메뉴 건너뛰기




Volumn 12, Issue 2, 2010, Pages 249-260

Evolutionary aspects of hemoglobin scavengers

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 MICROGLOBULIN; BINDING PROTEIN; HAPTOGLOBIN; HEME; HEME BINDING PROTEIN; HEMOGLOBIN; HEMOGLOBIN BINDIGN PROTEIN; HEMOPEXIN; SCAVENGER; SCAVENGER RECEPTOR; SERUM ALBUMIN; UNCLASSIFIED DRUG;

EID: 77949497125     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2009.2760     Document Type: Review
Times cited : (40)

References (93)
  • 2
    • 0020469360 scopus 로고
    • Hemoglobin binding site and its relationship to the serine protease-like active site of haptoglobin
    • Arcoleo JP and Greer J. Hemoglobin binding site and its relationship to the serine protease-like active site of hapto-globin. J Biol Chem 257: 10063-10068, 1982. (Pubitemid 13251004)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.17 , pp. 10063-10068
    • Arcoleo, J.P.1    Greer, J.2
  • 3
    • 0037328927 scopus 로고    scopus 로고
    • Haptoglobin directly affects T cells and suppresses T helper cell type 2 cytokine release
    • DOI 10.1046/j.1365-2567.2003.01569.x
    • Arredouani M, Matthijs P, Van Hoeyveld E, Kasran A, Baumann H, Ceuppens JL, and Stevens E. Haptoglobin directly affects T cells and suppresses T helper cell type 2 cy-tokine release. Immunology 108: 144-151, 2003. (Pubitemid 36232863)
    • (2003) Immunology , vol.108 , Issue.2 , pp. 144-151
    • Arredouani, M.1    Matthijs, P.2    Van Hoeyveld, E.3    Kasran, A.4    Baumann, H.5    Ceuppens, J.L.6    Stevens, E.7
  • 5
    • 0021032128 scopus 로고
    • Purification of haptoglobin and its effects on lymphocyte and alveolar macrophage responses
    • Baseler MW and Burrell R. Purification of haptoglobin and its effects on lymphocyte and alveolar macrophage responses. Inflammation 7: 387-400, 1983. (Pubitemid 14249859)
    • (1983) Inflammation , vol.7 , Issue.4 , pp. 387-400
    • Baseler, M.W.1    Burrell, R.2
  • 6
    • 0014678367 scopus 로고
    • The evolution of methaemalbumin
    • Baur EW. The evolution of methaemalbumin. Comp Biochem Physiol 30: 657-664, 1969.
    • (1969) Comp Biochem Physiol , vol.30 , pp. 657-664
    • Baur, E.W.1
  • 7
    • 0021966016 scopus 로고
    • Structure and expression of the human haptoglobin locus
    • Bensi G, Raugei G, Klefenz H, and Cortese R. Structure and expression of the human haptoglobin locus. EMBO J 4: 119-126, 1985.
    • (1985) EMBO J , vol.4 , pp. 119-126
    • Bensi, G.1    Raugei, G.2    Klefenz, H.3    Cortese, R.4
  • 11
    • 0015759501 scopus 로고
    • Studies on the properties of fish hemoglobins: Molecular properties and interaction with third components of the isolated hemoglobins from trout (Salmo irideus)
    • Brunori M, Giardina B, Chiancone E, Spagnuolo C, Binotti I, and Antonini E. Studies on the properties of fish hemoglobins: molecular properties and interaction with third components of the isolated hemoglobins from trout (Salmo irideus). Eur J Biochem 39: 563-570, 1973.
    • (1973) Eur J Biochem , vol.39 , pp. 563-570
    • Brunori, M.1    Giardina, B.2    Chiancone, E.3    Spagnuolo, C.4    Binotti, I.5    Antonini, E.6
  • 12
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn HF and Jandl JH. Exchange of heme among hemoglobins and between hemoglobin and albumin. J Biol Chem 243: 465-475, 1968.
    • (1968) J Biol Chem , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 13
    • 0018089740 scopus 로고
    • Structure and evolution of Ar-tiodactyla haptoglobins
    • Busby WH Jr and Travis JC. Structure and evolution of Ar-tiodactyla haptoglobins. Comp Biochem Physiol B 60: 389-396, 1978.
    • (1978) Comp Biochem Physiol B , vol.60 , pp. 389-396
    • Busby Jr., W.H.1    Travis, J.C.2
  • 15
    • 0347295937 scopus 로고    scopus 로고
    • A novel murine complement-related gene encoding a C1r-like serum protein
    • DOI 10.1016/S0161-5890(02)00283-3
    • Circolo A, Garnier G, and Volanakis JE. A novel murine complement-related gene encoding a C1r-like serum protein. Mol Immunol 39: 899-906, 2003. (Pubitemid 36398347)
    • (2003) Molecular Immunology , vol.39 , Issue.14 , pp. 899-906
    • Circolo, A.1    Garnier, G.2    Volanakis, J.E.3
  • 18
    • 0019854961 scopus 로고
    • A novel and specific method for the purification of hemoglobin-binding proteins
    • DOI 10.1016/0003-2697(81)90593-5
    • Delers F, Lombart C, Domingo M, and Musquera S. A novel and specific method for the purification of hemoglobin-binding proteins. Anal Biochem 118: 353-357, 1981. (Pubitemid 12145876)
    • (1981) Analytical Biochemistry , vol.118 , Issue.2 , pp. 353-357
    • Delers, F.1    Lombart, C.2    Domingo, M.3    Musquera, S.4
  • 21
    • 0017175735 scopus 로고
    • Subunit dissociation in fish hemoglobins
    • Edelstein SJ, McEwen B, and Gibson QH. Subunit dissociation in fish hemoglobins. J Biol Chem 251: 7632-7637, 1976.
    • (1976) J Biol Chem , vol.251 , pp. 7632-7637
    • Edelstein, S.J.1    McEwen, B.2    Gibson, Q.H.3
  • 22
    • 34547208855 scopus 로고    scopus 로고
    • Heme binding to albuminoid proteins is the result of recent evolution
    • DOI 10.1080/15216540701474523, PII 780754129
    • Fasano M, Fanali G, Leboffe L, and Ascenzi P. Heme binding to albuminoid proteins is the result of recent evolution. IUBMB Life 59: 436-440, 2007. (Pubitemid 47123995)
    • (2007) IUBMB Life , vol.59 , Issue.7 , pp. 436-440
    • Fasano, M.1    Fanali, G.2    Leboffe, L.3    Ascenzi, P.4
  • 23
    • 1642463804 scopus 로고    scopus 로고
    • The lectin-complement pathway - Its role in innate immunity and evolution
    • DOI 10.1111/j.0105-2896.2004.0123.x
    • Fujita T, Matsushita M, and Endo Y. The lectin-complement pathway: its role in innate immunity and evolution. Immunol Rev 198: 185-202, 2004. (Pubitemid 38406944)
    • (2004) Immunological Reviews , vol.198 , pp. 185-202
    • Fujita, T.1    Matsushita, M.2    Endo, Y.3
  • 24
    • 0036008987 scopus 로고    scopus 로고
    • The acute phase response of rainbow trout (Oncorhynchus mykiss) plasma proteins to viral, bacterial and fungal inflammatory agents
    • DOI 10.1006/fsim.2001.0367
    • Gerwick L, Steinhauer R, Lapatra S, Sandell T, Ortuno J, Hajiseyedjavadi N, and Bayne CJ. The acute phase response of rainbow trout (Oncorhynchus mykiss) plasma proteins to viral, bacterial and fungal inflammatory agents. Fish Shellfish Immunol 12: 229-242, 2002. (Pubitemid 34196966)
    • (2002) Fish and Shellfish Immunology , vol.12 , Issue.3 , pp. 229-242
    • Gerwick, L.1    Steinhauer, R.2    Lapatra, S.3    Sandell, T.4    Ortuno, J.5    Hajiseyedjavadi, N.6    Bayne, C.J.7
  • 25
    • 0024466207 scopus 로고
    • The phylogenetic odyssey of the erythrocyte. I. Hemoglobin: The universal respiratory pigment
    • Glomski CA and Tamburlin J. The phylogenetic odyssey of the erythrocyte. I. Hemoglobin: the universal respiratory pigment. Histol Histopathol 4: 509-514, 1989. (Pubitemid 19259798)
    • (1989) Histology and Histopathology , vol.4 , Issue.4 , pp. 509-514
    • Glomski, C.A.1    Tamburlin, J.2
  • 29
    • 0037955994 scopus 로고    scopus 로고
    • Molecular and morphological phylogenies of Ruminantia and the alternative position of the Moschidae
    • DOI 10.1080/10635150309343
    • Hassanin A and Douzery EJ. Molecular and morphological phylogenies of Ruminantia and the alternative position of the Moschidae. Syst Biol 52: 206-228, 2003. (Pubitemid 36594678)
    • (2003) Systematic Biology , vol.52 , Issue.2 , pp. 206-228
    • Hassanin, A.1    Douzery, E.J.P.2
  • 30
    • 0024147006 scopus 로고
    • Secretion of glyco-sylated human recombinant haptoglobin in baculovirus-infected insect cells
    • Heinderyckx M, Jacobs P, and Bollen A. Secretion of glyco-sylated human recombinant haptoglobin in baculovirus-infected insect cells. Mol Biol Rep 13: 225-232, 1988.
    • (1988) Mol Biol Rep , vol.13 , pp. 225-232
    • Heinderyckx, M.1    Jacobs, P.2    Bollen, A.3
  • 31
    • 2342478624 scopus 로고    scopus 로고
    • The occurrence of two types of hemopexin-like protein in medaka and differences in their affinity to heme
    • DOI 10.1242/jeb.00897
    • Hirayama M, Kobiyama A, Kinoshita S, and Watabe S. The occurrence of two types of hemopexin-like protein in Me-daka and differences in their affinity to heme. J Exp Biol 207: 1387-1398, 2004. (Pubitemid 38562865)
    • (2004) Journal of Experimental Biology , vol.207 , Issue.8 , pp. 1387-1398
    • Hirayama, M.1    Kobiyama, A.2    Kinoshita, S.3    Watabe, S.4
  • 32
    • 0022806770 scopus 로고
    • Molecular models for the putative dimer of sea lamprey hemoglobin
    • Honzatko RB and Hendrickson WA. Molecular models for the putative dimer of sea lamprey hemoglobin. Proc Natl Acad Sci USA 83: 8487-8491, 1986.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8487-8491
    • Honzatko, R.B.1    Hendrickson, W.A.2
  • 34
    • 27144551314 scopus 로고    scopus 로고
    • Identification of the receptor scavenging hemopexin-heme complexes
    • DOI 10.1182/blood-2005-03-1185
    • Hvidberg V, Maniecki MB, Jacobsen C, Hojrup P, Moller HJ, and Moestrup SK. Identification of the receptor scavenging hemopexin-heme complexes. Blood 106: 2572-2579, 2005. (Pubitemid 41510836)
    • (2005) Blood , vol.106 , Issue.7 , pp. 2572-2579
    • Hvidberg, V.1    Maniecki, M.B.2    Jacobsen, C.3    Hojrup, P.4    Moller, H.J.5    Moestrup, S.K.6
  • 35
    • 0035937794 scopus 로고    scopus 로고
    • Isolation, characterization, and cDNA cloning of chicken turpentine-induced protein, a new member of the scavenger receptor cysteine-rich (SRCR) family of proteins
    • Iwasaki K, Morimatsu M, Inanami O, Uchida E, Syuto B, Kuwabara M, and Niiyama M. Isolation, characterization, and cDNA cloning of chicken turpentine-induced protein, a new member of the scavenger receptor cysteine-rich (SRCR) family of proteins. J Biol Chem 276: 9400-9405, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 9400-9405
    • Iwasaki, K.1    Morimatsu, M.2    Inanami, O.3    Uchida, E.4    Syuto, B.5    Kuwabara, M.6    Niiyama, M.7
  • 36
    • 0013863955 scopus 로고
    • Serum haptoglobins in some North American catostomid fishes
    • Koehn RK. Serum haptoglobins in some North American catostomid fishes. Comp Biochem Physiol 17: 349-352, 1966.
    • (1966) Comp Biochem Physiol , vol.17 , pp. 349-352
    • Koehn, R.K.1
  • 38
    • 0016237467 scopus 로고
    • Evidence of homology between the beta-chain of human haptoglobin and the chymotrypsin family of serine proteases
    • Kurosky A, Barnett DR, Rasco MA, Lee TH, and Bowman BH. Evidence of homology between the beta-chain of human haptoglobin and the chymotrypsin family of serine proteases. Biochem Genet 11: 279-293, 1974.
    • (1974) Biochem Genet , vol.11 , pp. 279-293
    • Kurosky, A.1    Barnett, D.R.2    Rasco, M.A.3    Lee, T.H.4    Bowman, B.H.5
  • 39
    • 38949214694 scopus 로고    scopus 로고
    • A unique tetrameric structure of deer plasma haptoglobin - An evolutionary advantage in the Hp 2-2 phenotype with homogeneous structure
    • DOI 10.1111/j.1742-4658.2008.06267.x
    • Lai IH, Lin KY, Larsson M, Yang MC, Shiau CH, Liao MH, and Mao SJ. A unique tetrameric structure of deer plasma haptoglobin: an evolutionary advantage in the Hp 2-2 phe-notype with homogeneous structure. FEBS J 275: 981-993, 2008. (Pubitemid 351230215)
    • (2008) FEBS Journal , vol.275 , Issue.5 , pp. 981-993
    • Lai, I.H.1    Lin, K.-Y.2    Larsson, M.3    Yang, M.C.4    Shiau, C.-H.5    Liao, M.-H.6    Mao, S.J.T.7
  • 40
    • 36949035599 scopus 로고    scopus 로고
    • Evidence of tandem repeat and extra thiol-groups resulted in the polymeric formation of bovine haptoglobin: A unique structure of Hp 2-2 phenotype
    • Lai YA, Lai IH, Tseng CF, Lee J, and Mao SJ. Evidence of tandem repeat and extra thiol-groups resulted in the polymeric formation of bovine haptoglobin: a unique structure of Hp 2-2 phenotype. J Biochem Mol Biol 40: 1028-1038, 2007. (Pubitemid 350242291)
    • (2007) Journal of Biochemistry and Molecular Biology , vol.40 , Issue.6 , pp. 1028-1038
    • Yi, A.L.1    Lai, I.H.2    Chi, F.T.3    Lee, J.4    Mao, S.J.T.5
  • 42
    • 0000030730 scopus 로고
    • The formation of complexes between haemoglobins and plasma proteins in a variety of animals
    • Liang CC. The formation of complexes between haemoglobins and plasma proteins in a variety of animals. Biochem J 66: 552-558, 1957.
    • (1957) Biochem J , vol.66 , pp. 552-558
    • Liang, C.C.1
  • 44
    • 10944261319 scopus 로고    scopus 로고
    • Molecular characterization of the haptoglobin-hemoglobin receptor CD163: Ligand binding properties of the scavenger receptor cysteine-rich domain region
    • DOI 10.1074/jbc.M409629200
    • Madsen M, Moller HJ, Nielsen MJ, Jacobsen C, Graversen JH, van den Berg T, and Moestrup SK. Molecular characterization of the haptoglobin.hemoglobin receptor CD163: ligand binding properties of the scavenger receptor cysteine-rich domain region. J Biol Chem 279: 51561-51567, 2004. (Pubitemid 40017906)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 51561-51567
    • Madsen, M.1    Moller, H.J.2    Nielsen, M.J.3    Jacobsen, C.4    Graversen, J.H.5    Van Den Berg, T.6    Moestrup, S.K.7
  • 45
    • 0023004756 scopus 로고
    • The evolution of multigene families: Human haptoglobin genes
    • Maeda N and Smithies O. The evolution of multigene families: human haptoglobin genes. Annu Rev Genet 20: 81-108, 1986.
    • (1986) Annu Rev Genet , vol.20 , pp. 81-108
    • Maeda, N.1    Smithies, O.2
  • 46
    • 0021288584 scopus 로고
    • 2 gene
    • Maeda N, Yang F, Barnett DR, Bowman BH, and Smithies O. Duplication within the haptoglobin Hp2 gene. Nature 309: 131-135, 1984. (Pubitemid 14142780)
    • (1984) Nature , vol.309 , Issue.5964 , pp. 131-135
    • Maeda, N.1    Yang, F.2    Barnett, D.R.3
  • 47
    • 4644290697 scopus 로고    scopus 로고
    • Identification of the major proteins of the organic matrix of emu (Dromaius novaehollandiae) and rhea (Rhea americana) eggshell calcified layer
    • DOI 10.1080/00071660400001157
    • Mann K. Identification of the major proteins of the organic matrix of emu (Dromaius novaehollandiae) and rhea (Rhea americana) eggshell calcified layer. Br Poult Sci 45: 483-490, 2004. (Pubitemid 39290156)
    • (2004) British Poultry Science , vol.45 , Issue.4 , pp. 483-490
    • Mann, K.1
  • 48
    • 0025678674 scopus 로고
    • Hemoglobin binding with haptoglobin: Delineation of the haptoglobin binding site on the alpha-chain of human hemoglobin
    • McCormick DJ and Atassi MZ. Hemoglobin binding with haptoglobin: delineation of the haptoglobin binding site on the alpha-chain of human hemoglobin. J Protein Chem 9: 735-742, 1990.
    • (1990) J Protein Chem , vol.9 , pp. 735-742
    • McCormick, D.J.1    Atassi, M.Z.2
  • 49
    • 0023762976 scopus 로고
    • Complex events in the evolution of the haptoglobin gene cluster in primates
    • McEvoy SM and Maeda N. Complex events in the evolution of the haptoglobin gene cluster in primates. J Biol Chem 263: 15740-15747, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 15740-15747
    • McEvoy, S.M.1    Maeda, N.2
  • 50
    • 0005008505 scopus 로고
    • Haptoglobintypisierung von Serumproben ausgewählter Säugetiere mittels Stärkeelektrophorese
    • Meier F, Seidel B, Geserick G, Luther P, and Patzelt D. Haptoglobintypisierung von Serumproben ausgewählter Säugetiere mittels Stärkeelektrophorese. Mh Vet-Med 35: 617-620, 1980.
    • (1980) Mh Vet-Med , vol.35 , pp. 617-620
    • Meier, F.1    Seidel, B.2    Geserick, G.3    Luther, P.4    Patzelt, D.5
  • 51
    • 27644537494 scopus 로고    scopus 로고
    • Trypanosome lytic factor, a subclass of high-density lipoprotein, forms cation-selective pores in membranes
    • DOI 10.1016/j.molbiopara.2005.08.018, PII S0166685105002616
    • Molina-Portela Mdel P, Lugli EB, Recio-Pinto E, and Raper J. Trypanosome lytic factor, a subclass of high-density lipo-protein, forms cation-selective pores in membranes. Mol Biochem Parasitol 144: 218-226, 2005. (Pubitemid 41572228)
    • (2005) Molecular and Biochemical Parasitology , vol.144 , Issue.2 , pp. 218-226
    • Molina-Portela, M.D.P.1    Lugli, E.B.2    Recio-Pinto, E.3    Raper, J.4
  • 53
    • 0032512650 scopus 로고    scopus 로고
    • Characterization of the human serum trypanosome toxin, haptoglobin- related protein
    • DOI 10.1074/jbc.273.7.3884
    • Muranjan M, Nussenzweig V, and Tomlinson S. Characterization of the human serum trypanosome toxin, haptoglobin-related protein. J Biol Chem 273: 3884-3887, 1998. (Pubitemid 28103245)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.7 , pp. 3884-3887
    • Muranjan, M.1    Nussenzweig, V.2    Tomlinson, S.3
  • 54
    • 0012052568 scopus 로고
    • Elevation of serum haptoglobin in rabbits in response to experimental inflammation
    • Murray RK and Connell GE. Elevation of serum haptoglobin in rabbits in response to experimental inflammation. Nature 186: 86, 1960.
    • (1960) Nature , vol.186 , pp. 86
    • Murray, R.K.1    Connell, G.E.2
  • 55
    • 0018390811 scopus 로고
    • Identification of haptoglobin in chicken serum and specificity of the chicken haptoglobin-hemoglobin complex formation
    • Musquera S, Lombart C, Jayle MF, Rogard M, and Waks M. Identification of haptoglobin in chicken serum and specificity of the chicken haptoglobin- hemoglobin complex formation. Comp Biochem Physiol B 62: 241-244, 1979. (Pubitemid 9137713)
    • (1979) Comparative Biochemistry and Physiology , vol.62 , Issue.3 , pp. 241-244
    • Musquera, S.1    Lombart, C.2    Jayle, M.F.3
  • 56
    • 0017556547 scopus 로고
    • Haptoglobins in some Galliformes birds
    • Musquera S and Planas J. Haptoglobins in some Galliformes birds. Poult Sci 56: 1777-1782, 1977.
    • (1977) Poult Sci , vol.56 , pp. 1777-1782
    • Musquera, S.1    Planas, J.2
  • 57
    • 0015216974 scopus 로고
    • The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin
    • Nagel RL and Gibson QH. The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin. J Biol Chem 246: 69-73, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 69-73
    • Nagel, R.L.1    Gibson, Q.H.2
  • 58
    • 32344449586 scopus 로고    scopus 로고
    • Gene expression profiling in common cormorant liver with an oligo array: Assessing the potential toxic effects of environmental contaminants
    • DOI 10.1021/es051386m
    • Nakayama K, Iwata H, Kim EY, Tashiro K, and Tanabe S. Gene expression profilingincommon cormorant liver with an oligo array: assessing thepotential toxic effectsofenvironmen-tal contaminants. Environ Sci Technol 40: 1076-1083, 2006. (Pubitemid 43222201)
    • (2006) Environmental Science and Technology , vol.40 , Issue.3 , pp. 1076-1083
    • Nakayama, K.1    Iwata, H.2    Kim, E.-Y.3    Tashiro, K.4    Tanabe, S.5
  • 59
    • 33745859724 scopus 로고    scopus 로고
    • The macrophage scavenger receptor CD163: Endocytic properties of cytoplasmic tail variants
    • DOI 10.1189/jlb.1005602
    • Nielsen MJ, Madsen M, Moller HJ, and Moestrup SK. The macrophage scavenger receptor CD163: endocytic properties of cytoplasmic tail variants. J Leukoc Biol 79: 837-845, 2006. (Pubitemid 44835616)
    • (2006) Journal of Leukocyte Biology , vol.79 , Issue.4 , pp. 837-845
    • Nielsen, M.J.1    Madsen, M.2    Moller, H.J.3    Moestrup, S.K.4
  • 62
    • 0002068667 scopus 로고
    • Detection of haemoglobin, haemoglobin-haptoglobin complexes and other substances with peroxidase activity after zone electropho-resis
    • Owen JA, Silberman HJ, and Got C. Detection of haemoglobin, haemoglobin-haptoglobin complexes and other substances with peroxidase activity after zone electropho-resis. Nature 182: 1373, 1958.
    • (1958) Nature , vol.182 , pp. 1373
    • Owen, J.A.1    Silberman, H.J.2    Got, C.3
  • 63
    • 53449101873 scopus 로고    scopus 로고
    • Mutual self-defence: The try-panolytic factor story
    • Pays E and Vanhollebeke B. Mutual self-defence: the try-panolytic factor story. Microbes Infect 10: 985-989, 2008.
    • (2008) Microbes Infect , vol.10 , pp. 985-989
    • Pays, E.1    Vanhollebeke, B.2
  • 65
    • 34250362534 scopus 로고
    • Sur la préparation d'une nou-velle fraction des protéines plasmatiques l'haptoglobine
    • Polonovski M and Jayle MF. Sur la préparation d'une nou-velle fraction des protéines plasmatiques, l'haptoglobine. C R Seanc Soc Biol 211: 517-519, 1940.
    • (1940) C R Seanc Soc Biol , vol.211 , pp. 517-519
    • Polonovski, M.1    Jayle, M.F.2
  • 66
    • 54849423259 scopus 로고    scopus 로고
    • Human haptoglobin structure and function: A molecular modelling study
    • Polticelli F, Bocedi A, Minervini G, and Ascenzi P. Human haptoglobin structure and function: a molecular modelling study. FEBS J 275: 5648-5656, 2008.
    • (2008) FEBS J , vol.275 , pp. 5648-5656
    • Polticelli, F.1    Bocedi, A.2    Minervini, G.3    Ascenzi, P.4
  • 67
    • 14544275616 scopus 로고    scopus 로고
    • A genetic algorithm approach to detecting lineage-specific variation in selection pressure
    • DOI 10.1093/molbev/msi031
    • Pond SL and Frost SD. A genetic algorithm approach to detecting lineage-specific variation in selection pressure. Mol Biol Evol 22: 478-485, 2005. (Pubitemid 40299496)
    • (2005) Molecular Biology and Evolution , vol.22 , Issue.3 , pp. 478-485
    • Kosakovsky Pond, S.L.1    Frost, S.D.W.2
  • 68
    • 17744395033 scopus 로고    scopus 로고
    • Datamonkey: Rapid detection of selective pressure on individual sites of codon alignments
    • DOI 10.1093/bioinformatics/bti320
    • Pond SL and Frost SD. Datamonkey: rapid detection of selective pressure on individual sites of codon alignments. Bioinformatics 21: 2531-2533, 2005. (Pubitemid 40731616)
    • (2005) Bioinformatics , vol.21 , Issue.10 , pp. 2531-2533
    • Kosakovsky Pond, S.L.1    Frost, S.D.W.2
  • 69
    • 0028158348 scopus 로고
    • The SRCR superfamily: A family reminiscent of the Ig superfamily
    • DOI 10.1016/0968-0004(94)90165-1
    • Resnick D, Pearson A, and Krieger M. The SRCR super-family: a family reminiscent of the Ig superfamily. Trends Biochem Sci 19: 5-8, 1994. (Pubitemid 24028723)
    • (1994) Trends in Biochemical Sciences , vol.19 , Issue.1 , pp. 5-8
    • Resnick, D.1    Pearson, A.2    Krieger, M.3
  • 70
    • 0014993071 scopus 로고
    • Hp 2-2 like phenotypes in mammals
    • Ritter H and Schmitt J. Hp 2-2 like phenotypes in mammals. Humangenetik 12: 351-353, 1971.
    • (1971) Humangenetik , vol.12 , pp. 351-353
    • Ritter, H.1    Schmitt, J.2
  • 71
    • 4043065142 scopus 로고    scopus 로고
    • The Scavenger Receptor Cysteine-Rich (SRCR) domain: An ancient and highly conserved protein module of the innate immune system
    • Sarrias MR, Gronlund J, Padilla O, Madsen J, Holmskov U, and Lozano F. The Scavenger Receptor Cysteine-Rich (SRCR) domain: an ancient and highly conserved protein module of the innate immune system. Crit Rev Immunol 24: 1-37, 2004. (Pubitemid 39655010)
    • (2004) Critical Reviews in Immunology , vol.24 , Issue.1 , pp. 1-37
    • Sarrias, M.R.1    Gronlund, J.2    Padilla, O.3    Madsen, J.4    Holmskov, U.5    Lozano, F.6
  • 72
    • 34250305134 scopus 로고    scopus 로고
    • Gating the radical hemoglobin to macrophages: The anti-inflammatory role of CD163, a scavenger receptor
    • DOI 10.1089/ars.2007.1576
    • Schaer DJ, Alayash AI, and Buehler PW. Gating the radical hemoglobin to macrophages: the anti-inflammatory role of CD163, a scavenger receptor. Antioxid Redox Signal 9: 991-999, 2007. (Pubitemid 46919600)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.7 , pp. 991-999
    • Schaer, D.J.1    Alayash, A.I.2    Buehler, P.W.3
  • 73
    • 30144435054 scopus 로고    scopus 로고
    • CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin
    • DOI 10.1182/blood-2005-03-1014
    • Schaer DJ, Schaer CA, Buehler PW, Boykins RA, Schoedon G, Alayash AI, and Schaffner A. CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin. Blood 107: 373-380, 2006. (Pubitemid 43053566)
    • (2006) Blood , vol.107 , Issue.1 , pp. 373-380
    • Schaer, D.J.1    Schaer, C.A.2    Buehler, P.W.3    Boykins, R.A.4    Schoedon, G.5    Alayash, A.I.6    Schaffner, A.7
  • 75
    • 0033452452 scopus 로고    scopus 로고
    • Proprotein and prohormone convertases: A family of subtilases generating diverse bioactive polypeptides
    • DOI 10.1016/S0006-8993(99)01909-5, PII S0006899399019095
    • Seidah NG and Chretien M. Proprotein and prohormone convertases: a family of subtilases generating diverse bio-active polypeptides. Brain Res 848: 45-62, 1999. (Pubitemid 30001653)
    • (1999) Brain Research , vol.848 , Issue.1-2 , pp. 45-62
    • Seidah, N.G.1    Chretien, M.2
  • 77
    • 0001075339 scopus 로고
    • Chromosomal rearrangements and the evolution of haptoglobin genes
    • Smithies O, Connell GE, and Dixon GH. Chromosomal rearrangements and the evolution of haptoglobin genes. Nature 196: 232-236, 1962.
    • (1962) Nature , vol.196 , pp. 232-236
    • Smithies, O.1    Connell, G.E.2    Dixon, G.H.3
  • 78
    • 0031891213 scopus 로고    scopus 로고
    • Hemopexin from four species inhibits the association of heme with cultured hepatoma cells or primary rat hepatocytes exhibiting a small number of species specific hemopexin receptors
    • DOI 10.1002/hep.510270324
    • Taketani S, Immenschuh S, Go S, Sinclair PR, Stockert RJ, Liem HH, and Muller Eberhard U. Hemopexin from four species inhibits the association of heme with cultured hep-atoma cells or primary rat hepatocytes exhibiting a small number of species specific hemopexin receptors. Hepatology 27: 808-814, 1998. (Pubitemid 28103559)
    • (1998) Hepatology , vol.27 , Issue.3 , pp. 808-814
    • Taketani, S.1
  • 79
    • 0029283353 scopus 로고
    • Polyacrylamide gel elec-trophoretic patterns of chicken serum in acute inflammation induced by intramuscular injection of turpentine
    • Tohjo H, Miyoshi F, Uchida E, Niiyama M, Syuto B, Moritsu Y, Ichikawa S, and Takeuchi M. Polyacrylamide gel elec-trophoretic patterns of chicken serum in acute inflammation induced by intramuscular injection of turpentine. Poult Sci 74: 648-655, 1995.
    • (1995) Poult Sci , vol.74 , pp. 648-655
    • Tohjo, H.1    Miyoshi, F.2    Uchida, E.3    Niiyama, M.4    Syuto, B.5    Moritsu, Y.6    Ichikawa, S.7    Takeuchi, M.8
  • 80
    • 0036259938 scopus 로고    scopus 로고
    • Hemopexin: Structure, function, and regulation
    • DOI 10.1089/104454902753759717
    • Tolosano E and Altruda F. Hemopexin: structure, function, and regulation. DNA Cell Biol 21: 297-306, 2002. (Pubitemid 34594543)
    • (2002) DNA and Cell Biology , vol.21 , Issue.4 , pp. 297-306
    • Tolosano, E.1    Altruda, F.2
  • 81
    • 0024974981 scopus 로고
    • Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin
    • Tosi M, Duponchel C, Meo T, and Couture-Tosi E. Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin. J Mol Biol 208: 709-714, 1989.
    • (1989) J Mol Biol , vol.208 , pp. 709-714
    • Tosi, M.1    Duponchel, C.2    Meo, T.3    Couture-Tosi, E.4
  • 82
    • 0015320371 scopus 로고
    • Haptoglobin evolution: Polymeric forms of Hp in the Bovidae and Cervidae families
    • Travis JC and Sanders BG. Haptoglobin evolution: polymeric forms of Hp in the Bovidae and Cervidae families. J Exp Zool 180: 141-148, 1972.
    • (1972) J Exp Zool , vol.180 , pp. 141-148
    • Travis, J.C.1    Sanders, B.G.2
  • 83
    • 0026468833 scopus 로고
    • Identification of a haptoglobin-hemoglobin complex in the Alaskan Least Cisco (Coregonus sardinella)
    • Wahl SM, Boger JK, Michael V, and Duffy LK. Identification of a haptoglobin-hemoglobin complex in the Alaskan Least Cisco (Coregonus sardinella). Appl Theoret Electrophor 3: 17-20, 1992.
    • (1992) Appl Theoret Electrophor , vol.3 , pp. 17-20
    • Wahl, S.M.1    Boger, J.K.2    Michael, V.3    Duffy, L.K.4
  • 85
    • 33947260958 scopus 로고    scopus 로고
    • Haptoglobin 1-1 genotype and the risk of life-threatening streptococcus infection: Evolutionary implications
    • DOI 10.1016/j.jinf.2006.05.002, PII S0163445306001708
    • Wasserzug O, Blum S, Klement E, Lejbkowicz F, Miller-Lotan R, and Levy AP. Haptoglobin 1-1 genotype and the risk of life-threatening Streptococcus infection: evolutionary implications. J Infect 54: 410, 2007. (Pubitemid 46430268)
    • (2007) Journal of Infection , vol.54 , Issue.4 , pp. 410
    • Wasserzug, O.1    Blum, S.2    Klement, E.3    Lejbkowicz, F.4    Miller-Lotan, R.5    Levy, A.P.6
  • 86
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber RE and Vinogradov SN. Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol Rev 81: 569-628, 2001. (Pubitemid 32267074)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 87
    • 0021624634 scopus 로고
    • Structure and assembly of haptoglobin polymers by electron microscopy
    • DOI 10.1016/0022-2836(84)90342-5
    • Wejman JC, Hovsepian D, Wall JS, Hainfeld JF, and Greer J. Structure and assembly of haptoglobin polymers by electron microscopy. J Mol Biol 174: 343-368, 1984. (Pubitemid 15011744)
    • (1984) Journal of Molecular Biology , vol.174 , Issue.2 , pp. 343-368
    • Wejman, J.C.1    Hovsepian, D.2    Wall, J.S.3
  • 88
    • 0021604865 scopus 로고
    • Structure of haptoglobin and the haptoglobin-hemoglobin complex by electron microscopy
    • DOI 10.1016/0022-2836(84)90341-3
    • Wejman JC, Hovsepian D, Wall JS, Hainfeld JF, and Greer J. Structure of haptoglobin and the haptoglobin-hemoglobin complex by electron microscopy. J Mol Biol 174: 319-341, 1984. (Pubitemid 15011743)
    • (1984) Journal of Molecular Biology , vol.174 , Issue.2 , pp. 319-341
    • Wejman, J.C.1    Hovsepian, D.2    Wall, J.S.3
  • 89
    • 0032814076 scopus 로고    scopus 로고
    • Evolution of haemoglobin function: Molecular adaptations to environment
    • DOI 10.1046/j.1440-1681.1999.03091.x
    • Wells RM. Evolution of haemoglobin function: molecular adaptations to environment. Clin Exp Pharmacol Physiol 26: 591-595, 1999. (Pubitemid 29369916)
    • (1999) Clinical and Experimental Pharmacology and Physiology , vol.26 , Issue.8 , pp. 591-595
    • Wells, R.M.G.1
  • 90
    • 35748941219 scopus 로고    scopus 로고
    • Convergent evolution of human and bovine haptoglobin: Partial duplication of the genes
    • DOI 10.1007/s00239-007-9002-3
    • Wicher KB and Fries E. Convergent evolution of human and bovine haptoglobin: partial duplication of the genes. J Mol Evol 65: 373-379, 2007. (Pubitemid 350050649)
    • (2007) Journal of Molecular Evolution , vol.65 , Issue.4 , pp. 373-379
    • Wicher, K.B.1    Fries, E.2
  • 91
    • 33645228299 scopus 로고    scopus 로고
    • Haptoglobin, a hemoglobin-binding plasma protein, is present in bony fish and mammals but not in frog and chicken
    • Wicher KB and Fries E. Haptoglobin, a hemoglobin-binding plasma protein, is present in bony fish and mammals but not in frog and chicken. Proc Natl Acad Sci USA 103: 4168-4173, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4168-4173
    • Wicher, K.B.1    Fries, E.2
  • 93
    • 0022546705 scopus 로고
    • Haemoglobin binding with haptoglobin. Localization of the haptoglobin-binding sites on the β-chain of human haemoglobin by synthetic overlapping peptides encompassing the entire chain
    • Yoshioka N and Atassi MZ. Haemoglobin binding with haptoglobin: localization of the haptoglobin-binding sites on the b-chain of human haemoglobin by synthetic overlapping peptides encompassing the entire chain. Biochem J 234: 453-456, 1986. (Pubitemid 16049848)
    • (1986) Biochemical Journal , vol.234 , Issue.2 , pp. 453-456
    • Yoshioka, N.1    Atassi, M.Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.