메뉴 건너뛰기




Volumn 166, Issue , 1998, Pages 15-26

The phylogeny and evolution of the thioester bond-containing proteins C3, C4 and α2-macroglobulin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2 MACROGLOBULIN; COMPLEMENT COMPONENT C3; COMPLEMENT COMPONENT C4; THIOESTER;

EID: 0032416611     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-065X.1998.tb01249.x     Document Type: Review
Times cited : (156)

References (89)
  • 1
    • 0001429001 scopus 로고
    • The role of sulphur in proteins
    • Nevra TI.H, ed. New York: Academic Press
    • Liu T. The role of sulphur in proteins. In: Nevra TI.H, ed. The proteins. Vol 3. New York: Academic Press; 1976. p. 239-402
    • (1976) The Proteins , vol.3 , pp. 239-402
    • Liu, T.1
  • 2
    • 0023173876 scopus 로고
    • Mechanism of action of glutathione-dependant enzymes
    • Douglas RT. Mechanism of action of glutathione-dependant enzymes. Adv Immunol 1987;59:103-137.
    • (1987) Adv Immunol , vol.59 , pp. 103-137
    • Douglas, R.T.1
  • 3
    • 0002764047 scopus 로고
    • The phylogeny and evolution of the complement system
    • Whaley K, Loos M, Weiler JM, eds. London: Kluwer
    • Dodds AW, Day AJ. The phylogeny and evolution of the complement system. In: Whaley K, Loos M, Weiler JM, eds. Complement in health and disease. 2nd ed. London: Kluwer; 1993. p. 39-88.
    • (1993) Complement in Health and Disease. 2nd Ed. , pp. 39-88
    • Dodds, A.W.1    Day, A.J.2
  • 4
    • 0002828688 scopus 로고    scopus 로고
    • Complement-related proteins in invertebrates
    • Soderhall K, Iwanaga S, Vasta GR, eds. Fair Haven (NJ): SOS Publications
    • Dodds AW, Day AJ. Complement-related proteins in invertebrates. In: Soderhall K, Iwanaga S, Vasta GR, eds. New directions in invertebrate immunology. Fair Haven (NJ): SOS Publications; 1996. p. 303-341.
    • (1996) New Directions in Invertebrate Immunology , pp. 303-341
    • Dodds, A.W.1    Day, A.J.2
  • 6
    • 0028958669 scopus 로고
    • The CD19/CR2/TAPA-1 complex of B lymphocytes: Linking natural and acquired immunity
    • Fearon DT, Carter RH. The CD19/CR2/TAPA-1 complex of B lymphocytes: linking natural and acquired immunity. Annu Rev Immunol 1995;13:127-149.
    • (1995) Annu Rev Immunol , vol.13 , pp. 127-149
    • Fearon, D.T.1    Carter, R.H.2
  • 7
    • 0031921084 scopus 로고    scopus 로고
    • The role of complement and complement receptors in induction and regulation of immunity
    • Carroll MC. The role of complement and complement receptors in induction and regulation of immunity. Annu Rev Immunol 1998;16:545-568.
    • (1998) Annu Rev Immunol , vol.16 , pp. 545-568
    • Carroll, M.C.1
  • 8
    • 0028235185 scopus 로고
    • Complement activation by recombinant HIV-1 glycoprotein gp120
    • Susal C, Kirschfink M, Kropelin M, Daniel V, Opelz G. Complement activation by recombinant HIV-1 glycoprotein gp120. J Immunol 1994;152:6028-6034
    • (1994) J Immunol , vol.152 , pp. 6028-6034
    • Susal, C.1    Kirschfink, M.2    Kropelin, M.3    Daniel, V.4    Opelz, G.5
  • 9
    • 0010417592 scopus 로고
    • Common evolutionary origin of α-2-macroglobulin and complement components C3 and C4
    • Sottrup Jensen L, et al. Common evolutionary origin of α-2-macroglobulin and complement components C3 and C4. Proc Natl Acad Sci USA 1985;82:9-13.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 9-13
    • Sottrup Jensen, L.1
  • 10
    • 0020164637 scopus 로고
    • Evolution of α2-macroglobulin. The demonstration in a variety of vertebrate species of a protein resembling human α2-macroglobulin
    • Starkey PM, Barrett AJ. Evolution of α2-macroglobulin. The demonstration in a variety of vertebrate species of a protein resembling human α2-macroglobulin. Biochem J 1982;205:91-95.
    • (1982) Biochem J , vol.205 , pp. 91-95
    • Starkey, P.M.1    Barrett, A.J.2
  • 11
    • 0028670452 scopus 로고
    • α2-Macroglobulin, complement, and biologic defense: Antigens, growth factors, microbial proteases, and receptor ligation
    • Chu CT, Pizzo SV. α2-Macroglobulin, complement, and biologic defense: antigens, growth factors, microbial proteases, and receptor ligation. Lab Invest 1994;71:792-812.
    • (1994) Lab Invest , vol.71 , pp. 792-812
    • Chu, C.T.1    Pizzo, S.V.2
  • 12
    • 0028127044 scopus 로고
    • Role of internal thiol esters in the α-macroglobulin-proteinase binding mechanism
    • Sottrup Jensen L. Role of internal thiol esters in the α-macroglobulin-proteinase binding mechanism. Ann N Y Acad Sci 1994;737:172-187.
    • (1994) Ann N Y Acad Sci , vol.737 , pp. 172-187
    • Sottrup Jensen, L.1
  • 13
    • 0024383768 scopus 로고
    • Proteinase binding and inhibition by the monomeric α-macroglobulin rat α 1 inhibitor3
    • Enghild JJ, Salvesen G, Thogersen IB, Pizzo SV. Proteinase binding and inhibition by the monomeric α-macroglobulin rat α 1 Inhibitor3. J Biol Chem 1989;264:11428-11435.
    • (1989) J Biol Chem , vol.264 , pp. 11428-11435
    • Enghild, J.J.1    Salvesen, G.2    Thogersen, I.B.3    Pizzo, S.V.4
  • 14
    • 0021099670 scopus 로고
    • An endopeptidase inhibitor, similar to mammalian α2-macroglobulin, detected in the hemolymph of an invertebrate, Limulus polyphemus
    • Quigley JP, Armstrong PB. An endopeptidase inhibitor, similar to mammalian α2-macroglobulin, detected in the hemolymph of an invertebrate, Limulus polyphemus. J Biol Chem 1983;258:7903-7906.
    • (1983) J Biol Chem , vol.258 , pp. 7903-7906
    • Quigley, J.P.1    Armstrong, P.B.2
  • 15
    • 0021930639 scopus 로고
    • An α2-macroglobulin-like activity in the blood of chelicerate and mandibulate arthropods
    • Armstrong PB, Rossner MT, Quigley JP. An α2-macroglobulin-like activity in the blood of chelicerate and mandibulate arthropods. J Exp Zool 1985;236:1-9.
    • (1985) J Exp Zool , vol.236 , pp. 1-9
    • Armstrong, P.B.1    Rossner, M.T.2    Quigley, J.P.3
  • 16
    • 0345317664 scopus 로고
    • Purification of a proteinase inhibitor from hemolymph of sea crab (Portunus trituberculatus)
    • Kim SB, Lee KS, Yoo BS, Chang CS, Kim JK. Purification of a proteinase inhibitor from hemolymph of sea crab (Portunus trituberculatus). Korean J Biochem 1993;26:511-517.
    • (1993) Korean J Biochem , vol.26 , pp. 511-517
    • Kim, S.B.1    Lee, K.S.2    Yoo, B.S.3    Chang, C.S.4    Kim, J.K.5
  • 17
    • 0023665215 scopus 로고
    • A functional, thioester-containing α2-macroglobulin homologue isolated from the hemolymph of the American lobster (Homarus americanus)
    • Spycher SE, Arya S, Isenman DE, Painter RH. A functional, thioester-containing α2-macroglobulin homologue isolated from the hemolymph of the American lobster (Homarus americanus). J Biol Chem 1987;262:14606-14611.
    • (1987) J Biol Chem , vol.262 , pp. 14606-14611
    • Spycher, S.E.1    Arya, S.2    Isenman, D.E.3    Painter, R.H.4
  • 18
    • 0023684972 scopus 로고
    • Purification and characterization of an α2-macroglobulin-like proteinase inhibitor from plasma of the crayfish Pacifastacus leniusculus
    • Hergenhahn HG, Hall M, Soderhall K. Purification and characterization of an α2-macroglobulin-like proteinase inhibitor from plasma of the crayfish Pacifastacus leniusculus. Biochem J 1988;255:801-806.
    • (1988) Biochem J , vol.255 , pp. 801-806
    • Hergenhahn, H.G.1    Hall, M.2    Soderhall, K.3
  • 20
    • 0026721960 scopus 로고
    • Purification and characterization of an α-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris
    • Thogersen IB, Salvesen G, Brucato FH, Pizzo SV, Enghild JJ. Purification and characterization of an α-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris. Biochem J 1992;285:521-527.
    • (1992) Biochem J , vol.285 , pp. 521-527
    • Thogersen, I.B.1    Salvesen, G.2    Brucato, F.H.3    Pizzo, S.V.4    Enghild, J.J.5
  • 21
    • 0029849796 scopus 로고    scopus 로고
    • Purification and characterization of a tetrameric α-macroglobulin proteinase inhibitor from the gastropod mollusc Biomphalaria glabrata
    • Bender RC, Bayne CJ. Purification and characterization of a tetrameric α-macroglobulin proteinase inhibitor from the gastropod mollusc Biomphalaria glabrata. Biochem J 1996;316:893-900.
    • (1996) Biochem J , vol.316 , pp. 893-900
    • Bender, R.C.1    Bayne, C.J.2
  • 22
    • 0026038884 scopus 로고
    • Reaction of proteinases with α2-macroglobulin from the American horseshoe crab, Limulus
    • Quigley JP, Ikai A, Arakawa H, Osada T, Armstrong PB. Reaction of proteinases with α2-macroglobulin from the American horseshoe crab, Limulus. J Biol Chem 1991;266:19426-19431.
    • (1991) J Biol Chem , vol.266 , pp. 19426-19431
    • Quigley, J.P.1    Ikai, A.2    Arakawa, H.3    Osada, T.4    Armstrong, P.B.5
  • 23
    • 0030577021 scopus 로고    scopus 로고
    • Localisation of the major reactive lysine residue involved in the self-crosslinking of proteinase-activated Limulus α2-macroglobulin
    • Dolmer K, Husted LB, Armstrong PB, Sottrup Jensen L. Localisation of the major reactive lysine residue involved in the self-crosslinking of proteinase-activated Limulus α2-macroglobulin. FEBS Lett 1996;393:37-40.
    • (1996) FEBS Lett , vol.393 , pp. 37-40
    • Dolmer, K.1    Husted, L.B.2    Armstrong, P.B.3    Sottrup Jensen, L.4
  • 24
    • 8044252161 scopus 로고    scopus 로고
    • Molecular cloning of Limulus α2-macroglobulin
    • Iwaki D, et al. Molecular cloning of Limulus α2-macroglobulin. Eur J Biochem 1996;242:822-831.
    • (1996) Eur J Biochem , vol.242 , pp. 822-831
    • Iwaki, D.1
  • 25
    • 0024990650 scopus 로고
    • α-Macroglobulin from Limulus polyphemus exhibits proteinase inhibitory activity and participates in a hemolytic system
    • Enghild JJ, et al. α-Macroglobulin from Limulus polyphemus exhibits proteinase inhibitory activity and participates in a hemolytic system. Biochemistry 1990;29:10070-10080.
    • (1990) Biochemistry , vol.29 , pp. 10070-10080
    • Enghild, J.J.1
  • 26
    • 0031595407 scopus 로고    scopus 로고
    • α2-Macroglobulin does not function as a C3 homologue in the plasma hemolytic system of the American horse-shoe crab, Limulus
    • Armstrong PB, Melchior R, Swarakar S, Quigley JP. α2-Macroglobulin does not function as a C3 homologue in the plasma hemolytic system of the American horse-shoe crab, Limulus. Mol Immunol 1998;35:47-53.
    • (1998) Mol Immunol , vol.35 , pp. 47-53
    • Armstrong, P.B.1    Melchior, R.2    Swarakar, S.3    Quigley, J.P.4
  • 27
    • 0028287043 scopus 로고
    • Invertebrate α2-macroglobulin: Structure-function and the ancient thiol ester bond
    • Quigley JP, Armstrong PB. Invertebrate α2-macroglobulin: structure-function and the ancient thiol ester bond. Ann N Y Acad Sci 1994;712:131-145.
    • (1994) Ann N Y Acad Sci , vol.712 , pp. 131-145
    • Quigley, J.P.1    Armstrong, P.B.2
  • 29
    • 0021166726 scopus 로고
    • Role of endogenous proteinase inhibitors in the regulation of the blood clotting system of the horseshoe crab, Limulus polyphemus
    • Armstrong PB, Levin J, Quigley JP. Role of endogenous proteinase inhibitors in the regulation of the blood clotting system of the horseshoe crab, Limulus polyphemus. Thromb Haemost 1984;52:117-120
    • (1984) Thromb Haemost , vol.52 , pp. 117-120
    • Armstrong, P.B.1    Levin, J.2    Quigley, J.P.3
  • 30
    • 0023656771 scopus 로고
    • Purification and characterization of a high-Mr proteinase inhibitor of pro-phenol oxidase activation from crayfish plasma
    • Hergenhahn HG, Aspan A, Soderhall K. Purification and characterization of a high-Mr proteinase inhibitor of pro-phenol oxidase activation from crayfish plasma. Biochem J 1987;248:223-228
    • (1987) Biochem J , vol.248 , pp. 223-228
    • Hergenhahn, H.G.1    Aspan, A.2    Soderhall, K.3
  • 31
    • 0029928757 scopus 로고    scopus 로고
    • The role of hemolymph coagulation in innate immunity
    • Muta T, Iwanaga S. The role of hemolymph coagulation in innate immunity. Curr Opin Immunol 1996;8:41-47.
    • (1996) Curr Opin Immunol , vol.8 , pp. 41-47
    • Muta, T.1    Iwanaga, S.2
  • 32
    • 0032005367 scopus 로고    scopus 로고
    • Role of prophenoloxidase-activating system in invertebrate immunity
    • Soderhall K, Cerenius L. Role of prophenoloxidase-activating system in invertebrate immunity. Cur Opin Immunol 1998;10:23-28.
    • (1998) Cur Opin Immunol , vol.10 , pp. 23-28
    • Soderhall, K.1    Cerenius, L.2
  • 33
    • 0001665337 scopus 로고
    • Surface localisation and high affinity for calcium of a 500kd liver membrane protein closely related to LDL receptor suggests a physiological role as a lipoprotein receptor
    • Herz J, Hamann U, Rogne S, Myklebost O, Gausepohl H, Stanley KK. Surface localisation and high affinity for calcium of a 500kd liver membrane protein closely related to LDL receptor suggests a physiological role as a lipoprotein receptor. EMBO J 1988;7:4119-4127
    • (1988) EMBO J , vol.7 , pp. 4119-4127
    • Herz, J.1    Hamann, U.2    Rogne, S.3    Myklebost, O.4    Gausepohl, H.5    Stanley, K.K.6
  • 34
    • 0028019068 scopus 로고
    • Complete cloning and sequencing of rat gp330/"megalin", a distinctive member of the low density lipoprotein receptor gene family
    • Saito A, Pietromonaco S, Loo AK, Farquhar MG. Complete cloning and sequencing of rat gp330/"megalin", a distinctive member of the low density lipoprotein receptor gene family. Proc Natl Acad Sci USA 1994;91:9725-9729.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9725-9729
    • Saito, A.1    Pietromonaco, S.2    Loo, A.K.3    Farquhar, M.G.4
  • 35
    • 0027298893 scopus 로고
    • A gene for a low density lipoprotein receptor-related protein in the nematode Caenorhabditis elegans
    • Yochem J, Greenwald I. A gene for a low density lipoprotein receptor-related protein in the nematode Caenorhabditis elegans. Proc Natl Acad Sci USA 1993;90:4572-4576.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4572-4576
    • Yochem, J.1    Greenwald, I.2
  • 36
    • 0028173897 scopus 로고
    • Structures and functions of multiligand lipoprotein receptors: Macrophage scavenger receptors and LDL receptor-related protein (LRP)
    • Krieger M, Herz J. Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor-related protein (LRP). Annu Rev Biochem 1994;63:601-637.
    • (1994) Annu Rev Biochem , vol.63 , pp. 601-637
    • Krieger, M.1    Herz, J.2
  • 37
    • 0028181155 scopus 로고
    • The α2-macroglobulin receptor and epithelial glycoprotein-330: Two giant receptors mediating endocytosis of multiple ligands
    • Moestrup SK. The α2-macroglobulin receptor and epithelial glycoprotein-330: two giant receptors mediating endocytosis of multiple ligands. Biochim Biophys Acta 1994;1197:197-213.
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 197-213
    • Moestrup, S.K.1
  • 39
    • 0028952441 scopus 로고
    • Isolation, primary structure, and evolution of the third component of chicken complement and evidence for a new member of the α2-macroglobulin family
    • Mavroidis M, Sunyer JO, Lambris JD. Isolation, primary structure, and evolution of the third component of chicken complement and evidence for a new member of the α2-macroglobulin family. J Immunol 1995;154:2164-2174.
    • (1995) J Immunol , vol.154 , pp. 2164-2174
    • Mavroidis, M.1    Sunyer, J.O.2    Lambris, J.D.3
  • 40
    • 0027380116 scopus 로고
    • Third component of trout complement. cDNA cloning and conservation of functional sites
    • Lambris JD, Lao Z, Pang J, Alsenz J. Third component of trout complement. cDNA cloning and conservation of functional sites. J Immunol 1993;151:6123-6134.
    • (1993) J Immunol , vol.151 , pp. 6123-6134
    • Lambris, J.D.1    Lao, Z.2    Pang, J.3    Alsenz, J.4
  • 41
    • 0026522052 scopus 로고
    • Complete complementary DNA sequence of the third component of complement of lamprey. Implication for the evolution of thioester containing proteins
    • Nonaka M, Takahashi M. Complete complementary DNA sequence of the third component of complement of lamprey. Implication for the evolution of thioester containing proteins. J Immunol 1992;148:3290-3295.
    • (1992) J Immunol , vol.148 , pp. 3290-3295
    • Nonaka, M.1    Takahashi, M.2
  • 43
    • 0344022550 scopus 로고    scopus 로고
    • Opsonic complement C3 in the solitary ascidian Halocynthia roretzi
    • In press
    • Ji X, et al. Opsonic complement C3 in the solitary ascidian Halocynthia roretzi. J Immunol (In press).
    • J Immunol
    • Ji, X.1
  • 44
    • 0032521276 scopus 로고    scopus 로고
    • Sea urchin coelomocytes specifically express a homologue of the complement component C3
    • Al Sharif WZ, Sunyer JO, Lambris JD, Smith LC. Sea urchin coelomocytes specifically express a homologue of the complement component C3. J Immunol 1998;160:2983-2997.
    • (1998) J Immunol , vol.160 , pp. 2983-2997
    • Al Sharif, W.Z.1    Sunyer, J.O.2    Lambris, J.D.3    Smith, L.C.4
  • 45
    • 0028920683 scopus 로고
    • The third component of Xenopus complement: cDNA cloning, structural and functional analysis, and evidence for an alternate C3 transcript
    • Lambris JD, et al. The third component of Xenopus complement: cDNA cloning, structural and functional analysis, and evidence for an alternate C3 transcript. Eur J Immunol 1995;25:572-578.
    • (1995) Eur J Immunol , vol.25 , pp. 572-578
    • Lambris, J.D.1
  • 46
    • 0025023651 scopus 로고
    • Molecular aspects of C3 interactions and structural/functional analysis of C3 from different species
    • Becherer JD, Alsenz J, Lambris JD. Molecular aspects of C3 interactions and structural/functional analysis of C3 from different species. Curr Top Microbiol Immunol 1990;153:45-72.
    • (1990) Curr Top Microbiol Immunol , vol.153 , pp. 45-72
    • Becherer, J.D.1    Alsenz, J.2    Lambris, J.D.3
  • 47
    • 0028577729 scopus 로고
    • Molecular cloning and derived primary structure of cobra venom factor
    • Fritzinger DC, Bredehorst R, Vogel CW. Molecular cloning and derived primary structure of cobra venom factor. Proc Natl Acad Sci USA 1994;91:12775-12779.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12775-12779
    • Fritzinger, D.C.1    Bredehorst, R.2    Vogel, C.W.3
  • 48
    • 0019303559 scopus 로고
    • Inherited structural polymorphism of the fourth component of human complement
    • Awdeh ZL, Alper CA. Inherited structural polymorphism of the fourth component of human complement. Proc Natl Acad Sci USA 1980;77:3576-3580.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 3576-3580
    • Awdeh, Z.L.1    Alper, C.A.2
  • 49
    • 0021472477 scopus 로고
    • A comparison of the properties of two classes, C4A and C4B, of the human complement component C4
    • Law SKA, Dodds AW, Porter RR. A comparison of the properties of two classes, C4A and C4B, of the human complement component C4. EMBO J 1984;3:1819-1823.
    • (1984) EMBO J , vol.3 , pp. 1819-1823
    • Law, S.K.A.1    Dodds, A.W.2    Porter, R.R.3
  • 50
    • 0021259318 scopus 로고
    • The molecular basis for the difference in immune hemolysis activity of the Chido and Rodgers isotypes of human complement component C4
    • Isenman DE, Young JR. The molecular basis for the difference in immune hemolysis activity of the Chido and Rodgers isotypes of human complement component C4. J Immunol 1984;132:3019-3027.
    • (1984) J Immunol , vol.132 , pp. 3019-3027
    • Isenman, D.E.1    Young, J.R.2
  • 51
    • 0022123973 scopus 로고
    • The origin of the very variable haemolytic activities of the common human complement component C4 allotypes including C4-A6
    • Dodds AW, Law SKA, Porter RR. The origin of the very variable haemolytic activities of the common human complement component C4 allotypes including C4-A6. EMBO J 1985;4:2239-2244.
    • (1985) EMBO J , vol.4 , pp. 2239-2244
    • Dodds, A.W.1    Law, S.K.A.2    Porter, R.R.3
  • 52
    • 0022917255 scopus 로고
    • The purification and properties of some less common allotypes of the fourth component of human complement
    • Dodds AW, Law SKA, Porter RR. The purification and properties of some less common allotypes of the fourth component of human complement. Immunogenetics 1986;24:279-285.
    • (1986) Immunogenetics , vol.24 , pp. 279-285
    • Dodds, A.W.1    Law, S.K.A.2    Porter, R.R.3
  • 53
    • 0021165944 scopus 로고
    • The structural basis of the multiple forms of human complement component C4
    • Belt KT, Carroll MC, Porter RR. The structural basis of the multiple forms of human complement component C4. Cell 1984;36:907-914.
    • (1984) Cell , vol.36 , pp. 907-914
    • Belt, K.T.1    Carroll, M.C.2    Porter, R.R.3
  • 55
    • 0022814528 scopus 로고
    • Structural basis of the polymorphism of human complement components C4A and C4B: Gene size, reactivity and antigenicity
    • Yu CY, Belt KT, Giles CM, Campbell RD, Porter RR. Structural basis of the polymorphism of human complement components C4A and C4B: gene size, reactivity and antigenicity. EMBO J 1986;5:2873-2881.
    • (1986) EMBO J , vol.5 , pp. 2873-2881
    • Yu, C.Y.1    Belt, K.T.2    Giles, C.M.3    Campbell, R.D.4    Porter, R.R.5
  • 56
    • 0022183833 scopus 로고
    • Complete nucleotide and derived amino acid sequences of the fourth component of mouse complement (C4). Evolutionary aspects
    • Nonaka M, Nakayama K, Yeul YD, Takahashi M. Complete nucleotide and derived amino acid sequences of the fourth component of mouse complement (C4). Evolutionary aspects. J Biol Chem 1985;260:10936-10943.
    • (1985) J Biol Chem , vol.260 , pp. 10936-10943
    • Nonaka, M.1    Nakayama, K.2    Yeul, Y.D.3    Takahashi, M.4
  • 57
    • 0023883825 scopus 로고
    • Structural basis of the binding specificity of the thioester-containing proteins, C4, C3 and α-2-macroglobulin
    • Dodds AW, Law SKA. Structural basis of the binding specificity of the thioester-containing proteins, C4, C3 and α-2-macroglobulin. Complement 1988;5:89-97.
    • (1988) Complement , vol.5 , pp. 89-97
    • Dodds, A.W.1    Law, S.K.A.2
  • 58
    • 0025089362 scopus 로고
    • Substitution of a single amino acid (aspartic acid for histidine) converts the functional activity of human complement C4B to C4A
    • Carroll MC, Fathallah DM, Bergamaschini L, Alicot EM, Isenman DE. Substitution of a single amino acid (aspartic acid for histidine) converts the functional activity of human complement C4B to C4A. Proc Natl Acad Sci USA 1990;87:6868-6872
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6868-6872
    • Carroll, M.C.1    Fathallah, D.M.2    Bergamaschini, L.3    Alicot, E.M.4    Isenman, D.E.5
  • 59
    • 0027419950 scopus 로고
    • Covalent binding properties of the human complement protein C4 and hydrolysis rate of the internal thioester upon activation
    • Sepp A, Dodds AW, Anderson MJ, Campbell RD, Willis AC, Law SK. Covalent binding properties of the human complement protein C4 and hydrolysis rate of the internal thioester upon activation. Protein Sci 1993;2:706-716.
    • (1993) Protein Sci , vol.2 , pp. 706-716
    • Sepp, A.1    Dodds, A.W.2    Anderson, M.J.3    Campbell, R.D.4    Willis, A.C.5    Law, S.K.6
  • 60
    • 0030053692 scopus 로고    scopus 로고
    • The reaction mechanism of the internal thioester in the human complement component C4
    • Dodds AW, Ren XD, Willis AC, Law SK. The reaction mechanism of the internal thioester in the human complement component C4. Nature 1996;379:177-179.
    • (1996) Nature , vol.379 , pp. 177-179
    • Dodds, A.W.1    Ren, X.D.2    Willis, A.C.3    Law, S.K.4
  • 62
    • 0032557324 scopus 로고    scopus 로고
    • X-ray structure of C3d: A C3 fragment and ligand for complement receptor 2
    • Nagar B, Jones RG, Diefenbach RJ, Isenman DE, Rini JM. X-ray structure of C3d: a C3 fragment and ligand for complement receptor 2. Science 1998;280:1277-1281.
    • (1998) Science , vol.280 , pp. 1277-1281
    • Nagar, B.1    Jones, R.G.2    Diefenbach, R.J.3    Isenman, D.E.4    Rini, J.M.5
  • 63
    • 0032051769 scopus 로고    scopus 로고
    • Isolation and initial characterisation of complement components C3 and C4 of the nurse shark and the channel catfish
    • Dodds AW, Smith SL, Levine RP, Willis AC. Isolation and initial characterisation of complement components C3 and C4 of the nurse shark and the channel catfish. Dev Comp Immunol 1998;22:207-216.
    • (1998) Dev Comp Immunol , vol.22 , pp. 207-216
    • Dodds, A.W.1    Smith, S.L.2    Levine, R.P.3    Willis, A.C.4
  • 64
    • 0019510781 scopus 로고
    • The complement system in rainbow trout (Salmo gairdneri). II. Purification and characterization of the fifth component (C5)
    • Nonaka M, Natsuume Sakai S, Takahashi M. The complement system in rainbow trout (Salmo gairdneri). II. Purification and characterization of the fifth component (C5). J Immunol 1981;126:1495-1498.
    • (1981) J Immunol , vol.126 , pp. 1495-1498
    • Nonaka, M.1    Natsuume Sakai, S.2    Takahashi, M.3
  • 65
    • 0030028797 scopus 로고    scopus 로고
    • Sea urchin genes expressed in activated coelomocytes are identified by expressed sequence tags. Complement homologues and other putative immune response genes suggest immune system homology within the deuterostomes
    • Smith LC, Chang L, Britten RJ, Davidson EH. Sea urchin genes expressed in activated coelomocytes are identified by expressed sequence tags. Complement homologues and other putative immune response genes suggest immune system homology within the deuterostomes. J Immunol 1996;156:593-602.
    • (1996) J Immunol , vol.156 , pp. 593-602
    • Smith, L.C.1    Chang, L.2    Britten, R.J.3    Davidson, E.H.4
  • 66
    • 0018101172 scopus 로고
    • Chido and Rodgers blood groups are distinct antigenic components of human complement C4
    • O'Neill GJ, Yang SY, Tegoli J, Berger R, Dupont B. Chido and Rodgers blood groups are distinct antigenic components of human complement C4. Nature 1978;273:668-670.
    • (1978) Nature , vol.273 , pp. 668-670
    • O'Neill, G.J.1    Yang, S.Y.2    Tegoli, J.3    Berger, R.4    Dupont, B.5
  • 67
    • 0030732316 scopus 로고    scopus 로고
    • New insights into the genomic organization and origin of the major histocompatibility complex: Role of chromosomal (genome) duplication in the emergence of the adaptive immune system
    • Kasahara M. New insights into the genomic organization and origin of the major histocompatibility complex: role of chromosomal (genome) duplication in the emergence of the adaptive immune system. Hereditas 1997;127:59-65.
    • (1997) Hereditas , vol.127 , pp. 59-65
    • Kasahara, M.1
  • 68
    • 0030902728 scopus 로고    scopus 로고
    • Chromosomal duplication and the emergence of the adaptive immune system
    • Kasahara M, Nakaya J, Satta Y, Takahata N. Chromosomal duplication and the emergence of the adaptive immune system. Trends Genet 1997 13:90-92.
    • (1997) Trends Genet , vol.13 , pp. 90-92
    • Kasahara, M.1    Nakaya, J.2    Satta, Y.3    Takahata, N.4
  • 69
    • 0028296396 scopus 로고
    • Phylogeny of the C3/C4/C5 complement-component gene family indicates that CS diverged first
    • Hughes AL. Phylogeny of the C3/C4/C5 complement-component gene family indicates that CS diverged first. Mol Biol Evol 1994;11:417-25.
    • (1994) Mol Biol Evol , vol.11 , pp. 417-425
    • Hughes, A.L.1
  • 70
    • 0031238874 scopus 로고    scopus 로고
    • Molecular evolution of the vertebrate immune system
    • Hughes AL, Yeager M. Molecular evolution of the vertebrate immune system. Bioessays 1997;19:777-786.
    • (1997) Bioessays , vol.19 , pp. 777-786
    • Hughes, A.L.1    Yeager, M.2
  • 71
    • 0025070126 scopus 로고
    • Difference between C4A and C4B in the handling of immune complexes: The enhancement of CR1 binding is more important than the inhibition of immunoprecipitation
    • Gatenby PA, Barbosa JE, Lachmann PJ. Difference between C4A and C4B in the handling of immune complexes: the enhancement of CR1 binding is more important than the inhibition of immunoprecipitation. Clin Exp Immunol 1990;79:158-163.
    • (1990) Clin Exp Immunol , vol.79 , pp. 158-163
    • Gatenby, P.A.1    Barbosa, J.E.2    Lachmann, P.J.3
  • 72
    • 0345316677 scopus 로고    scopus 로고
    • Cloning of three trout C3 isoforms: Structural, functional and phylogenetic analysis
    • Sarrias MR, Zarkadis I, Sunyer JO, Lambris JD. Cloning of three trout C3 isoforms: structural, functional and phylogenetic analysis. Mol Immunol 1998;35:370.
    • (1998) Mol Immunol , vol.35 , pp. 370
    • Sarrias, M.R.1    Zarkadis, I.2    Sunyer, J.O.3    Lambris, J.D.4
  • 74
    • 0345316676 scopus 로고    scopus 로고
    • Molecular cloning and linkage analysis of Japanese Medaki fish complement C3 and C4
    • Kuroda N, Naruse K, Shima A, Sasaki M, Nonaka M. Molecular cloning and linkage analysis of Japanese Medaki fish complement C3 and C4. Mol Immunol 1998;35:367.
    • (1998) Mol Immunol , vol.35 , pp. 367
    • Kuroda, N.1    Naruse, K.2    Shima, A.3    Sasaki, M.4    Nonaka, M.5
  • 76
    • 0030461585 scopus 로고    scopus 로고
    • Cloning and sequencing of cDNAs encoding plasma α-macroglobulin and murinoglobulin from guinea pig: Implications for molecular evolution of α-macroglobulin family
    • Iwasaki H, Suzuki Y, Sinohara H. Cloning and sequencing of cDNAs encoding plasma α-macroglobulin and murinoglobulin from guinea pig: implications for molecular evolution of α-macroglobulin family. J Biochem Tokyo 1996;120:1167-1175.
    • (1996) J Biochem Tokyo , vol.120 , pp. 1167-1175
    • Iwasaki, H.1    Suzuki, Y.2    Sinohara, H.3
  • 77
    • 0021840095 scopus 로고
    • Nucleotide sequence of cDNA encoding human α2-macroglobulin and assignment of the chromosomal locus
    • Kan CC, Solomon E, Belt KT, Chain AC, Hiorns LR, Fey G. Nucleotide sequence of cDNA encoding human α2-macroglobulin and assignment of the chromosomal locus. Proc Natl Acad Sci USA 1985;82:2282-2286.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2282-2286
    • Kan, C.C.1    Solomon, E.2    Belt, K.T.3    Chain, A.C.4    Hiorns, L.R.5    Fey, G.6
  • 78
    • 0021747841 scopus 로고
    • Partial primary structure of human pregnancy zone protein: Extensive sequence homology with human α2-macroglobulin
    • Sottrup Jensen L, Folkersen J, Kristensen T, Tack BF. Partial primary structure of human pregnancy zone protein: extensive sequence homology with human α2-macroglobulin. Proc Natl Acad Sci USA 1984;81:7353-7357.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7353-7357
    • Sottrup Jensen, L.1    Folkersen, J.2    Kristensen, T.3    Tack, B.F.4
  • 79
    • 0026540595 scopus 로고
    • cDNA cloning and sequencing of rat α1-macroglobulin
    • Warmegard B, Martin N, Johansson S. cDNA cloning and sequencing of rat α1-macroglobulin. Biochemistry 1992;31:2346-2352.
    • (1992) Biochemistry , vol.31 , pp. 2346-2352
    • Warmegard, B.1    Martin, N.2    Johansson, S.3
  • 80
    • 0022413171 scopus 로고
    • Molecular cloning of DNA complementary to rat α2-macroglobulin mRNA
    • Hayashida K, et al. Molecular cloning of DNA complementary to rat α2-macroglobulin mRNA. J Biol Chem 1985;260:14224-14229.
    • (1985) J Biol Chem , vol.260 , pp. 14224-14229
    • Hayashida, K.1
  • 82
    • 0023245321 scopus 로고
    • Identification and sequencing of cDNA clones for the rodent negative acute-phase protein α1-inhibitor 3
    • Schweizer M, et al. Identification and sequencing of cDNA clones for the rodent negative acute-phase protein α1-inhibitor 3. Eur J Biochem 1987;164:375-381.
    • (1987) Eur J Biochem , vol.164 , pp. 375-381
    • Schweizer, M.1
  • 83
    • 0026478909 scopus 로고
    • The thioester and isotypic sites of complement component C4 in sheep and cattle
    • Ren XD, Dodds AW, Law SK. The thioester and isotypic sites of complement component C4 in sheep and cattle. Immunogenetics 1993;37:120-128.
    • (1993) Immunogenetics , vol.37 , pp. 120-128
    • Ren, X.D.1    Dodds, A.W.2    Law, S.K.3
  • 84
    • 0029875679 scopus 로고    scopus 로고
    • Fourth component of Xenopus laevis complement: cDNA cloning and linkage analysis of the frog MHC
    • Mo R, Kato Y, Nonaka M, Nakayama K, Takahashi M. Fourth component of Xenopus laevis complement: cDNA cloning and linkage analysis of the frog MHC. Immunogenetics 1996;43:360-369.
    • (1996) Immunogenetics , vol.43 , pp. 360-369
    • Mo, R.1    Kato, Y.2    Nonaka, M.3    Nakayama, K.4    Takahashi, M.5
  • 85
    • 0013141948 scopus 로고
    • Human complement component C3: cDNA coding sequence and derived primary structure
    • De Bruijn MH, Fey GH. Human complement component C3: cDNA coding sequence and derived primary structure. Proc Natl Acad Sci USA 1985;82:708-712.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 708-712
    • De Bruijn, M.H.1    Fey, G.H.2
  • 87
    • 0022501942 scopus 로고
    • Nucleotide sequence of complementary DNA and derived amino acid sequence of rabbit complement C3 α-chain
    • Kusano M, et al. Nucleotide sequence of complementary DNA and derived amino acid sequence of rabbit complement C3 α-chain. Immunol Invest 1986;15:365-378.
    • (1986) Immunol Invest , vol.15 , pp. 365-378
    • Kusano, M.1
  • 88
    • 0025315178 scopus 로고
    • Nucleotide and deduced amino acid sequence of rat complement C3
    • Misumi Y, Sohda M, Ikehara Y. Nucleotide and deduced amino acid sequence of rat complement C3. Nucleic Acids Res 1990;18:2178.
    • (1990) Nucleic Acids Res , vol.18 , pp. 2178
    • Misumi, Y.1    Sohda, M.2    Ikehara, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.