin homologues in Giardia lamblia
    • Fiedler, K.; Simons, K. Annexin homologues in Giardia lamblia. Trends Biochem. Sci. 1995, 20, 177-178.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 177-178
    • Fiedler, K.1    Simons, K.2
  • 116
    • 0026575572 scopus 로고
    • Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins
    • Huber, R.; Berendes, R.; Burger, A.; Schneider, M.; Karshikov, A.; Luecke, H.; Romisch, J.; Paques, E. Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins. J. Mol. Biol. 1992, 223, 683-704.
    • (1992) J. Mol. Biol , vol.223 , pp. 683-704
    • Huber, R.1    Berendes, R.2    Burger, A.3    Schneider, M.4    Karshikov, A.5    Luecke, H.6    Romisch, J.7    Paques, E.8
  • 117
    • 0025000276 scopus 로고
    • The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes
    • Huber, R.; Romisch, J.; Paques, E.P. The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes. EMBO J. 1990, 9, 3867-3874.
    • (1990) EMBO J , vol.9 , pp. 3867-3874
    • Huber, R.1    Romisch, J.2    Paques, E.P.3
  • 118
    • 0025038549 scopus 로고
    • The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity
    • Huber, R.; Schneider, M.; Mayr, I.; Romisch, J.; Paques, E.P. The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity. FEBS Lett. 1990, 275, 15-21.
    • (1990) FEBS Lett , vol.275 , pp. 15-21
    • Huber, R.1    Schneider, M.2    Mayr, I.3    Romisch, J.4    Paques, E.P.5
  • 119
    • 0027989808 scopus 로고
    • Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis
    • Koopman, G.; Reutelingsperger, C.P.; Kuijten, G.A.; Keehnen, R.M.; Pals, S.T.; van Oers, M.H. Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis. Blood 1994, 84, 1415-1420.
    • (1994) Blood , vol.84 , pp. 1415-1420
    • Koopman, G.1    Reutelingsperger, C.P.2    Kuijten, G.A.3    Keehnen, R.M.4    Pals, S.T.5    van Oers, M.H.6
  • 120
    • 39749123276 scopus 로고    scopus 로고
    • Apoptosis and necrosis: Detection, discrimination and phagocytosis
    • Krysko, D.V.; Vanden Berghe, T.; D'Herde, K.; Vandenabeele, P. Apoptosis and necrosis: detection, discrimination and phagocytosis. Methods 2008, 44, 205-221.
    • (2008) Methods , vol.44 , pp. 205-221
    • Krysko, D.V.1    Vanden Berghe, T.2    D'Herde, K.3    Vandenabeele, P.4
  • 121
    • 0032402088 scopus 로고    scopus 로고
    • Binding of annexin V to bilayers with various phospholipid compositions using glass beads in a flow cytometer
    • Stuart, M.C.; Reutelingsperger, C.P.; Frederik, P.M. Binding of annexin V to bilayers with various phospholipid compositions using glass beads in a flow cytometer. Cytometry 1998, 33, 414-419.
    • (1998) Cytometry , vol.33 , pp. 414-419
    • Stuart, M.C.1    Reutelingsperger, C.P.2    Frederik, P.M.3
  • 122
    • 0022387184 scopus 로고
    • Isolation and partial purification of a novel anticoagulant from arteries of human umbilical cord
    • Reutelingsperger, C.P.; Hornstra, G.; Hemker, H.C. Isolation and partial purification of a novel anticoagulant from arteries of human umbilical cord. Eur. J. Biochem. 1985, 151, 625-629.
    • (1985) Eur. J. Biochem , vol.151 , pp. 625-629
    • Reutelingsperger, C.P.1    Hornstra, G.2    Hemker, H.C.3
  • 123
    • 0023914085 scopus 로고
    • Purification and characterization of a novel protein from bovine aorta that inhibits coagulation. Inhibition of the phospholipid-dependent factor-Xa-catalyzed prothrombin activation, through a high-affinity binding of the anticoagulant to the phospholipids
    • Reutelingsperger, C.P.; Kop, J.M.; Hornstra, G.; Hemker, H.C. Purification and characterization of a novel protein from bovine aorta that inhibits coagulation. Inhibition of the phospholipid-dependent factor-Xa-catalyzed prothrombin activation, through a high-affinity binding of the anticoagulant to the phospholipids. Eur. J. Biochem. 1988, 173, 171-178.
    • (1988) Eur. J. Biochem , vol.173 , pp. 171-178
    • Reutelingsperger, C.P.1    Kop, J.M.2    Hornstra, G.3    Hemker, H.C.4
  • 126
    • 34247105815 scopus 로고    scopus 로고
    • Fibrinogen and fibrin: Scaffold proteins in hemostasis
    • Lord, S.T. Fibrinogen and fibrin: scaffold proteins in hemostasis. Curr. Opin. Hematol. 2007, 14, 236-241.
    • (2007) Curr. Opin. Hematol , vol.14 , pp. 236-241
    • Lord, S.T.1
  • 129
    • 14044277623 scopus 로고    scopus 로고
    • Annexin A5 down-regulates surface expression of tissue factor: A novel mechanism of regulating the membrane receptor repertoir
    • Ravassa, S.; Bennaghmouch, A.; Kenis, H.; Lindhout, T.; Hackeng, T.; Narula, J.; Hofstra, L.; Reutelingsperger, C. Annexin A5 down-regulates surface expression of tissue factor: a novel mechanism of regulating the membrane receptor repertoir. J. Biol. Chem. 2005, 280, 6028-6035.
    • (2005) J. Biol. Chem , vol.280 , pp. 6028-6035
    • Ravassa, S.1    Bennaghmouch, A.2    Kenis, H.3    Lindhout, T.4    Hackeng, T.5    Narula, J.6    Hofstra, L.7    Reutelingsperger, C.8
  • 130
    • 0035193527 scopus 로고    scopus 로고
    • Sequential expression of annexin A5 in the vasculature and skeletal elements during mouse development
    • Brachvogel, B.; Welzel, H.; Moch, H.; von der Mark, K.; Hofmann, C.; Poschl, E. Sequential expression of annexin A5 in the vasculature and skeletal elements during mouse development. Mech. Dev. 2001, 109, 389-393.
    • (2001) Mech. Dev , vol.109 , pp. 389-393
    • Brachvogel, B.1    Welzel, H.2    Moch, H.3    von der Mark, K.4    Hofmann, C.5    Poschl, E.6


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