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Volumn 9, Issue 12, 2011, Pages 1179-1190

Mannose-binding lectin and the balance between immune protection and complication

Author keywords

coagulation; complement; deficiency; infection; inflammation; mannose binding lectin; MASP; pattern recognition molecules

Indexed keywords

INTERLEUKIN 6; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE 1; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE 2; MANNOSE BINDING LECTIN; UNCLASSIFIED DRUG;

EID: 82455184700     PISSN: 14787210     EISSN: 17448336     Source Type: Journal    
DOI: 10.1586/eri.11.136     Document Type: Review
Times cited : (48)

References (141)
  • 1
    • 30044433696 scopus 로고    scopus 로고
    • The mannose-binding lectin: A prototypic pattern recognition molecule
    • Takahashi K, Ip WE, Michelow IC, Ezekowitz RA. The mannose-binding lectin: a prototypic pattern recognition molecule. Curr. Opin. Immunol. 18(1), 16-23 (2006).
    • (2006) Curr. Opin. Immunol. , vol.18 , Issue.1 , pp. 16-23
    • Takahashi, K.1    Ip, W.E.2    Michelow, I.C.3    Ezekowitz, R.A.4
  • 2
    • 27744452942 scopus 로고    scopus 로고
    • The role of the mannose-binding lectin in innate immunity
    • Takahashi K, Ezekowitz RA. The role of the mannose-binding lectin in innate immunity. Clin. Infect. Dis. 41(Suppl. 7), S440-S444 (2005).
    • (2005) Clin. Infect. Dis. , vol.41 , Issue.7
    • Takahashi, K.1    Ezekowitz, R.A.2
  • 3
    • 0027320098 scopus 로고
    • Studies on the carbohydrate-binding characteristics of human pulmonary surfactant-associated protein A and comparison with two other collectins: Mannan-binding protein and conglutinin
    • Pt 3
    • Haurum JS, Thiel S, Haagsman HP, Laursen SB, Larsen B, Jensenius JC. Studies on the carbohydrate-binding characteristics of human pulmonary surfactant-associated protein A and comparison with two other collectins: mannan-binding protein and conglutinin. Biochem. J. 293(Pt 3), 873-878 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 873-878
    • Haurum, J.S.1    Thiel, S.2    Haagsman, H.P.3    Laursen, S.B.4    Larsen, B.5    Jensenius, J.C.6
  • 4
    • 0017797684 scopus 로고
    • Isolation and characterization of a mannan-binding protein from rabbit liver
    • Kawasaki T, Etoh R, Yamashina I. Isolation and characterization of a mannan-binding protein from rabbit liver. Biochem. Biophys. Res. Commun. 81(3), 1018-1024 (1978).
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , Issue.3 , pp. 1018-1024
    • Kawasaki, T.1    Etoh, R.2    Yamashina, I.3
  • 5
    • 1542724425 scopus 로고    scopus 로고
    • Mannose-binding lectin binds to two major outer membrane proteins opacity protein and porin of Neisseria meningitidis
    • Estabrook MM, Jack DL, Klein NJ, Jarvis GA. Mannose-binding lectin binds to two major outer membrane proteins, opacity protein and porin, of Neisseria meningitidis. J. Immunol. 172(6), 3784-3792 (2004).
    • (2004) J. Immunol. , vol.172 , Issue.6 , pp. 3784-3792
    • Estabrook, M.M.1    Jack, D.L.2    Klein, N.J.3    Jarvis, G.A.4
  • 6
    • 78649500126 scopus 로고    scopus 로고
    • Mannose-binding lectin and its associated proteases MASPs mediate coagulation and its deficiency is a risk factor in developing complications from infection including disseminated intravascular coagulation
    • Takahashi K, Chang WC, Takahashi M et al. Mannose-binding lectin and its associated proteases (MASPs) mediate coagulation and its deficiency is a risk factor in developing complications from infection, including disseminated intravascular coagulation. Immunobiology 216(1-2), 96-102 (2011).
    • (2011) Immunobiology , vol.216 , Issue.1-2 , pp. 96-102
    • Takahashi, K.1    Chang, W.C.2    Takahashi, M.3
  • 7
    • 78650694711 scopus 로고    scopus 로고
    • Recombinant chimeric lectins consisting of mannose-binding lectin and L-ficolin are potent inhibitors of influenza A virus compared with mannose-binding lectin
    • Chang WC, Hartshorn KL, White MR et al. Recombinant chimeric lectins consisting of mannose-binding lectin and L-ficolin are potent inhibitors of influenza A virus compared with mannose-binding lectin. Biochem. Pharmacol. 81(3), 388-395 (2011).
    • (2011) Biochem. Pharmacol. , vol.81 , Issue.3 , pp. 388-395
    • Chang, W.C.1    Hartshorn, K.L.2    White, M.R.3
  • 8
    • 39549104720 scopus 로고    scopus 로고
    • Simultaneous activation of complement and coagulation by MBL-associated serine protease 2
    • Krarup A, Wallis R, Presanis JS, Gal P, Sim RB. Simultaneous activation of complement and coagulation by MBL-associated serine protease 2. PLoS ONE 2, e623 (2007).
    • (2007) PLoS ONE , vol.2
    • Krarup, A.1    Wallis, R.2    Presanis, J.S.3    Gal, P.4    Sim, R.B.5
  • 9
    • 0347915527 scopus 로고    scopus 로고
    • Differential substrate and inhibitor profiles for human MASP-1 and MASP-2
    • Presanis JS, Hajela K, Ambrus G, Gal P, Sim RB. Differential substrate and inhibitor profiles for human MASP-1 and MASP-2. Mol. Immunol. 40(13), 921-929 (2004).
    • (2004) Mol. Immunol. , vol.40 , Issue.13 , pp. 921-929
    • Presanis, J.S.1    Hajela, K.2    Ambrus, G.3    Gal, P.4    Sim, R.B.5
  • 10
    • 1642463804 scopus 로고    scopus 로고
    • The lectin-complement pathway - Its role in innate immunity and evolution
    • Fujita T, Matsushita M, Endo Y. The lectin-complement pathway - its role in innate immunity and evolution. Immunol. Rev. 198, 185-202 (2004).
    • (2004) Immunol. Rev. , vol.198 , pp. 185-202
    • Fujita, T.1    Matsushita, M.2    Endo, Y.3
  • 11
    • 77950909532 scopus 로고    scopus 로고
    • A novel mannose-binding lectin/ ficolin-associated protein is highly expressed in heart and skeletal muscle tissues and inhibits complement activation
    • Skjoedt MO, Hummelshoj T, Palarasah Y et al. A novel mannose-binding lectin/ ficolin-associated protein is highly expressed in heart and skeletal muscle tissues and inhibits complement activation. J. Biol. Chem. 285(11), 8234-8243 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.11 , pp. 8234-8243
    • Skjoedt, M.O.1    Hummelshoj, T.2    Palarasah, Y.3
  • 12
    • 79957606522 scopus 로고    scopus 로고
    • Characterization of the complex between mannose-binding lectin trimer and mannose-binding lectin-associated serine proteases
    • Tateishi K, Kanemoto T, Fujita T, Matsushita M. Characterization of the complex between mannose-binding lectin trimer and mannose-binding lectin-associated serine proteases. Microbiol. Immunol. 55(6), 427-433 (2011).
    • (2011) Microbiol. Immunol. , vol.55 , Issue.6 , pp. 427-433
    • Tateishi, K.1    Kanemoto, T.2    Fujita, T.3    Matsushita, M.4
  • 13
    • 0032531088 scopus 로고    scopus 로고
    • Different molecular events result in low protein levels of mannan-binding lectin in populations from southeast Africa and South America
    • Madsen HO, Satz ML, Hogh B, Svejgaard A, Garred P. Different molecular events result in low protein levels of mannan-binding lectin in populations from southeast Africa and South America. J. Immunol. 161(6), 3169-3175 (1998).
    • (1998) J. Immunol. , vol.161 , Issue.6 , pp. 3169-3175
    • Madsen, H.O.1    Satz, M.L.2    Hogh, B.3    Svejgaard, A.4    Garred, P.5
  • 14
    • 0026453082 scopus 로고
    • Diallelic polymorphism may explain variations of the blood concentration of mannan-binding protein in Eskimos but not in black Africans
    • Garred P, Madsen HO, Kurtzhals JA et al. Diallelic polymorphism may explain variations of the blood concentration of mannan-binding protein in Eskimos, but not in black Africans. Eur. J. Immunogenet. 19(6), 403-412 (1992).
    • (1992) Eur. J. Immunogenet. , vol.19 , Issue.6 , pp. 403-412
    • Garred, P.1    Madsen, H.O.2    Kurtzhals, J.A.3
  • 15
    • 0042565848 scopus 로고    scopus 로고
    • Mannose-binding lectin deficiency - Revisited
    • Garred P, Larsen F, Madsen HO, Koch C. Mannose-binding lectin deficiency - revisited. Mol. Immunol. 40(2-4), 73-84 (2003).
    • (2003) Mol. Immunol. , vol.40 , Issue.2-4 , pp. 73-84
    • Garred, P.1    Larsen, F.2    Madsen, H.O.3    Koch, C.4
  • 17
    • 0034738657 scopus 로고    scopus 로고
    • Detection of structural gene mutations and promoter polymorphisms in the mannan-binding lectin MBL gene by polymerase chain reaction with sequence-specific primers
    • Steffensen R, Thiel S, Varming K, Jersild C, Jensenius JC. Detection of structural gene mutations and promoter polymorphisms in the mannan-binding lectin (MBL) gene by polymerase chain reaction with sequence-specific primers. J. Immunol. Methods 241(1-2), 33-42 (2000).
    • (2000) J. Immunol. Methods , vol.241 , Issue.1-2 , pp. 33-42
    • Steffensen, R.1    Thiel, S.2    Varming, K.3    Jersild, C.4    Jensenius, J.C.5
  • 18
    • 0025872928 scopus 로고
    • Molecular basis of opsonic defect in immunodeficient children
    • Sumiya M, Super M, Tabona P et al. Molecular basis of opsonic defect in immunodeficient children. Lancet 337(8757), 1569-1570 (1991).
    • (1991) Lancet , vol.337 , Issue.8757 , pp. 1569-1570
    • Sumiya, M.1    Super, M.2    Tabona, P.3
  • 19
    • 78650412747 scopus 로고    scopus 로고
    • Lack of the pattern recognition molecule mannose-binding lectin increases susceptibility to influenza A virus infection
    • Chang WC, White MR, Moyo P et al. Lack of the pattern recognition molecule mannose-binding lectin increases susceptibility to influenza A virus infection. BMC Immunol. 11(1), 64 (2010).
    • (2010) BMC Immunol. , vol.11 , Issue.1 , pp. 64
    • Chang, W.C.1    White, M.R.2    Moyo, P.3
  • 20
    • 2542420995 scopus 로고    scopus 로고
    • Mannose-binding lectin-deficient mice are susceptible to infection with Staphylococcus aureus
    • Shi L, Takahashi K, Dundee J et al. Mannose-binding lectin-deficient mice are susceptible to infection with Staphylococcus aureus. J. Exp. Med. 199(10), 1379-1390 (2004).
    • (2004) J. Exp. Med. , vol.199 , Issue.10 , pp. 1379-1390
    • Shi, L.1    Takahashi, K.2    Dundee, J.3
  • 21
    • 31144468724 scopus 로고    scopus 로고
    • Deficiency of mannose-binding lectin greatly increases susceptibility to postburn infection with Pseudomonas aeruginosa
    • Moller-Kristensen M, Ip WK, Shi L et al. Deficiency of mannose-binding lectin greatly increases susceptibility to postburn infection with Pseudomonas aeruginosa. J. Immunol. 176(3), 1769-1775 (2006).
    • (2006) J. Immunol. , vol.176 , Issue.3 , pp. 1769-1775
    • Moller-Kristensen, M.1    Ip, W.K.2    Shi, L.3
  • 22
    • 8144230009 scopus 로고    scopus 로고
    • Mannan-binding lectin modulates the response to HSV-2 infection
    • Gadjeva M, Paludan SR, Thiel S et al. Mannan-binding lectin modulates the response to HSV-2 infection. Clin. Exp. Immunol. 138(2), 304-311 (2004).
    • (2004) Clin. Exp. Immunol. , vol.138 , Issue.2 , pp. 304-311
    • Gadjeva, M.1    Paludan, S.R.2    Thiel, S.3
  • 23
    • 78049515838 scopus 로고    scopus 로고
    • Mannan-binding lectin deficiency results in unusual antibody production and excessive experimental colitis in response to mannose-expressing mild gut pathogens
    • Muller S, Schaffer T, Flogerzi B et al. Mannan-binding lectin deficiency results in unusual antibody production and excessive experimental colitis in response to mannose-expressing mild gut pathogens. Gut 59(11), 1493-1500 (2010).
    • (2010) Gut , vol.59 , Issue.11 , pp. 1493-1500
    • Muller, S.1    Schaffer, T.2    Flogerzi, B.3
  • 24
    • 13444283302 scopus 로고    scopus 로고
    • Dynamic evolution of coagulopathy in the first day of severe sepsis: Relationship with mortality and organ failure
    • Dhainaut JF, Shorr AF, Macias WL et al. Dynamic evolution of coagulopathy in the first day of severe sepsis: relationship with mortality and organ failure. Crit. Care Med. 33(2), 341-348 (2005).
    • (2005) Crit. Care Med. , vol.33 , Issue.2 , pp. 341-348
    • Dhainaut, J.F.1    Shorr, A.F.2    Macias, W.L.3
  • 25
    • 0347130902 scopus 로고    scopus 로고
    • Biphasic activated partial thromboplastin time waveform and adverse events in non-intensive care unit patients
    • Smith EY, Charles LA, Van Cott EM. Biphasic activated partial thromboplastin time waveform and adverse events in non-intensive care unit patients. Am. J. Clin. Pathol. 121(1), 138-141 (2004).
    • (2004) Am. J. Clin. Pathol. , vol.121 , Issue.1 , pp. 138-141
    • Smith, E.Y.1    Charles, L.A.2    Van Cott, E.M.3
  • 26
    • 54049083511 scopus 로고    scopus 로고
    • The coagulant response in sepsis
    • viii
    • Levi M. The coagulant response in sepsis. Clin. Chest Med. 29(4), 627-642, viii (2008).
    • (2008) Clin. Chest Med. , vol.29 , Issue.4 , pp. 627-642
    • Levi, M.1
  • 28
    • 10644283860 scopus 로고    scopus 로고
    • Prospective validation of the International society of thrombosis and haemostasis scoring system for disseminated intravascular coagulation
    • Bakhtiari K, Meijers JC, de Jonge E, Levi M. Prospective validation of the International society of thrombosis and haemostasis scoring system for disseminated intravascular coagulation. Crit. Care Med. 32(12), 2416-2421 (2004).
    • (2004) Crit. Care Med. , vol.32 , Issue.12 , pp. 2416-2421
    • Bakhtiari, K.1    Meijers, J.C.2    De Jonge, E.3    Levi, M.4
  • 29
    • 0037310722 scopus 로고    scopus 로고
    • Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: A study on recombinant catalytic fragments
    • Ambrus G, Gal P, Kojima M et al. Natural substrates and inhibitors of mannan-binding lectin-associated serine protease-1 and -2: a study on recombinant catalytic fragments. J. Immunol. 170(3), 1374-1382 (2003).
    • (2003) J. Immunol. , vol.170 , Issue.3 , pp. 1374-1382
    • Ambrus, G.1    Gal, P.2    Kojima, M.3
  • 30
    • 0036747195 scopus 로고    scopus 로고
    • The biological functions of MBL-associated serine proteases MASPs
    • Hajela K, Kojima M, Ambrus G et al. The biological functions of MBL-associated serine proteases (MASPs).Immunobiology 205(4-5), 467-475 (2002).
    • (2002) Immunobiology , vol.205 , Issue.4-5 , pp. 467-475
    • Hajela, K.1    Kojima, M.2    Ambrus, G.3
  • 31
    • 53149096593 scopus 로고    scopus 로고
    • The action of MBL-associated serine protease 1 MASP1 on factor XIII and fibrinogen
    • Krarup A, Gulla KC, Gal P, Hajela K, Sim RB. The action of MBL-associated serine protease 1 (MASP1) on factor XIII and fibrinogen. Biochim. Biophys. Acta 1784(9), 1294-1300 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1784 , Issue.9 , pp. 1294-1300
    • Krarup, A.1    Gulla, K.C.2    Gal, P.3    Hajela, K.4    Sim, R.B.5
  • 33
    • 1642580504 scopus 로고    scopus 로고
    • Age-dependent development of the splenic marginal zone in human infants is associated with different causes of death
    • Kruschinski C, Zidan M, Debertin AS, von Horsten S, Pabst R. Age-dependent development of the splenic marginal zone in human infants is associated with different causes of death. Hum. Pathol. 35(1), 113-121 (2004).
    • (2004) Hum. Pathol. , vol.35 , Issue.1 , pp. 113-121
    • Kruschinski, C.1    Zidan, M.2    Debertin, A.S.3    Von Horsten, S.4    Pabst, R.5
  • 35
    • 65449118333 scopus 로고    scopus 로고
    • Neonatal protection by an innate immune system of human milk consisting of oligosaccharides and glycans
    • Newburg DS. Neonatal protection by an innate immune system of human milk consisting of oligosaccharides and glycans. J. Anim. Sci. 87(Suppl. 13), 26-34 (2009).
    • (2009) J. Anim. Sci. , vol.87 , Issue.13 , pp. 26-34
    • Newburg, D.S.1
  • 36
    • 0037114187 scopus 로고    scopus 로고
    • L-MBP is expressed in epithelial cells of mouse small intestine
    • Uemura K, Saka M, Nakagawa T et al. L-MBP is expressed in epithelial cells of mouse small intestine. J. Immunol. 169(12), 6945-6950 (2002).
    • (2002) J. Immunol. , vol.169 , Issue.12 , pp. 6945-6950
    • Uemura, K.1    Saka, M.2    Nakagawa, T.3
  • 38
    • 78649495777 scopus 로고    scopus 로고
    • Mannose-binding lectin is produced by vaginal epithelial cells and its level in the vaginal fluid is influenced by progesterone
    • Bulla R, De Seta F, Radillo O et al. Mannose-binding lectin is produced by vaginal epithelial cells and its level in the vaginal fluid is influenced by progesterone. Mol. Immunol. 48(1-3), 281-286 (2010).
    • (2010) Mol. Immunol. , vol.48 , Issue.1-3 , pp. 281-286
    • Bulla, R.1    De Seta, F.2    Radillo, O.3
  • 39
    • 22144468057 scopus 로고    scopus 로고
    • Ultraviolet-B recruits mannose-binding lectin into skin from non-cutaneous sources
    • Lokitz ML, Zhang W, Bashir M et al. Ultraviolet-B recruits mannose-binding lectin into skin from non-cutaneous sources. J. Invest. Dermatol. 125(1), 166-173 (2005).
    • (2005) J. Invest. Dermatol. , vol.125 , Issue.1 , pp. 166-173
    • Lokitz, M.L.1    Zhang, W.2    Bashir, M.3
  • 40
    • 60549102114 scopus 로고    scopus 로고
    • Mannose-binding lectin is present in the infected airway: A possible pulmonary defence mechanism
    • Fidler KJ, Hilliard TN, Bush A et al. Mannose-binding lectin is present in the infected airway: a possible pulmonary defence mechanism. Thorax 64(2), 150-155 (2009).
    • (2009) Thorax , vol.64 , Issue.2 , pp. 150-155
    • Fidler, K.J.1    Hilliard, T.N.2    Bush, A.3
  • 41
    • 42549127332 scopus 로고    scopus 로고
    • Mannose binding lectin gene deficiency increases susceptibility to traumatic brain injury in mice
    • Yager PH, You Z, Qin T et al. Mannose binding lectin gene deficiency increases susceptibility to traumatic brain injury in mice. J. Cereb. Blood Flow. Metab. 28(5), 1030-1039 (2008).
    • (2008) J. Cereb. Blood Flow. Metab. , vol.28 , Issue.5 , pp. 1030-1039
    • Yager, P.H.1    You, Z.2    Qin, T.3
  • 42
    • 33845786617 scopus 로고    scopus 로고
    • Identification and characterization of a novel human collectin CL-K1
    • Keshi H, Sakamoto T, Kawai T et al. Identification and characterization of a novel human collectin CL-K1. Microbiol. Immunol. 50(12), 1001-1013 (2006).
    • (2006) Microbiol. Immunol. , vol.50 , Issue.12 , pp. 1001-1013
    • Keshi, H.1    Sakamoto, T.2    Kawai, T.3
  • 43
    • 79958823141 scopus 로고    scopus 로고
    • Disease-causing mutations in genes of the complement system
    • Degn SE, Jensenius JC, Thiel S. Disease-causing mutations in genes of the complement system. Am. J. Hum. Genet. 88(6), 689-705 (2011).
    • (2011) Am. J. Hum. Genet. , vol.88 , Issue.6 , pp. 689-705
    • Degn, S.E.1    Jensenius, J.C.2    Thiel, S.3
  • 45
    • 40449099734 scopus 로고    scopus 로고
    • Directing an appropriate immune response: The role of defense collagens and other soluble pattern recognition molecules
    • Fraser DA, Tenner AJ. Directing an appropriate immune response: the role of defense collagens and other soluble pattern recognition molecules. Curr. Drug Targets 9(2), 113-122 (2008).
    • (2008) Curr. Drug Targets , vol.9 , Issue.2 , pp. 113-122
    • Fraser, D.A.1    Tenner, A.J.2
  • 46
    • 34548321364 scopus 로고    scopus 로고
    • Complement activating soluble pattern recognition molecules with collagen-like regions mannan-binding lectin, ficolins and associated proteins
    • Thiel S. Complement activating soluble pattern recognition molecules with collagen-like regions, mannan-binding lectin, ficolins and associated proteins. Mol. Immunol. 44(16), 3875-3888 (2007).
    • (2007) Mol. Immunol. , vol.44 , Issue.16 , pp. 3875-3888
    • Thiel, S.1
  • 47
    • 73349128762 scopus 로고    scopus 로고
    • MAp44 a human protein associated with pattern recognition molecules of the complement system and regulating the lectin pathway of complement activation
    • Degn SE, Hansen AG, Steffensen R, Jacobsen C, Jensenius JC, Thiel S. MAp44, a human protein associated with pattern recognition molecules of the complement system and regulating the lectin pathway of complement activation. J. Immunol. 183(11), 7371-7378 (2009).
    • (2009) J. Immunol. , vol.183 , Issue.11 , pp. 7371-7378
    • Degn, S.E.1    Hansen, A.G.2    Steffensen, R.3    Jacobsen, C.4    Jensenius, J.C.5    Thiel, S.6
  • 48
    • 0034897825 scopus 로고    scopus 로고
    • MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway
    • Dahl MR, Thiel S, Matsushita M et al. MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway. Immunity 15(1), 127-135 (2001).
    • (2001) Immunity , vol.15 , Issue.1 , pp. 127-135
    • Dahl, M.R.1    Thiel, S.2    Matsushita, M.3
  • 49
    • 33846618236 scopus 로고    scopus 로고
    • Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway
    • Moller-Kristensen M, Thiel S, Sjoholm A, Matsushita M, Jensenius JC. Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway. Int. Immunol. 19(2), 141-149 (2007).
    • (2007) Int. Immunol. , vol.19 , Issue.2 , pp. 141-149
    • Moller-Kristensen, M.1    Thiel, S.2    Sjoholm, A.3    Matsushita, M.4    Jensenius, J.C.5
  • 50
    • 78149483744 scopus 로고    scopus 로고
    • Essential role of complement mannose-binding lectin-associated serine proteases-1/3 in the murine collagen antibody-induced model of inflammatory arthritis
    • Banda NK, Takahashi M, Levitt B et al. Essential role of complement mannose-binding lectin-associated serine proteases-1/3 in the murine collagen antibody-induced model of inflammatory arthritis. J. Immunol. 185(9), 5598-5606 (2010).
    • (2010) J. Immunol. , vol.185 , Issue.9 , pp. 5598-5606
    • Banda, N.K.1    Takahashi, M.2    Levitt, B.3
  • 51
    • 17344367227 scopus 로고    scopus 로고
    • Production and purification of recombinants of mouse MASP-2 and sMAP
    • Iwaki D, Fujita T. Production and purification of recombinants of mouse MASP-2 and sMAP. J. Endotoxin. Res. 11(1), 47-50 (2005).
    • (2005) J. Endotoxin. Res. , vol.11 , Issue.1 , pp. 47-50
    • Iwaki, D.1    Fujita, T.2
  • 52
    • 76149085506 scopus 로고    scopus 로고
    • Essential role of mannose-binding lectin-associated serine protease-1 in activation of the complement factor D
    • Takahashi M, Ishida Y, Iwaki D et al. Essential role of mannose-binding lectin-associated serine protease-1 in activation of the complement factor D. J. Exp. Med. 207(1), 29-37 (2010).
    • (2010) J. Exp. Med. , vol.207 , Issue.1 , pp. 29-37
    • Takahashi, M.1    Ishida, Y.2    Iwaki, D.3
  • 53
    • 9644291604 scopus 로고    scopus 로고
    • An optimized murine model of ferric chloride-induced arterial thrombosis for thrombosis research
    • Wang X, Xu L. An optimized murine model of ferric chloride-induced arterial thrombosis for thrombosis research. Thromb. Res. 115(1-2), 95-100 (2005).
    • (2005) Thromb. Res. , vol.115 , Issue.1-2 , pp. 95-100
    • Wang, X.1    Xu, L.2
  • 55
    • 77949383621 scopus 로고    scopus 로고
    • Activation of mannan-binding lectin-associated serine proteases leads to generation of a fibrin clot
    • Gulla KC, Gupta K, Krarup A et al. Activation of mannan-binding lectin-associated serine proteases leads to generation of a fibrin clot. Immunology 129(4), 482-495 (2010).
    • (2010) Immunology , vol.129 , Issue.4 , pp. 482-495
    • Gulla, K.C.1    Gupta, K.2    Krarup, A.3
  • 56
    • 70450225119 scopus 로고    scopus 로고
    • Interactions of ficolin and mannose-binding lectin with fibrinogen/fibrin augment the lectin complement pathway
    • Endo Y, Nakazawa N, Iwaki D, Takahashi M, Matsushita M, Fujita T. Interactions of ficolin and mannose-binding lectin with fibrinogen/fibrin augment the lectin complement pathway. J. Innate. Immun. 2(1), 33-42 (2010).
    • (2010) J. Innate. Immun. , vol.2 , Issue.1 , pp. 33-42
    • Endo, Y.1    Nakazawa, N.2    Iwaki, D.3    Takahashi, M.4    Matsushita, M.5    Fujita, T.6
  • 57
    • 33845438522 scopus 로고    scopus 로고
    • Small mannose-binding lectin-associated protein plays a regulatory role in the lectin complement pathway
    • Iwaki D, Kanno K, Takahashi M et al. Small mannose-binding lectin-associated protein plays a regulatory role in the lectin complement pathway. J. Immunol. 177(12), 8626-8632 (2006).
    • (2006) J. Immunol. , vol.177 , Issue.12 , pp. 8626-8632
    • Iwaki, D.1    Kanno, K.2    Takahashi, M.3
  • 58
    • 0026920707 scopus 로고
    • Distinct and overlapping functions of allelic forms of human mannose binding protein
    • Super M, Gillies SD, Foley S et al. Distinct and overlapping functions of allelic forms of human mannose binding protein. Nat. Genet. 2(1), 50-55 (1992).
    • (1992) Nat. Genet. , vol.2 , Issue.1 , pp. 50-55
    • Super, M.1    Gillies, S.D.2    Foley, S.3
  • 59
    • 0029045792 scopus 로고
    • Interplay between promoter and structural gene variants control basal serum level of mannan-binding protein
    • Madsen HO, Garred P, Thiel S et al. Interplay between promoter and structural gene variants control basal serum level of mannan-binding protein. J. Immunol. 155(6), 3013-3020 (1995).
    • (1995) J. Immunol. , vol.155 , Issue.6 , pp. 3013-3020
    • Madsen, H.O.1    Garred, P.2    Thiel, S.3
  • 60
    • 0028236241 scopus 로고
    • A new frequent allele is the missing link in the structural polymorphism of the human mannan-binding protein
    • Madsen HO, Garred P, Kurtzhals JA et al. A new frequent allele is the missing link in the structural polymorphism of the human mannan-binding protein. Immunogenetics 40(1), 37-44 (1994).
    • (1994) Immunogenetics , vol.40 , Issue.1 , pp. 37-44
    • Madsen, H.O.1    Garred, P.2    Kurtzhals, J.A.3
  • 61
    • 0036748175 scopus 로고    scopus 로고
    • Structural and functional aspects of complement activation by mannose-binding protein
    • Wallis R. Structural and functional aspects of complement activation by mannose-binding protein. Immunobiology 205(4-5), 433-445 (2002).
    • (2002) Immunobiology , vol.205 , Issue.4-5 , pp. 433-445
    • Wallis, R.1
  • 62
    • 0030008251 scopus 로고    scopus 로고
    • Mutations in the human mannose-binding protein gene: Frequencies in several population groups
    • Lipscombe RJ, Beatty DW, Ganczakowski M et al. Mutations in the human mannose-binding protein gene: frequencies in several population groups. Eur. J. Hum. Genet. 4(1), 13-19 (1996).
    • (1996) Eur. J. Hum. Genet. , vol.4 , Issue.1 , pp. 13-19
    • Lipscombe, R.J.1    Beatty, D.W.2    Ganczakowski, M.3
  • 63
    • 34748834134 scopus 로고    scopus 로고
    • The MBL2 LYQA secretor haplotype is an independent predictor of postoperative myocardial infarction in whites undergoing coronary artery bypass graft surgery
    • Collard CD, Shernan SK, Fox AA et al. The MBL2 'LYQA secretor' haplotype is an independent predictor of postoperative myocardial infarction in whites undergoing coronary artery bypass graft surgery. Circulation 116(Suppl. 11), S106-S112 (2007).
    • (2007) Circulation , vol.116 , Issue.11
    • Collard, C.D.1    Shernan, S.K.2    Fox, A.A.3
  • 64
    • 0028971585 scopus 로고
    • The Gly-54->Asp allelic form of human mannose-binding protein MBP fails to bind MBP-associated serine protease
    • Pt 3
    • Matsushita M, Ezekowitz RA, Fujita T. The Gly-54->Asp allelic form of human mannose-binding protein (MBP) fails to bind MBP-associated serine protease. Biochem. J. 311(Pt 3), 1021-1023 (1995).
    • (1995) Biochem. J. , vol.311 , pp. 1021-1023
    • Matsushita, M.1    Ezekowitz, R.A.2    Fujita, T.3
  • 65
    • 1842740356 scopus 로고    scopus 로고
    • Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: Indirect effects of naturally occurring mutations on protease binding and activation
    • Wallis R, Shaw JM, Uitdehaag J, Chen CB, Torgersen D, Drickamer K. Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: indirect effects of naturally occurring mutations on protease binding and activation. J. Biol. Chem. 279(14), 14065-14073 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.14 , pp. 14065-14073
    • Wallis, R.1    Shaw, J.M.2    Uitdehaag, J.3    Chen, C.B.4    Torgersen, D.5    Drickamer, K.6
  • 66
    • 0034613383 scopus 로고    scopus 로고
    • Interaction of mannose-binding protein with associated serine proteases: Effects of naturally occurring mutations
    • Wallis R, Dodd RB. Interaction of mannose-binding protein with associated serine proteases: effects of naturally occurring mutations. J. Biol. Chem. 275(40), 30962-30969 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.40 , pp. 30962-30969
    • Wallis, R.1    Dodd, R.B.2
  • 67
    • 33645850696 scopus 로고    scopus 로고
    • Mannan-binding lectin MBL- mediated opsonization is enhanced by the alternative pathway amplification loop
    • Brouwer N, Dolman KM, van Zwieten R et al. Mannan-binding lectin (MBL)- mediated opsonization is enhanced by the alternative pathway amplification loop. Mol. Immunol. 43(13), 2051-2060 (2006).
    • (2006) Mol. Immunol. , vol.43 , Issue.13 , pp. 2051-2060
    • Brouwer, N.1    Dolman, K.M.2    Van Zwieten, R.3
  • 68
    • 35748950136 scopus 로고    scopus 로고
    • Pathogenic complement activation in collagen antibody-induced arthritis in mice requires amplification by the alternative pathway
    • Banda NK, Takahashi K, Wood AK, Holers VM, Arend WP. Pathogenic complement activation in collagen antibody-induced arthritis in mice requires amplification by the alternative pathway. J. Immunol. 179(6), 4101-4109 (2007).
    • (2007) J. Immunol. , vol.179 , Issue.6 , pp. 4101-4109
    • Banda, N.K.1    Takahashi, K.2    Wood, A.K.3    Holers, V.M.4    Arend, W.P.5
  • 69
    • 34250700510 scopus 로고    scopus 로고
    • Role of the alternative pathway in the early complement activation following major trauma
    • Ganter MT, Brohi K, Cohen MJ et al. Role of the alternative pathway in the early complement activation following major trauma. Shock 28(1), 29-34 (2007).
    • (2007) Shock , vol.28 , Issue.1 , pp. 29-34
    • Ganter, M.T.1    Brohi, K.2    Cohen, M.J.3
  • 70
    • 46049088698 scopus 로고    scopus 로고
    • An age-dependent association of mannose-binding lectin-2 genetic variants on HIV-1-related disease in children
    • Singh KK, Lieser A, Ruan PK, Fenton T, Spector SA. An age-dependent association of mannose-binding lectin-2 genetic variants on HIV-1-related disease in children. J. Aller. Clin. Immunol. 122(1), 173-180 (2008).
    • (2008) J. Aller. Clin. Immunol. , vol.122 , Issue.1 , pp. 173-180
    • Singh, K.K.1    Lieser, A.2    Ruan, P.K.3    Fenton, T.4    Spector, S.A.5
  • 71
    • 38049036445 scopus 로고    scopus 로고
    • Mannose-binding lectin MBL genotype in relation to risk of nosocomial infection in pre-term neonates in the neonatal intensive care unit
    • van der Zwet WC, Catsburg A, van Elburg RM, Savelkoul PH, Vandenbroucke-Grauls CM. Mannose-binding lectin (MBL) genotype in relation to risk of nosocomial infection in pre-term neonates in the neonatal intensive care unit. Clin. Microbiol. Infect. 14(2), 130-135 (2008).
    • (2008) Clin. Microbiol. Infect. , vol.14 , Issue.2 , pp. 130-135
    • Van Der Zwet, W.C.1    Catsburg, A.2    Van Elburg, R.M.3    Savelkoul, P.H.4    Vandenbroucke-Grauls, C.M.5
  • 72
    • 52649118504 scopus 로고    scopus 로고
    • Mannose-binding lectin status is associated with risk of major infection following myeloablative sibling allogeneic hematopoietic stem cell transplantation
    • Mullighan CG, Heatley SL, Danner S et al. Mannose-binding lectin status is associated with risk of major infection following myeloablative sibling allogeneic hematopoietic stem cell transplantation. Blood 112(5), 2120-2128 (2008).
    • (2008) Blood , vol.112 , Issue.5 , pp. 2120-2128
    • Mullighan, C.G.1    Heatley, S.L.2    Danner, S.3
  • 74
    • 33847378056 scopus 로고    scopus 로고
    • Age-dependent association of human mannose-binding lectin mutations with susceptibility to invasive meningococcal disease in childhood
    • Faber J, Schuessler T, Finn A et al. Age-dependent association of human mannose-binding lectin mutations with susceptibility to invasive meningococcal disease in childhood. Ped. Infect. Dis. J. 26(3), 243-246 (2007).
    • (2007) Ped. Infect. Dis. J. , vol.26 , Issue.3 , pp. 243-246
    • Faber, J.1    Schuessler, T.2    Finn, A.3
  • 75
    • 38749153572 scopus 로고    scopus 로고
    • Mannose-binding lectin enhances Toll-like receptors 2 and 6 signaling from the phagosome
    • Ip WK, Takahashi K, Moore KJ, Stuart LM, Ezekowitz RA. Mannose-binding lectin enhances Toll-like receptors 2 and 6 signaling from the phagosome. J. Exp. Med. 205(1), 169-181 (2008).
    • (2008) J. Exp. Med. , vol.205 , Issue.1 , pp. 169-181
    • Ip, W.K.1    Takahashi, K.2    Moore, K.J.3    Stuart, L.M.4    Ezekowitz, R.A.5
  • 76
    • 28444483567 scopus 로고    scopus 로고
    • Relative roles of complement factor 3 and mannose-binding lectin in host defense against infection
    • Takahashi K, Shi L, Gowda LD, Ezekowitz RA. Relative roles of complement factor 3 and mannose-binding lectin in host defense against infection. Infect. Immun. 73(12), 8188-8193 (2005).
    • (2005) Infect. Immun. , vol.73 , Issue.12 , pp. 8188-8193
    • Takahashi, K.1    Shi, L.2    Gowda, L.D.3    Ezekowitz, R.A.4
  • 77
    • 0024446048 scopus 로고
    • Association of low levels of mannan-binding protein with a common defect of opsonisation
    • Super M, Thiel S, Lu J, Levinsky RJ, Turner MW. Association of low levels of mannan-binding protein with a common defect of opsonisation. Lancet 2(8674), 1236-1239 (1989).
    • (1989) Lancet , vol.2 , Issue.8674 , pp. 1236-1239
    • Super, M.1    Thiel, S.2    Lu, J.3    Levinsky, R.J.4    Turner, M.W.5
  • 78
    • 0030832773 scopus 로고    scopus 로고
    • Participation of tissue factor and thrombin in posttraumatic systemic inflammatory syndrome
    • Gando S, Kameue T, Nanzaki S, Hayakawa T, Nakanishi Y. Participation of tissue factor and thrombin in posttraumatic systemic inflammatory syndrome. Crit. Care Med. 25(11), 1820-1826 (1997).
    • (1997) Crit. Care Med. , vol.25 , Issue.11 , pp. 1820-1826
    • Gando, S.1    Kameue, T.2    Nanzaki, S.3    Hayakawa, T.4    Nakanishi, Y.5
  • 79
    • 0029082904 scopus 로고
    • Outcome of disseminated intravascular coagulation in relation to the score when treatment was begun
    • Mie DIC study group.
    • Wada H, Wakita Y, Nakase T et al. Outcome of disseminated intravascular coagulation in relation to the score when treatment was begun. Mie DIC study group. Thromb. Haemost. 74(3), 848-852 (1995).
    • (1995) Thromb. Haemost. , vol.74 , Issue.3 , pp. 848-852
    • Wada, H.1    Wakita, Y.2    Nakase, T.3
  • 80
    • 0033584457 scopus 로고    scopus 로고
    • Disseminated intravascular coagulation
    • Levi M, ten Cate H. Disseminated intravascular coagulation. N. Engl. J. Med. 341(8), 586-592 (1999).
    • (1999) N. Engl. J. Med. , vol.341 , Issue.8 , pp. 586-592
    • Levi, M.1    Ten Cate, H.2
  • 81
    • 0036785406 scopus 로고    scopus 로고
    • Biphasic transmittance waveform in the APTT coagulation assay is due to the formation of a Ca++-dependent complex of C-reactive protein with very-low-density lipoprotein and is a novel marker of impending disseminated intravascular coagulation
    • Toh CH, Samis J, Downey C et al. Biphasic transmittance waveform in the APTT coagulation assay is due to the formation of a Ca(++)-dependent complex of C-reactive protein with very-low-density lipoprotein and is a novel marker of impending disseminated intravascular coagulation. Blood 100(7), 2522-2529 (2002).
    • (2002) Blood , vol.100 , Issue.7 , pp. 2522-2529
    • Toh, C.H.1    Samis, J.2    Downey, C.3
  • 82
    • 0031949847 scopus 로고    scopus 로고
    • Early identification and prognostic implications in disseminated intravascular coagulation through transmittance waveform analysis
    • Downey C, Kazmi R, Toh CH. Early identification and prognostic implications in disseminated intravascular coagulation through transmittance waveform analysis. Thromb. Haemost. 80(1), 65-69 (1998).
    • (1998) Thromb. Haemost. , vol.80 , Issue.1 , pp. 65-69
    • Downey, C.1    Kazmi, R.2    Toh, C.H.3
  • 83
    • 67650645257 scopus 로고    scopus 로고
    • The coagulopathy of trauma: A review of mechanisms
    • Hess JR, Brohi K, Dutton RP et al. The coagulopathy of trauma: a review of mechanisms. J. Trauma. 65(4), 748-754 (2008).
    • (2008) J. Trauma. , vol.65 , Issue.4 , pp. 748-754
    • Hess, J.R.1    Brohi, K.2    Dutton, R.P.3
  • 84
    • 0642373576 scopus 로고    scopus 로고
    • Infection and inflammation and the coagulation system
    • Levi M, Keller TT, van Gorp E, ten Cate H. Infection and inflammation and the coagulation system. Cardiovasc. Res. 60(1), 26-39 (2003).
    • (2003) Cardiovasc. Res. , vol.60 , Issue.1 , pp. 26-39
    • Levi, M.1    Keller, T.T.2    Van Gorp, E.3    Ten Cate, H.4
  • 85
    • 0033815368 scopus 로고    scopus 로고
    • Pathophysiology of disseminated intravascular coagulation in sepsis
    • ten Cate H. Pathophysiology of disseminated intravascular coagulation in sepsis. Crit. Care Med. 28(Suppl. 9), S9-S11 (2000).
    • (2000) Crit. Care Med. , vol.28 , Issue.9
    • Ten Cate, H.1
  • 86
    • 78650289203 scopus 로고    scopus 로고
    • Role of C5 activation products in sepsis
    • Ward PA. Role of C5 activation products in sepsis. Sci. World J. 10, 2395-2402 (2010).
    • (2010) Sci. World J. , vol.10 , pp. 2395-2402
    • Ward, P.A.1
  • 87
    • 30044438804 scopus 로고    scopus 로고
    • Mannose-binding lectin in chronic hepatitis B virus infection
    • Chong WP, To YF, Ip WK et al. Mannose-binding lectin in chronic hepatitis B virus infection. Hepatology 42(5), 1037-1045 (2005).
    • (2005) Hepatology , vol.42 , Issue.5 , pp. 1037-1045
    • Chong, W.P.1    To, Y.F.2    Ip, W.K.3
  • 88
    • 42049114253 scopus 로고    scopus 로고
    • Mannan-binding lectin MBL2 gene polymorphism in chronic hepatitis C: Association with the severity of liver fibrosis and response to interferon therapy
    • Alves Pedroso ML, Boldt AB, Pereira-Ferrari L et al. Mannan-binding lectin MBL2 gene polymorphism in chronic hepatitis C: association with the severity of liver fibrosis and response to interferon therapy. Clin. Exp. Immunol. 152(2), 258-264 (2008).
    • (2008) Clin. Exp. Immunol. , vol.152 , Issue.2 , pp. 258-264
    • Alves Pedroso, M.L.1    Boldt, A.B.2    Pereira-Ferrari, L.3
  • 90
    • 0032102703 scopus 로고    scopus 로고
    • Bacteriology of burns
    • Revathi G, Puri J, Jain BK. Bacteriology of burns. Burns 24(4), 347-349 (1998).
    • (1998) Burns , vol.24 , Issue.4 , pp. 347-349
    • Revathi, G.1    Puri, J.2    Jain, B.K.3
  • 91
    • 0035131887 scopus 로고    scopus 로고
    • Microbiologic aspects of predominant bacteria isolated from the burn patients in Korea
    • Song W, Lee KM, Kang HJ, Shin DH, Kim DK. Microbiologic aspects of predominant bacteria isolated from the burn patients in Korea. Burns 27(2), 136-139 (2001).
    • (2001) Burns , vol.27 , Issue.2 , pp. 136-139
    • Song, W.1    Lee, K.M.2    Kang, H.J.3    Shin, D.H.4    Kim, D.K.5
  • 94
    • 77955574439 scopus 로고    scopus 로고
    • Contribution of bacterial and viral infections to attributable mortality in patients with severe burns: An autopsy series
    • D'Avignon LC, Hogan BK, Murray CK et al. Contribution of bacterial and viral infections to attributable mortality in patients with severe burns: an autopsy series. Burns 36(6), 773-779 (2010).
    • (2010) Burns , vol.36 , Issue.6 , pp. 773-779
    • D'Avignon, L.C.1    Hogan, B.K.2    Murray, C.K.3
  • 96
    • 0034292361 scopus 로고    scopus 로고
    • Distinct effects of surfactant protein A or D deficiency during bacterial infection on the lung
    • LeVine AM, Whitsett JA, Gwozdz JA et al. Distinct effects of surfactant protein A or D deficiency during bacterial infection on the lung. J. Immunol. 165(7), 3934-3940 (2000).
    • (2000) J. Immunol. , vol.165 , Issue.7 , pp. 3934-3940
    • LeVine, A.M.1    Whitsett, J.A.2    Gwozdz, J.A.3
  • 97
    • 0036008399 scopus 로고    scopus 로고
    • Surfactant protein-A - Deficient mice display an exaggerated early inflammatory response to a b-resistant strain of influenza A virus
    • Li G, Siddiqui J, Hendry M et al. Surfactant protein-A - deficient mice display an exaggerated early inflammatory response to a b-resistant strain of influenza A virus. Am. J. Respir. Cell Mol. Biol. 26(3), 277-282 (2002).
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.26 , Issue.3 , pp. 277-282
    • Li, G.1    Siddiqui, J.2    Hendry, M.3
  • 98
    • 0035889906 scopus 로고    scopus 로고
    • Surfactant protein D enhances clearance of influenza A virus from the lung in vivo
    • LeVine AM, Whitsett JA, Hartshorn KL, Crouch EC, Korfhagen TR. Surfactant protein D enhances clearance of influenza A virus from the lung in vivo. J. Immunol. 167(10), 5868-5873 (2001).
    • (2001) J. Immunol. , vol.167 , Issue.10 , pp. 5868-5873
    • LeVine, A.M.1    Whitsett, J.A.2    Hartshorn, K.L.3    Crouch, E.C.4    Korfhagen, T.R.5
  • 99
    • 33645102517 scopus 로고    scopus 로고
    • Alveolar macrophages and emphysema in surfactant protein-D-deficient mice
    • Yoshida M, Whitsett JA. Alveolar macrophages and emphysema in surfactant protein-D-deficient mice. Respirol. 11(Suppl.), S37-S40 (2006).
    • (2006) Respirol. , vol.11
    • Yoshida, M.1    Whitsett, J.A.2
  • 100
    • 14844363449 scopus 로고    scopus 로고
    • Mannose-binding lectin-deficient mice display defective apoptotic cell clearance but no autoimmune phenotype
    • Stuart LM, Takahashi K, Shi L, Savill J, Ezekowitz RA. Mannose-binding lectin-deficient mice display defective apoptotic cell clearance but no autoimmune phenotype. J. Immunol. 174(6), 3220-3226 (2005).
    • (2005) J. Immunol. , vol.174 , Issue.6 , pp. 3220-3226
    • Stuart, L.M.1    Takahashi, K.2    Shi, L.3    Savill, J.4    Ezekowitz, R.A.5
  • 101
  • 102
    • 3142615914 scopus 로고    scopus 로고
    • Hydrogen peroxide activates the Gas6-Axl pathway in vascular smooth muscle cells
    • Konishi A, Aizawa T, Mohan A, Korshunov VA, Berk BC. Hydrogen peroxide activates the Gas6-Axl pathway in vascular smooth muscle cells. J. Biol. Chem. 279(27), 28766-28770 (2004).
    • (2004) J. Biol. Chem. , vol.279 , Issue.27 , pp. 28766-28770
    • Konishi, A.1    Aizawa, T.2    Mohan, A.3    Korshunov, V.A.4    Berk, B.C.5
  • 104
    • 0027102386 scopus 로고
    • Hypoxia-mediated induction of endothelial cell interleukin-1a an autocrine mechanism promoting expression of leukocyte adhesion molecules on the vessel surface
    • Shreeniwas R, Koga S, Karakurum M et al. Hypoxia-mediated induction of endothelial cell interleukin-1a. An autocrine mechanism promoting expression of leukocyte adhesion molecules on the vessel surface. J. Clin. Invest. 90(6), 2333-2339 (1992).
    • (1992) J. Clin. Invest. , vol.90 , Issue.6 , pp. 2333-2339
    • Shreeniwas, R.1    Koga, S.2    Karakurum, M.3
  • 105
    • 0036636876 scopus 로고    scopus 로고
    • Developmental differences in the role of interleukins in hyperoxic lung injury in animal models
    • Bhandari V. Developmental differences in the role of interleukins in hyperoxic lung injury in animal models. Front. Biosci. 7, d1624-d1633 (2002).
    • (2002) Front. Biosci. , vol.7
    • Bhandari, V.1
  • 106
    • 0042121356 scopus 로고    scopus 로고
    • Impaired lung function and serum leptin in men and women with normal body weight: A population based study
    • Sin DD, Man SF. Impaired lung function and serum leptin in men and women with normal body weight: a population based study. Thorax 58(8), 695-698 (2003).
    • (2003) Thorax , vol.58 , Issue.8 , pp. 695-698
    • Sin, D.D.1    Man, S.F.2
  • 107
    • 79957945650 scopus 로고    scopus 로고
    • Leptin promotes fibroproliferative acute respiratory distress syndrome by inhibiting peroxisome proliferator-activated receptor-g
    • Jain M, Budinger GR, Lo A et al. Leptin promotes fibroproliferative acute respiratory distress syndrome by inhibiting peroxisome proliferator-activated receptor-{g}. Am. J. Respir. Crit. Care Med. 183(11), 1490-1498 (2011).
    • (2011) Am. J. Respir. Crit. Care Med. , vol.183 , Issue.11 , pp. 1490-1498
    • Jain, M.1    Budinger, G.R.2    Lo, A.3
  • 109
    • 79955491537 scopus 로고    scopus 로고
    • A role for matrix metalloproteinase 9 in IFN g-mediated injury in developing lungs: Relevance to bronchopulmonary dysplasia
    • Harijith A, Choo-Wing R, Cataltepe S et al. A role for matrix metalloproteinase 9 in IFN{g}-mediated injury in developing lungs: relevance to bronchopulmonary dysplasia. Am. J. Respir. Cell Mol. Biol. 44(5), 621-630 (2011).
    • (2011) Am. J. Respir. Cell Mol. Biol. , vol.44 , Issue.5 , pp. 621-630
    • Harijith, A.1    Choo-Wing, R.2    Cataltepe, S.3
  • 110
    • 0032695668 scopus 로고    scopus 로고
    • Association of mannose-binding lectin gene heterogeneity with severity of lung disease and survival in cystic fibrosis
    • Garred P, Pressler T, Madsen HO et al. Association of mannose-binding lectin gene heterogeneity with severity of lung disease and survival in cystic fibrosis. J. Clin. Invest. 104(4), 431-437 (1999).
    • (1999) J. Clin. Invest. , vol.104 , Issue.4 , pp. 431-437
    • Garred, P.1    Pressler, T.2    Madsen, H.O.3
  • 113
    • 77955657700 scopus 로고    scopus 로고
    • Association between mannose-binding lectin, high-sensitivity C-reactive protein and the progression of diabetic nephropathy in Type 1 diabetes
    • Hansen TK, Forsblom C, Saraheimo M et al. Association between mannose-binding lectin, high-sensitivity C-reactive protein and the progression of diabetic nephropathy in Type 1 diabetes. Diabetologia 53(7), 1517-1524 (2010).
    • (2010) Diabetologia , vol.53 , Issue.7 , pp. 1517-1524
    • Hansen, T.K.1    Forsblom, C.2    Saraheimo, M.3
  • 114
    • 33749558979 scopus 로고    scopus 로고
    • Mannose-binding lectin and mortality in Type 2 diabetes
    • Hansen TK, Gall MA, Tarnow L et al. Mannose-binding lectin and mortality in Type 2 diabetes. Arch. Intern. Med. 166(18), 2007-2013 (2006).
    • (2006) Arch. Intern. Med. , vol.166 , Issue.18 , pp. 2007-2013
    • Hansen, T.K.1    Gall, M.A.2    Tarnow, L.3
  • 115
    • 79955531966 scopus 로고    scopus 로고
    • High levels of mannose-binding lectin are associated with poor outcomes after lung transplantation
    • Carroll KE, Dean MM, Heatley SL et al. High levels of mannose-binding lectin are associated with poor outcomes after lung transplantation. Transplantation 91(9), 1044-1049 (2011).
    • (2011) Transplantation , vol.91 , Issue.9 , pp. 1044-1049
    • Carroll, K.E.1    Dean, M.M.2    Heatley, S.L.3
  • 116
    • 41149083693 scopus 로고    scopus 로고
    • Mannose-binding lectin is involved in multiple organ dysfunction syndrome after cardiac surgery: Effects of blood transfusions
    • Bilgin YM, Brand A, Berger SP, Daha MR, Roos A. Mannose-binding lectin is involved in multiple organ dysfunction syndrome after cardiac surgery: effects of blood transfusions. Transfusion 48(4), 601-608 (2008).
    • (2008) Transfusion , vol.48 , Issue.4 , pp. 601-608
    • Bilgin, Y.M.1    Brand, A.2    Berger, S.P.3    Daha, M.R.4    Roos, A.5
  • 117
    • 77952343756 scopus 로고    scopus 로고
    • Influence of functional deficiency of complement mannose-binding lectin on outcome of patients with acute ST-elevation myocardial infarction undergoing primary percutaneous coronary intervention
    • Trendelenburg M, Theroux P, Stebbins A, Granger C, Armstrong P, Pfisterer M. Influence of functional deficiency of complement mannose-binding lectin on outcome of patients with acute ST-elevation myocardial infarction undergoing primary percutaneous coronary intervention. Eur. Heart J. 31(10), 1181-1187 (2010).
    • (2010) Eur. Heart J. , vol.31 , Issue.10 , pp. 1181-1187
    • Trendelenburg, M.1    Theroux, P.2    Stebbins, A.3    Granger, C.4    Armstrong, P.5    Pfisterer, M.6
  • 118
    • 77249163834 scopus 로고    scopus 로고
    • Deficiency of complement factor MBL in a patient required cardiac surgery after an acute myocardial infarction with underlining chronic lymphocytic leukemia
    • Lai LT, Lee DC, Ko W, Shevde K, Zhang M. Deficiency of complement factor MBL in a patient required cardiac surgery after an acute myocardial infarction with underlining chronic lymphocytic leukemia. Int. J. Cardiol. 139(2), e24-e26 (2010).
    • (2010) Int. J. Cardiol. , vol.139 , Issue.2
    • Lai, L.T.1    Lee, D.C.2    Ko, W.3    Shevde, K.4    Zhang, M.5
  • 119
    • 21244496324 scopus 로고    scopus 로고
    • Mannose-binding lectin is a regulator of inflammation that accompanies myocardial ischemia and reperfusion injury
    • Walsh MC, Bourcier T, Takahashi K et al. Mannose-binding lectin is a regulator of inflammation that accompanies myocardial ischemia and reperfusion injury. J. Immunol. 175(1), 541-546 (2005).
    • (2005) J. Immunol. , vol.175 , Issue.1 , pp. 541-546
    • Walsh, M.C.1    Bourcier, T.2    Takahashi, K.3
  • 120
    • 33749152112 scopus 로고    scopus 로고
    • Activation of the lectin pathway by natural IgM in a model of ischemia/reperfusion injury
    • Zhang M, Takahashi K, Alicot EM et al. Activation of the lectin pathway by natural IgM in a model of ischemia/reperfusion injury. J. Immunol. 177(7), 4727-4734 (2006).
    • (2006) J. Immunol. , vol.177 , Issue.7 , pp. 4727-4734
    • Zhang, M.1    Takahashi, K.2    Alicot, E.M.3
  • 121
    • 21044450184 scopus 로고    scopus 로고
    • Mannan-binding lectin recognizes structures on ischaemic reperfused mouse kidneys and is implicated in tissue injury
    • Moller-Kristensen M, Wang W, Ruseva M et al. Mannan-binding lectin recognizes structures on ischaemic reperfused mouse kidneys and is implicated in tissue injury. Scand. J. Immunol. 61(5), 426-434 (2005).
    • (2005) Scand. J. Immunol. , vol.61 , Issue.5 , pp. 426-434
    • Moller-Kristensen, M.1    Wang, W.2    Ruseva, M.3
  • 122
    • 19344377535 scopus 로고    scopus 로고
    • Interactions between the innate immune and blood coagulation systems
    • Esmon CT. Interactions between the innate immune and blood coagulation systems. Trends Immunol. 25(10), 536-542 (2004).
    • (2004) Trends Immunol. , vol.25 , Issue.10 , pp. 536-542
    • Esmon, C.T.1
  • 123
    • 1942439753 scopus 로고    scopus 로고
    • Crosstalk between inflammation and thrombosis
    • Esmon CT. Crosstalk between inflammation and thrombosis. Maturitas 47(4), 305-314 (2004).
    • (2004) Maturitas , vol.47 , Issue.4 , pp. 305-314
    • Esmon, C.T.1
  • 125
    • 0028323245 scopus 로고
    • Elimination of interleukin 6 attenuates coagulation activation in experimental endotoxemia in chimpanzees
    • van der Poll T, Levi M, Hack CE et al. Elimination of interleukin 6 attenuates coagulation activation in experimental endotoxemia in chimpanzees. J. Exp. Med. 179(4), 1253-1259 (1994).
    • (1994) J. Exp. Med. , vol.179 , Issue.4 , pp. 1253-1259
    • Van Der Poll, T.1    Levi, M.2    Hack, C.E.3
  • 126
    • 0027294656 scopus 로고
    • Soluble E-selectin is found in supernatants of activated endothelial cells and is elevated in the serum of patients with septic shock
    • Newman W, Beall LD, Carson CW et al. Soluble E-selectin is found in supernatants of activated endothelial cells and is elevated in the serum of patients with septic shock. J. Immunol. 150(2), 644-654 (1993).
    • (1993) J. Immunol. , vol.150 , Issue.2 , pp. 644-654
    • Newman, W.1    Beall, L.D.2    Carson, C.W.3
  • 127
    • 0036255482 scopus 로고    scopus 로고
    • Markers of endothelial damage in organ dysfunction and sepsis
    • Reinhart K, Bayer O, Brunkhorst F, Meisner M. Markers of endothelial damage in organ dysfunction and sepsis. Crit. Care Med. 30(Suppl. 5), S302-S312 (2002).
    • (2002) Crit. Care Med. , vol.30 , Issue.5
    • Reinhart, K.1    Bayer, O.2    Brunkhorst, F.3    Meisner, M.4
  • 128
    • 0034927833 scopus 로고    scopus 로고
    • Microvascular coagulopathy and disseminated intravascular coagulation
    • S95-S97 discussion
    • ten Cate H, Schoenmakers SH, Franco R et al. Microvascular coagulopathy and disseminated intravascular coagulation. Crit. Care Med. 29(Suppl. 7), S95-S97; discussion S97-S98 (2001).
    • (2001) Crit. Care Med. , vol.29 , Issue.7
    • Ten Cate, H.1    Schoenmakers, S.H.2    Franco, R.3
  • 129
    • 0028897616 scopus 로고
    • Internalization of Staphylococcus aureus by endothelial cells induces cytokine gene expression
    • Yao L, Bengualid V, Lowy FD, Gibbons JJ, Hatcher VB, Berman JW. Internalization of Staphylococcus aureus by endothelial cells induces cytokine gene expression. Infect. Immun. 63(5), 1835-1839 (1995).
    • (1995) Infect. Immun. , vol.63 , Issue.5 , pp. 1835-1839
    • Yao, L.1    Bengualid, V.2    Lowy, F.D.3    Gibbons, J.J.4    Hatcher, V.B.5    Berman, J.W.6
  • 130
    • 0034849547 scopus 로고    scopus 로고
    • Endothelial oxidative stress activates the lectin complement pathway: Role of cytokeratin 1
    • Collard CD, Montalto MC, Reenstra WR, Buras JA, Stahl GL. Endothelial oxidative stress activates the lectin complement pathway: role of cytokeratin 1. Am. J. Pathol. 159(3), 1045-1054 (2001).
    • (2001) Am. J. Pathol. , vol.159 , Issue.3 , pp. 1045-1054
    • Collard, C.D.1    Montalto, M.C.2    Reenstra, W.R.3    Buras, J.A.4    Stahl, G.L.5
  • 131
    • 0035869586 scopus 로고    scopus 로고
    • A keratin peptide inhibits mannose-binding lectin
    • Montalto MC, Collard CD, Buras JA et al. A keratin peptide inhibits mannose-binding lectin. J. Immunol. 166(6), 4148-4153 (2001).
    • (2001) J. Immunol. , vol.166 , Issue.6 , pp. 4148-4153
    • Montalto, M.C.1    Collard, C.D.2    Buras, J.A.3
  • 133
    • 33746862576 scopus 로고    scopus 로고
    • Naturally occurring NF-kB inhibitors
    • Nam NH. Naturally occurring NF-kB inhibitors. Mini. Rev. Med. Chem. 6(8), 945-951 (2006).
    • (2006) Mini. Rev. Med. Chem. , vol.6 , Issue.8 , pp. 945-951
    • Nam, N.H.1
  • 134
    • 70349255738 scopus 로고    scopus 로고
    • Complement protease MASP-1 activates human endothelial cells: PAR4 activation is a link between complement and endothelial function
    • Megyeri M, Mako V, Beinrohr L et al. Complement protease MASP-1 activates human endothelial cells: PAR4 activation is a link between complement and endothelial function. J. Immunol. 183(5), 3409-3416 (2009).
    • (2009) J. Immunol. , vol.183 , Issue.5 , pp. 3409-3416
    • Megyeri, M.1    Mako, V.2    Beinrohr, L.3
  • 135
    • 0033532164 scopus 로고    scopus 로고
    • Molecular cloning of a novel human collectin from liver CL-L1
    • Ohtani K, Suzuki Y, Eda S et al. Molecular cloning of a novel human collectin from liver (CL-L1).J. Biol. Chem. 274(19), 13681-13689 (1999).
    • (1999) J. Biol. Chem. , vol.274 , Issue.19 , pp. 13681-13689
    • Ohtani, K.1    Suzuki, Y.2    Eda, S.3
  • 136
    • 0035941356 scopus 로고    scopus 로고
    • The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells
    • Ohtani K, Suzuki Y, Eda S et al. The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells. J. Biol. Chem. 276(47), 44222-44228 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.47 , pp. 44222-44228
    • Ohtani, K.1    Suzuki, Y.2    Eda, S.3
  • 137
  • 138
    • 77949878087 scopus 로고    scopus 로고
    • Carbohydrate recognition properties of human ficolins: Glycan array screening reveals the sialic acid binding specificity of M-ficolin
    • Gout E, Garlatti V, Smith DF et al. Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity of M-ficolin. J. Biol. Chem. 285(9), 6612-6622 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.9 , pp. 6612-6622
    • Gout, E.1    Garlatti, V.2    Smith, D.F.3
  • 139
    • 33748954258 scopus 로고    scopus 로고
    • Phase I safety tolerability and pharmacokinetic study of recombinant human mannan-binding lectin
    • Petersen KA, Matthiesen F, Agger T et al. Phase I safety, tolerability, and pharmacokinetic study of recombinant human mannan-binding lectin. J. Clin. Immunol. 26(5), 465-475 (2006).
    • (2006) J. Clin. Immunol. , vol.26 , Issue.5 , pp. 465-475
    • Petersen, K.A.1    Matthiesen, F.2    Agger, T.3
  • 140
    • 77955283062 scopus 로고    scopus 로고
    • A novel L-ficolin/mannose-binding lectin chimeric molecule with enhanced activity against Ebola virus
    • Michelow IC, Dong M, Mungall BA et al. A novel L-ficolin/mannose-binding lectin chimeric molecule with enhanced activity against Ebola virus. J. Biol. Chem. 285(32), 24729-24739 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.32 , pp. 24729-24739
    • Michelow, I.C.1    Dong, M.2    Mungall, B.A.3
  • 141
    • 33845265013 scopus 로고    scopus 로고
    • Variable mannose-binding lectin expression during postoperative acute-phase response
    • Van Till JW, Boermeester MA, Modderman PW et al. Variable mannose-binding lectin expression during postoperative acute-phase response. Surg. Infect. (Larchmt).7(5), 443-452 (2006).
    • (2006) Surg. Infect. Larchmt , vol.7 , Issue.5 , pp. 443-452
    • Van Till, J.W.1    Boermeester, M.A.2    Modderman, P.W.3


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