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Volumn 275, Issue 22, 2008, Pages 5648-5656

Human haptoglobin structure and function - A molecular modelling study

Author keywords

Chaperone like activity; Covalent multimers; Haemoglobin; Haptoglobin; Homology modelling

Indexed keywords

CD163 ANTIGEN; HAPTOGLOBIN;

EID: 54849423259     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06690.x     Document Type: Article
Times cited : (70)

References (44)
  • 2
    • 0025344693 scopus 로고
    • Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide
    • Perutz MF (1990) Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide. Annu Rev Physiol 52, 1 25.
    • (1990) Annu Rev Physiol , vol.52 , pp. 1-25
    • Perutz, M.F.1
  • 3
    • 0032900608 scopus 로고    scopus 로고
    • Hemoglobin is an honorary enzyme
    • Brunori M (1999) Hemoglobin is an honorary enzyme. Trends Biochem Sci 24, 158 161.
    • (1999) Trends Biochem Sci , vol.24 , pp. 158-161
    • Brunori, M.1
  • 5
    • 0033619248 scopus 로고    scopus 로고
    • The hemoglobin enzyme
    • Imai K (1999) The hemoglobin enzyme. Nature 401, 437 439.
    • (1999) Nature , vol.401 , pp. 437-439
    • Imai, K.1
  • 10
    • 0014231294 scopus 로고
    • An improved method of preparing haptoglobin polypeptide chains using guanidine hydrochloride
    • Gordon S, Cleve H Bearn AG (1968) An improved method of preparing haptoglobin polypeptide chains using guanidine hydrochloride. Proc Soc Exp Biol Med 127, 52 59.
    • (1968) Proc Soc Exp Biol Med , vol.127 , pp. 52-59
    • Gordon, S.1    Cleve, H.2    Bearn, A.G.3
  • 11
  • 12
    • 0019511133 scopus 로고
    • Haptoglobin heavy and light chains. Structural properties, reassembly, and formation of minicomplex with hemoglobin
    • Valette I, Waks M, Wejman JC, Arcoleo JP Greer J (1981) Haptoglobin heavy and light chains. Structural properties, reassembly, and formation of minicomplex with hemoglobin. J Biol Chem 256, 672 679.
    • (1981) J Biol Chem , vol.256 , pp. 672-679
    • Valette, I.1    Waks, M.2    Wejman, J.C.3    Arcoleo, J.P.4    Greer, J.5
  • 13
    • 0021604865 scopus 로고
    • Structure of haptoglobin and the haptoglobin-hemoglobin complex by electron microscopy
    • Wejman JC, Hovsepian D, Wall JS, Hainfeld JF Greer J (1984) Structure of haptoglobin and the haptoglobin-hemoglobin complex by electron microscopy. J Mol Biol 174, 319 341.
    • (1984) J Mol Biol , vol.174 , pp. 319-341
    • Wejman, J.C.1    Hovsepian, D.2    Wall, J.S.3    Hainfeld, J.F.4    Greer, J.5
  • 15
    • 0035874003 scopus 로고    scopus 로고
    • Homeostasis: A scavenger receptor for haemoglobin
    • Gordon S (2001) Homeostasis: a scavenger receptor for haemoglobin. Curr Biol 11, R399 R401.
    • (2001) Curr Biol , vol.11
    • Gordon, S.1
  • 16
    • 0036174088 scopus 로고    scopus 로고
    • CD163: A signal receptor scavenging haptoglobin-hemoglobin complexes from plasma
    • Graversen JH, Madsen M Moestrup SK (2002) CD163: a signal receptor scavenging haptoglobin-hemoglobin complexes from plasma. Int J Biochem Cell Biol 34, 309 414.
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 309-414
    • Graversen, J.H.1    Madsen, M.2    Moestrup, S.K.3
  • 17
    • 0020320825 scopus 로고
    • Kinetic aspects of hemoglobin.haptoglobin-receptor interaction in rat liver plasma membranes, isolated liver cells, and liver cells in primary culture
    • Kino K, Tsunoo H, Higa Y, Takami M Nakajima H (1982) Kinetic aspects of hemoglobin.haptoglobin-receptor interaction in rat liver plasma membranes, isolated liver cells, and liver cells in primary culture. J Biol Chem 257, 4828 4833.
    • (1982) J Biol Chem , vol.257 , pp. 4828-4833
    • Kino, K.1    Tsunoo, H.2    Higa, Y.3    Takami, M.4    Nakajima, H.5
  • 18
    • 0023689975 scopus 로고
    • Intrahepatocellular site of the catabolism of heme and globin moiety of hemoglobin-haptoglobin after intravenous administration to rats
    • Oshiro S Nakajima H (1988) Intrahepatocellular site of the catabolism of heme and globin moiety of hemoglobin-haptoglobin after intravenous administration to rats. J Biol Chem 263, 16032 16038.
    • (1988) J Biol Chem , vol.263 , pp. 16032-16038
    • Oshiro, S.1    Nakajima, H.2
  • 19
    • 0026731506 scopus 로고
    • Expression of haptoglobin receptors in human hepatoma cells
    • Okuda M, Tokunaga R Taketani S (1992) Expression of haptoglobin receptors in human hepatoma cells. Biochim Biophys Acta 1136, 143 149.
    • (1992) Biochim Biophys Acta , vol.1136 , pp. 143-149
    • Okuda, M.1    Tokunaga, R.2    Taketani, S.3
  • 21
    • 0032145516 scopus 로고    scopus 로고
    • Internalization study using EDTA-prepared hepatocytes for receptor-mediated endocytosis of haemoglobin-haptoglobin
    • Zuwala-Jagiello J Osada J (1998) Internalization study using EDTA-prepared hepatocytes for receptor-mediated endocytosis of haemoglobin-haptoglobin. Int J Biochem Cell Biol 30, 923 931.
    • (1998) Int J Biochem Cell Biol , vol.30 , pp. 923-931
    • Zuwala-Jagiello, J.1    Osada, J.2
  • 22
    • 0029854812 scopus 로고    scopus 로고
    • Biological and clinical significance of haptoglobin polymorphism in humans
    • Langlois MR Delanghe JR (1996) Biological and clinical significance of haptoglobin polymorphism in humans. Clin Chem 42, 1589 1600.
    • (1996) Clin Chem , vol.42 , pp. 1589-1600
    • Langlois, M.R.1    Delanghe, J.R.2
  • 23
    • 0021966016 scopus 로고
    • Structure and expression of the haptoglobin locus
    • Bensi G, Raugei G, Klefenz H Cortese R (1985) Structure and expression of the haptoglobin locus. EMBO J 4, 119 126.
    • (1985) EMBO J , vol.4 , pp. 119-126
    • Bensi, G.1    Raugei, G.2    Klefenz, H.3    Cortese, R.4
  • 24
    • 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
    • Lai IH, Lin KY, Larsson M, Yang MC, Shiau CH, Liao MH Mao SJ (2008) A unique tetrameric structure of deer plasma haptoglobin - an evolutionary advantage in the Hp 2-2 phenotype with homogeneous structure. FEBS J 275, 981 993.
    • (2008) FEBS J , vol.275 , 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.7
  • 25
    • 35748941219 scopus 로고    scopus 로고
    • Convergent evolution of human and bovine haptoglobin: Partial duplication of the genes
    • Wicher KB Fries E (2007) Convergent evolution of human and bovine haptoglobin: partial duplication of the genes. J Mol Evol 65, 373 379.
    • (2007) J Mol Evol , vol.65 , pp. 373-379
    • Wicher, K.B.1    Fries, E.2
  • 26
    • 0036805825 scopus 로고    scopus 로고
    • Study of chaperone-like activity of human haptoglobin: Conformational changes under heat shock conditions and localization of interaction sites
    • Ettrich R, Brandt W Jr., Kopecky V, Baumruk V, Hofbauerova K Pavlicek Z (2002) Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites. Biol Chem 383, 1667 1676.
    • (2002) Biol Chem , vol.383 , pp. 1667-1676
    • Ettrich, R.1    Brandt Jr., W.2    Kopecky, V.3    Baumruk, V.4    Hofbauerova, K.5    Pavlicek, Z.6
  • 27
    • 0036469280 scopus 로고    scopus 로고
    • The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex
    • Budayova-Spano M, Lacroix M, Thielens NM, Arlaud GJ, Fontecilla-Camps JC Gaboriaud C (2002) The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex. EMBO J 21, 231 239.
    • (2002) EMBO J , vol.21 , pp. 231-239
    • Budayova-Spano, M.1    Lacroix, M.2    Thielens, N.M.3    Arlaud, G.J.4    Fontecilla-Camps, J.C.5    Gaboriaud, C.6
  • 28
    • 0017084611 scopus 로고
    • Characterization of the cyanogen bromide fragments of the β chain of human haptoglobin
    • Kurosky A, Hay RE, Kim H, Touchstone B, Rasco MA Bowman BH (1976) Characterization of the cyanogen bromide fragments of the β chain of human haptoglobin. Biochemistry 15, 5326 5336.
    • (1976) Biochemistry , vol.15 , pp. 5326-5336
    • Kurosky, A.1    Hay, R.E.2    Kim, H.3    Touchstone, B.4    Rasco, M.A.5    Bowman, B.H.6
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26, 283 291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 30
    • 0034678903 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human complement c1s: A serine protease with a handle
    • Gaboriaud C, Rossi V, Bally I, Arlaud GJ Fontecilla-Camps JC (2000) Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle. EMBO J 19, 1755 1765.
    • (2000) EMBO J , vol.19 , pp. 1755-1765
    • Gaboriaud, C.1    Rossi, V.2    Bally, I.3    Arlaud, G.J.4    Fontecilla-Camps, J.C.5
  • 31
    • 0020656713 scopus 로고
    • Hemoglobin-binding site on haptoglobin probed by selective proteolysis
    • Lustbader JW, Arcoleo JP, Birken S Greer J (1983) Hemoglobin-binding site on haptoglobin probed by selective proteolysis. J Biol Chem 258, 1227 1234.
    • (1983) J Biol Chem , vol.258 , pp. 1227-1234
    • Lustbader, J.W.1    Arcoleo, J.P.2    Birken, S.3    Greer, J.4
  • 32
    • 23844458614 scopus 로고    scopus 로고
    • The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin
    • Yerbury JJ, Rybchyn MS, Easterbrook-Smith SB, Henriques C Wilson MR (2005) The acute phase protein haptoglobin is a mammalian extracellular chaperone with an action similar to clusterin. Biochemistry 44, 10914 10925.
    • (2005) Biochemistry , vol.44 , pp. 10914-10925
    • Yerbury, J.J.1    Rybchyn, M.S.2    Easterbrook-Smith, S.B.3    Henriques, C.4    Wilson, M.R.5
  • 33
    • 0018781771 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. the binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen
    • Bode W (1979) The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen. J Mol Biol 127, 357 374.
    • (1979) J Mol Biol , vol.127 , pp. 357-374
    • Bode, W.1
  • 36
    • 33847749415 scopus 로고    scopus 로고
    • A unique loop extension in the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex
    • Nielsen MJ, Petersen SV, Jacobsen C, Thirup S, Enghild JJ, Graversen JH Moestrup SK (2007) A unique loop extension in the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex. J Biol Chem 282, 1072 1079.
    • (2007) J Biol Chem , vol.282 , pp. 1072-1079
    • Nielsen, M.J.1    Petersen, S.V.2    Jacobsen, C.3    Thirup, S.4    Enghild, J.J.5    Graversen, J.H.6    Moestrup, S.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.