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Volumn 54, Issue 4, 2010, Pages 246-253

Plasma lipoproteins are important components of the immune system

Author keywords

Infection; Innate immunity; Lipoprotein(a); Plasma lipoprotein

Indexed keywords

HIGH DENSITY LIPOPROTEIN; LIPOPROTEIN A; LOW DENSITY LIPOPROTEIN; OXIDIZED LOW DENSITY LIPOPROTEIN; VERY LOW DENSITY LIPOPROTEIN;

EID: 77951074137     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2010.00203.x     Document Type: Review
Times cited : (57)

References (84)
  • 1
    • 0346752261 scopus 로고    scopus 로고
    • High cholesterol may protect against infections and atherosclerosis
    • Ravnskov U. (2003) High cholesterol may protect against infections and atherosclerosis. QJM 96: 927-34.
    • (2003) QJM , vol.96 , pp. 927-934
    • Ravnskov, U.1
  • 2
    • 0038447123 scopus 로고    scopus 로고
    • Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock
    • Van Amersfoort E.S., Van Berkel T.J., Kuiper J. (2003) Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock. Clin Microbiol Rev 16: 379-414.
    • (2003) Clin Microbiol Rev , vol.16 , pp. 379-414
    • van Amersfoort, E.S.1    van Berkel, T.J.2    Kuiper, J.3
  • 3
    • 3042606551 scopus 로고    scopus 로고
    • Effects of infection and inflammation on lipid and lipoprotein metabolism: Mechanisms and consequences to the host
    • Khovidhunkit W., Kim M.S., Memon R.A., Shigenaga J.K., Moser A.H., Feingold K.R., Grunfeld C. (2004) Effects of infection and inflammation on lipid and lipoprotein metabolism: mechanisms and consequences to the host. J Lipid Res 45: 1169-96.
    • (2004) J Lipid Res , vol.45 , pp. 1169-1196
    • Khovidhunkit, W.1    Kim, M.S.2    Memon, R.A.3    Shigenaga, J.K.4    Moser, A.H.5    Feingold, K.R.6    Grunfeld, C.7
  • 8
    • 0020631194 scopus 로고
    • Binding and partial inactivation of Staphylococcus aureus alpha-toxin by human plasma low density lipoprotein
    • Bhakdi S., Tranum-Jensen J., Utermann G., Fussle R. (1983) Binding and partial inactivation of Staphylococcus aureus alpha-toxin by human plasma low density lipoprotein. J Biol Chem 258: 5899-904.
    • (1983) J Biol Chem , vol.258 , pp. 5899-5904
    • Bhakdi, S.1    Tranum-Jensen, J.2    Utermann, G.3    Fussle, R.4
  • 10
    • 25444468813 scopus 로고    scopus 로고
    • Human high density lipoproteins are platforms for the assembly of multi-component innate immune complexes
    • Shiflett A.M., Bishop J.R., Pahwa A., Hajduk S.L. (2005) Human high density lipoproteins are platforms for the assembly of multi-component innate immune complexes. J Biol Chem 280: 32578-85.
    • (2005) J Biol Chem , vol.280 , pp. 32578-32585
    • Shiflett, A.M.1    Bishop, J.R.2    Pahwa, A.3    Hajduk, S.L.4
  • 12
    • 0037026527 scopus 로고    scopus 로고
    • Protective role of phospholipid oxidation products in endotoxin-induced tissue damage
    • Bochkov V.N., Kadl A., Huber J., Gruber F., Binder B.R., Leitinger N. (2002) Protective role of phospholipid oxidation products in endotoxin-induced tissue damage. Nature 419: 77-81.
    • (2002) Nature , vol.419 , pp. 77-81
    • Bochkov, V.N.1    Kadl, A.2    Huber, J.3    Gruber, F.4    Binder, B.R.5    Leitinger, N.6
  • 13
    • 0037449723 scopus 로고    scopus 로고
    • Minimally modified LDL binds to CD14, induces macrophage spreading via TLR4/MD-2, and inhibits phagocytosis of apoptotic cells
    • Miller Y.I., Viriyakosol S., Binder C.J., Feramisco J.R., Kirkland T.N., Witztum J.L. (2003) Minimally modified LDL binds to CD14, induces macrophage spreading via TLR4/MD-2, and inhibits phagocytosis of apoptotic cells. J Biol Chem 278: 1561-68.
    • (2003) J Biol Chem , vol.278 , pp. 1561-1568
    • Miller, Y.I.1    Viriyakosol, S.2    Binder, C.J.3    Feramisco, J.R.4    Kirkland, T.N.5    Witztum, J.L.6
  • 15
    • 0036096132 scopus 로고    scopus 로고
    • Oxidized phospholipids stimulate tissue factor expression in human endothelial cells via activation of ERK/EGR-1 and Ca++/NFAT
    • Bochkov V.N., Mechtcheriakova D., Lucerna M., Huber J., Malli R., Graier W.F., Hofer E., Binder B.R., Leitinger N. (2002) Oxidized phospholipids stimulate tissue factor expression in human endothelial cells via activation of ERK/EGR-1 and Ca++/NFAT. Blood 99: 199-206.
    • (2002) Blood , vol.99 , pp. 199-206
    • Bochkov, V.N.1    Mechtcheriakova, D.2    Lucerna, M.3    Huber, J.4    Malli, R.5    Graier, W.F.6    Hofer, E.7    Binder, B.R.8    Leitinger, N.9
  • 16
    • 59249090135 scopus 로고    scopus 로고
    • Trypanosome lytic factor, an antimicrobial high-density lipoprotein, ameliorates Leishmania infection
    • Samanovic M., Molina-Portela M.P., Chessler A.D., Burleigh B.A., Raper J. (2009) Trypanosome lytic factor, an antimicrobial high-density lipoprotein, ameliorates Leishmania infection. PLoS Pathog 5: e1000276.
    • (2009) PLoS Pathog , vol.5
    • Samanovic, M.1    Molina-Portela, M.P.2    Chessler, A.D.3    Burleigh, B.A.4    Raper, J.5
  • 17
    • 33646829831 scopus 로고    scopus 로고
    • Serum opacity factor, a streptococcal virulence factor that binds to apolipoproteins A-I and A-II and disrupts high density lipoprotein structure
    • Courtney H.S., Zhang Y.-M., Frank M.W., Rock C.O. (2006) Serum opacity factor, a streptococcal virulence factor that binds to apolipoproteins A-I and A-II and disrupts high density lipoprotein structure. J Biol Chem 281: 5515-21.
    • (2006) J Biol Chem , vol.281 , pp. 5515-5521
    • Courtney, H.S.1    Zhang, Y.-M.2    Frank, M.W.3    Rock, C.O.4
  • 18
    • 0025186067 scopus 로고
    • Apolipoprotein A-I and its amphipathic helix peptide analogues inhibit human immunodeficiency virus-induced syncytium formation
    • Owens B.J., Anantharamaiah G.M., Kahlon J.B., Srinivas R.V., Compans R.W., Segrest J.P. (1990) Apolipoprotein A-I and its amphipathic helix peptide analogues inhibit human immunodeficiency virus-induced syncytium formation. J Clin Invest 86: 1142-50.
    • (1990) J Clin Invest , vol.86 , pp. 1142-1150
    • Owens, B.J.1    Anantharamaiah, G.M.2    Kahlon, J.B.3    Srinivas, R.V.4    Compans, R.W.5    Segrest, J.P.6
  • 19
  • 22
    • 20744437263 scopus 로고    scopus 로고
    • An interplay between hypervariable region 1 of the hepatitis C virus E2 glycoprotein, the scavenger receptor BI, and high-density lipoprotein promotes both enhancement of infection and protection against neutralizing antibodies
    • Bartosch B., Verney G., Dreux M., Donot P., Morice Y., Penin F., Pawlotsky J.M., Lavillette D., Cosset F.L. (2005) An interplay between hypervariable region 1 of the hepatitis C virus E2 glycoprotein, the scavenger receptor BI, and high-density lipoprotein promotes both enhancement of infection and protection against neutralizing antibodies. J Virol 79: 8217-29.
    • (2005) J Virol , vol.79 , pp. 8217-8229
    • Bartosch, B.1    Verney, G.2    Dreux, M.3    Donot, P.4    Morice, Y.5    Penin, F.6    Pawlotsky, J.M.7    Lavillette, D.8    Cosset, F.L.9
  • 23
    • 14844337450 scopus 로고    scopus 로고
    • High density lipoproteins facilitate hepatitis C virus entry through the scavenger receptor class B type I
    • Voisset C., Callens N., Blanchard E., Op De Beeck A., Dubuisson J., Vu-Dac N. (2005) High density lipoproteins facilitate hepatitis C virus entry through the scavenger receptor class B type I. J Biol Chem 280: 7793-9.
    • (2005) J Biol Chem , vol.280 , pp. 7793-7799
    • Voisset, C.1    Callens, N.2    Blanchard, E.3    Op de Beeck, A.4    Dubuisson, J.5    Vu-Dac, N.6
  • 26
    • 58949091106 scopus 로고    scopus 로고
    • Apolipoprotein A-II augments monocyte responses to LPS by suppressing the inhibitory activity of LPS-binding protein
    • Thompson P.A., Berbee J.F., Rensen P.C., Kitchens R.L. (2008) Apolipoprotein A-II augments monocyte responses to LPS by suppressing the inhibitory activity of LPS-binding protein. Innate Immun 14: 365-74.
    • (2008) Innate Immun , vol.14 , pp. 365-374
    • Thompson, P.A.1    Berbee, J.F.2    Rensen, P.C.3    Kitchens, R.L.4
  • 30
    • 0142091765 scopus 로고    scopus 로고
    • pH6 antigen of Yersinia pestis interacts with plasma lipoproteins and cell membranes
    • Makoveichuk E., Cherepanov P., Lundberg S., Forsberg A., Olivecrona G. (2003) pH6 antigen of Yersinia pestis interacts with plasma lipoproteins and cell membranes. J Lipid Res 44: 320-30.
    • (2003) J Lipid Res , vol.44 , pp. 320-330
    • Makoveichuk, E.1    Cherepanov, P.2    Lundberg, S.3    Forsberg, A.4    Olivecrona, G.5
  • 32
    • 0031687891 scopus 로고    scopus 로고
    • Apolipoprotein E-deficient mice have impaired innate immune responses to Listeria monocytogenes in vivo
    • Roselaar S.E., Daugherty A. (1998) Apolipoprotein E-deficient mice have impaired innate immune responses to Listeria monocytogenes in vivo. J Lipid Res 39: 1740-3.
    • (1998) J Lipid Res , vol.39 , pp. 1740-1743
    • Roselaar, S.E.1    Daugherty, A.2
  • 36
    • 0035284803 scopus 로고    scopus 로고
    • Hypercholesterolemia exacerbates virus-induced immunopathologic liver disease via suppression of antiviral cytotoxic T cell responses
    • Ludewig B., Jaggi M., Dumrese T., Brduscha-Riem K., Odermatt B., Hengartner H., Zinkernagel R.M. (2001) Hypercholesterolemia exacerbates virus-induced immunopathologic liver disease via suppression of antiviral cytotoxic T cell responses. J Immunol 166: 3369-76.
    • (2001) J Immunol , vol.166 , pp. 3369-3376
    • Ludewig, B.1    Jaggi, M.2    Dumrese, T.3    Brduscha-Riem, K.4    Odermatt, B.5    Hengartner, H.6    Zinkernagel, R.M.7
  • 37
    • 0030954099 scopus 로고    scopus 로고
    • Hyperlipoproteinemia enhances susceptibility to acute disseminated Candida albicans infection in low-density-lipoprotein-receptor-deficient mice
    • Netea M.G., Demacker P.N., De Bont N., Boerman O.C., Stalenhoef A.F., Van Der Meer J.W., Kullberg B.J. (1997) Hyperlipoproteinemia enhances susceptibility to acute disseminated Candida albicans infection in low-density-lipoprotein-receptor-deficient mice. Infect Immun 65: 2663-7.
    • (1997) Infect Immun , vol.65 , pp. 2663-2667
    • Netea, M.G.1    Demacker, P.N.2    de Bont, N.3    Boerman, O.C.4    Stalenhoef, A.F.5    van der Meer, J.W.6    Kullberg, B.J.7
  • 42
    • 42149133781 scopus 로고    scopus 로고
    • The periodontal pathogen Porphyromonas gingivalis cleaves apoB-100 and increases the expression of apoM in LDL in whole blood leading to cell proliferation
    • Bengtsson T., Karlsson H., Gunnarsson P., Skoglund C., Elison C., Leanderson P., Lindahl M. (2008) The periodontal pathogen Porphyromonas gingivalis cleaves apoB-100 and increases the expression of apoM in LDL in whole blood leading to cell proliferation. J Intern Med 263: 558-71.
    • (2008) J Intern Med , vol.263 , pp. 558-571
    • Bengtsson, T.1    Karlsson, H.2    Gunnarsson, P.3    Skoglund, C.4    Elison, C.5    Leanderson, P.6    Lindahl, M.7
  • 44
    • 16344380083 scopus 로고    scopus 로고
    • Inherent specificities in natural antibodies: A key to immune defense against pathogen invasion
    • Baumgarth N., Tung J.W., Herzenberg L.A. (2005) Inherent specificities in natural antibodies: a key to immune defense against pathogen invasion. Springer Semin Immunopathol 26: 347-62.
    • (2005) Springer Semin Immunopathol , vol.26 , pp. 347-362
    • Baumgarth, N.1    Tung, J.W.2    Herzenberg, L.A.3
  • 46
    • 0030969856 scopus 로고    scopus 로고
    • Detection of the phosphorylcholine epitope in streptococci, Haemophilus and pathogenic Neisseriae by immunoblotting
    • Kolberg J., Hoiby E.A., Jantzen E. (1997) Detection of the phosphorylcholine epitope in streptococci, Haemophilus and pathogenic Neisseriae by immunoblotting. Microb Pathog 22: 321-9.
    • (1997) Microb Pathog , vol.22 , pp. 321-329
    • Kolberg, J.1    Hoiby, E.A.2    Jantzen, E.3
  • 47
    • 0031695884 scopus 로고    scopus 로고
    • The phosphorylcholine epitope undergoes phase variation on a 43-kilodalton protein in Pseudomonas aeruginosa and on pili of Neisseria meningitidis and Neisseria gonorrhoeae
    • Weiser J.N., Goldberg J.B., Pan N., Wilson L., Virji M. (1998) The phosphorylcholine epitope undergoes phase variation on a 43-kilodalton protein in Pseudomonas aeruginosa and on pili of Neisseria meningitidis and Neisseria gonorrhoeae. Infect Immun 66: 4263-7.
    • (1998) Infect Immun , vol.66 , pp. 4263-4267
    • Weiser, J.N.1    Goldberg, J.B.2    Pan, N.3    Wilson, L.4    Virji, M.5
  • 48
    • 0032997668 scopus 로고    scopus 로고
    • Phosphorylcholine: Friend or foe of the immune system?
    • Harnett W., Harnett M.M. (1999) Phosphorylcholine: friend or foe of the immune system? Immunol Today 20: 125-9.
    • (1999) Immunol Today , vol.20 , pp. 125-129
    • Harnett, W.1    Harnett, M.M.2
  • 49
    • 0036170629 scopus 로고    scopus 로고
    • Genetic and functional analysis of the phosphorylcholine moiety of commensal Neisseria lipopolysaccharide
    • Serino L., Virji M. (2002) Genetic and functional analysis of the phosphorylcholine moiety of commensal Neisseria lipopolysaccharide. Mol Microbiol 43: 437-48.
    • (2002) Mol Microbiol , vol.43 , pp. 437-448
    • Serino, L.1    Virji, M.2
  • 50
    • 0037097803 scopus 로고    scopus 로고
    • Protection from Streptococcus pneumoniae infection by C-reactive protein and natural antibody requires complement but not Fc gamma receptors
    • Mold C., Rodic-Polic B., Du Clos T.W. (2002) Protection from Streptococcus pneumoniae infection by C-reactive protein and natural antibody requires complement but not Fc gamma receptors. J Immunol 168: 6375-81.
    • (2002) J Immunol , vol.168 , pp. 6375-6381
    • Mold, C.1    Rodic-Polic, B.2    du Clos, T.W.3
  • 53
    • 4644279864 scopus 로고    scopus 로고
    • Cross-reactivity of human immunoglobulin G2 recognizing phosphorylcholine and evidence for protection against major bacterial pathogens of the human respiratory tract
    • Goldenberg H.B., Mccool T.L., Weiser J.N. (2004) Cross-reactivity of human immunoglobulin G2 recognizing phosphorylcholine and evidence for protection against major bacterial pathogens of the human respiratory tract. J Infect Dis 190: 1254-63.
    • (2004) J Infect Dis , vol.190 , pp. 1254-1263
    • Goldenberg, H.B.1    McCool, T.L.2    Weiser, J.N.3
  • 54
    • 0036839674 scopus 로고    scopus 로고
    • Opsonization of Actinobacillus actinomycetemcomitans by immunoglobulin G antibody reactive with phosphorylcholine
    • Purkall D., Tew J.G., Schenkein H.A. (2002) Opsonization of Actinobacillus actinomycetemcomitans by immunoglobulin G antibody reactive with phosphorylcholine. Infect Immun 70: 6485-8.
    • (2002) Infect Immun , vol.70 , pp. 6485-6488
    • Purkall, D.1    Tew, J.G.2    Schenkein, H.A.3
  • 55
    • 0033976515 scopus 로고    scopus 로고
    • Bacterial phosphorylcholine decreases susceptibility to the antimicrobial peptide LL-37/hCAP18 expressed in the upper respiratory tract
    • Lysenko E.S., Gould J., Bals R., Wilson J.M., Weiser J.N. (2000) Bacterial phosphorylcholine decreases susceptibility to the antimicrobial peptide LL-37/hCAP18 expressed in the upper respiratory tract. Infect Immun 68: 1664-71.
    • (2000) Infect Immun , vol.68 , pp. 1664-1671
    • Lysenko, E.S.1    Gould, J.2    Bals, R.3    Wilson, J.M.4    Weiser, J.N.5
  • 56
    • 0032536372 scopus 로고    scopus 로고
    • Phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae contributes to persistence in the respiratory tract and sensitivity to serum killing mediated by C-reactive protein
    • Weiser J.N., Pan N., Mcgowan K.L., Musher D., Martin A., Richards J. (1998) Phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae contributes to persistence in the respiratory tract and sensitivity to serum killing mediated by C-reactive protein. J Exp Med 187: 631-40.
    • (1998) J Exp Med , vol.187 , pp. 631-640
    • Weiser, J.N.1    Pan, N.2    McGowan, K.L.3    Musher, D.4    Martin, A.5    Richards, J.6
  • 57
    • 0033977680 scopus 로고    scopus 로고
    • The position of phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae affects binding and sensitivity to C-reactive protein-mediated killing
    • Lysenko E., Richards J.C., Cox A.D., Stewart A., Martin A., Kapoor M., Weiser J.N. (2000) The position of phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae affects binding and sensitivity to C-reactive protein-mediated killing. Mol Microbiol 35: 234-45.
    • (2000) Mol Microbiol , vol.35 , pp. 234-245
    • Lysenko, E.1    Richards, J.C.2    Cox, A.D.3    Stewart, A.4    Martin, A.5    Kapoor, M.6    Weiser, J.N.7
  • 58
    • 0342939538 scopus 로고    scopus 로고
    • Natural antibodies with the T15 idiotype may act in atherosclerosis, apoptotic clearance, and protective immunity
    • Shaw P.X., Horkko S., Chang M.K., Curtiss L.K., Palinski W., Silverman G.J., Witztum J.L. (2000) Natural antibodies with the T15 idiotype may act in atherosclerosis, apoptotic clearance, and protective immunity. J Clin Invest 105: 1731-40.
    • (2000) J Clin Invest , vol.105 , pp. 1731-1740
    • Shaw, P.X.1    Horkko, S.2    Chang, M.K.3    Curtiss, L.K.4    Palinski, W.5    Silverman, G.J.6    Witztum, J.L.7
  • 62
    • 7544229779 scopus 로고    scopus 로고
    • Are anti-oxidized low-density lipoprotein antibodies pathogenic or protective?
    • Shoenfeld Y., Wu R., Dearing L.D., Matsuura E. (2004) Are anti-oxidized low-density lipoprotein antibodies pathogenic or protective? Circulation 110: 2552-58.
    • (2004) Circulation , vol.110 , pp. 2552-2558
    • Shoenfeld, Y.1    Wu, R.2    Dearing, L.D.3    Matsuura, E.4
  • 63
    • 33644620371 scopus 로고    scopus 로고
    • Mildly oxidized low-density lipoprotein inhibits the in vitro induction of the specific antibody response to Candida albicans
    • Giordani L., Mattioli B., Quaranta M.G., Giacomini E., Libri I., Vari R., Masella R., Viora M. (2005) Mildly oxidized low-density lipoprotein inhibits the in vitro induction of the specific antibody response to Candida albicans. Free Radic Biol Med 39: 960-9.
    • (2005) Free Radic Biol Med , vol.39 , pp. 960-969
    • Giordani, L.1    Mattioli, B.2    Quaranta, M.G.3    Giacomini, E.4    Libri, I.5    Vari, R.6    Masella, R.7    Viora, M.8
  • 64
    • 69749086971 scopus 로고    scopus 로고
    • Lipoprotein(a): Biology and clinical importance
    • Mccormick S.P. (2004) Lipoprotein(a): biology and clinical importance. Clin Biochem Rev 25: 69-80.
    • (2004) Clin Biochem Rev , vol.25 , pp. 69-80
    • McCormick, S.P.1
  • 65
    • 10644264549 scopus 로고    scopus 로고
    • Lipoprotein(a): An elusive cardiovascular risk factor
    • Berglund L., Ramakrishnan R. (2004) Lipoprotein(a): an elusive cardiovascular risk factor. Arterioscler Thromb Vasc Biol 24: 2219-26.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 2219-2226
    • Berglund, L.1    Ramakrishnan, R.2
  • 66
    • 33845411733 scopus 로고    scopus 로고
    • Novel insights into Lp(a) physiology and pathogenicity: More questions than answers?
    • Koschinsky M.L. (2006) Novel insights into Lp(a) physiology and pathogenicity: more questions than answers? Cardiovasc Hematol Disord Drug Targets 6: 267-78.
    • (2006) Cardiovasc Hematol Disord Drug Targets , vol.6 , pp. 267-278
    • Koschinsky, M.L.1
  • 67
    • 33750816249 scopus 로고    scopus 로고
    • Lipoprotein(a): A unique risk factor for cardiovascular disease
    • Anuurad E., Boffa M.B., Koschinsky M.L., Berglund L. (2006) Lipoprotein(a): a unique risk factor for cardiovascular disease. Clin Lab Med 26: 751-72.
    • (2006) Clin Lab Med , vol.26 , pp. 751-772
    • Anuurad, E.1    Boffa, M.B.2    Koschinsky, M.L.3    Berglund, L.4
  • 68
    • 0033970155 scopus 로고    scopus 로고
    • Lipoprotein(a): From ancestral benefit to modern pathogen?
    • Lippi G., Guidi G. (2000) Lipoprotein(a): from ancestral benefit to modern pathogen? QJM 93: 75-84.
    • (2000) QJM , vol.93 , pp. 75-84
    • Lippi, G.1    Guidi, G.2
  • 69
    • 60549101700 scopus 로고    scopus 로고
    • A physiological function for apolipoprotein(a): A natural regulator of the inflammatory response
    • Hoover-Plow J., Hart E., Gong Y., Shchurin A., Schneeman T. (2009) A physiological function for apolipoprotein(a): a natural regulator of the inflammatory response. Exp Biol Med 234: 28-34.
    • (2009) Exp Biol Med , vol.234 , pp. 28-34
    • Hoover-Plow, J.1    Hart, E.2    Gong, Y.3    Shchurin, A.4    Schneeman, T.5
  • 71
    • 12944325306 scopus 로고    scopus 로고
    • Bacterial metastasis: The host plasminogen system in bacterial invasion
    • Lahteenmaki K., Edelman S., Korhonen T.K. (2005) Bacterial metastasis: the host plasminogen system in bacterial invasion. Trends Microbiol 13: 79-85.
    • (2005) Trends Microbiol , vol.13 , pp. 79-85
    • Lahteenmaki, K.1    Edelman, S.2    Korhonen, T.K.3
  • 72
    • 33746619204 scopus 로고    scopus 로고
    • The interaction between pathogens and the host coagulation system
    • Sun H. (2006) The interaction between pathogens and the host coagulation system. Physiology (Bethesda) 21: 281-8.
    • (2006) Physiology (Bethesda) , vol.21 , pp. 281-288
    • Sun, H.1
  • 74
    • 84923747738 scopus 로고    scopus 로고
    • Plasma lipoproteins are important components of the host defense system?
    • Han R. (2009) Plasma lipoproteins are important components of the host defense system? J Immunol 182: 134.74.
    • (2009) J Immunol , vol.182 , Issue.134 , pp. 74
    • Han, R.1
  • 75
    • 0024580112 scopus 로고
    • Lipoprotein a inhibits streptokinase-mediated activation of human plasminogen
    • Edelberg J.M., Gonzalez-Gronow M., Pizzo S.V. (1989) Lipoprotein a inhibits streptokinase-mediated activation of human plasminogen. Biochemistry 28: 2370-4.
    • (1989) Biochemistry , vol.28 , pp. 2370-2374
    • Edelberg, J.M.1    Gonzalez-Gronow, M.2    Pizzo, S.V.3
  • 77
    • 0242317267 scopus 로고    scopus 로고
    • The role of scavenger receptor class B type I (SR-BI) in lipid trafficking: Defining the rules for lipid traders
    • Rhainds D., Brissette L. (2004) The role of scavenger receptor class B type I (SR-BI) in lipid trafficking: Defining the rules for lipid traders. Int J Biochem Cell Biol 36: 39-77.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 39-77
    • Rhainds, D.1    Brissette, L.2
  • 78
    • 33846984609 scopus 로고    scopus 로고
    • Inflammation as a risk factor for carotid intimal-medial thickening, a measure of subclinical atherosclerosis in haemodialysis patients: The role of chlamydia and cytomegalovirus infection
    • Buyukhatipoglu H., Tiryaki O., Tahta K., Usalan C. (2007) Inflammation as a risk factor for carotid intimal-medial thickening, a measure of subclinical atherosclerosis in haemodialysis patients: the role of chlamydia and cytomegalovirus infection. Nephrology (Carlton) 12: 25-32.
    • (2007) Nephrology (Carlton) , vol.12 , pp. 25-32
    • Buyukhatipoglu, H.1    Tiryaki, O.2    Tahta, K.3    Usalan, C.4
  • 79
    • 35848936707 scopus 로고    scopus 로고
    • Apolipoprotein C-I is crucially involved in lipopolysaccharide-induced atherosclerosis development in apolipoprotein E-knockout mice
    • Westerterp M., Berbee J.F., Pires N.M., Van Mierlo G.J., Kleemann R., Romijn J.A., Havekes L.M., Rensen P.C. (2007) Apolipoprotein C-I is crucially involved in lipopolysaccharide-induced atherosclerosis development in apolipoprotein E-knockout mice. Circulation 116: 2173-81.
    • (2007) Circulation , vol.116 , pp. 2173-2181
    • Westerterp, M.1    Berbee, J.F.2    Pires, N.M.3    van Mierlo, G.J.4    Kleemann, R.5    Romijn, J.A.6    Havekes, L.M.7    Rensen, P.C.8
  • 81
    • 33744969769 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein autoantibodies, chronic infections, and carotid atherosclerosis in a population-based study
    • Mayr M., Kiechl S., Tsimikas S., Miller E., Sheldon J.,Willeit J., Witztum J.L., Xu Q. (2006) Oxidized low-density lipoprotein autoantibodies, chronic infections, and carotid atherosclerosis in a population-based study. J Am Coll Cardiol 47: 2436-43.
    • J Am Coll Cardiol , vol.47 , pp. 2436-2443
    • Mayr, M.1    Kiechl, S.2    Tsimikas, S.3    Miller, E.4    Sheldon, J.5    Willeit, J.6    Witztum, J.L.7    Xu, Q.8
  • 82
    • 28644446048 scopus 로고    scopus 로고
    • Dental infections and cardiovascular diseases: A review
    • Mattila K.J., Pussinen P.J., Paju S. (2005) Dental infections and cardiovascular diseases: a review. J Periodontol 76: 2085-8.
    • (2005) J Periodontol , vol.76 , pp. 2085-2088
    • Mattila, K.J.1    Pussinen, P.J.2    Paju, S.3
  • 84
    • 0017178654 scopus 로고
    • Comparison of the activities in inhibition of haemagglutination by different togaviruses for human serum lipoproteins and their constituents
    • Shortridge K.F., Ho W. K. (1976) Comparison of the activities in inhibition of haemagglutination by different togaviruses for human serum lipoproteins and their constituents. J Gen Virol 33: 523-7.
    • (1976) J Gen Virol , vol.33 , pp. 523-527
    • Shortridge, K.F.1    Ho, W.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.