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Volumn 26, Issue 5, 2013, Pages 789-794

Functional binding analysis of human fibrinogen as an iron- and heme-binding protein

Author keywords

Fibrinogen; Hemin; Iron; Protoporphyrin

Indexed keywords

FIBRINOGEN; HEMIN; IRON;

EID: 84885468679     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-013-9657-8     Document Type: Article
Times cited : (26)

References (24)
  • 1
    • 79957610056 scopus 로고    scopus 로고
    • Host fibrinogen stably bound to hemozoin rapidly activates monocytes via TLR-4 and CD11b/CD18-integrin: A new paradigm of hemozoin action
    • 21460246 10.1182/blood-2010-10-312413 1:CAS:528:DC%2BC3MXnt1Cmsrk%3D
    • Barrera V, Skorokhod OA, Baci D, Gremo G, Arese P, Schwarzer E (2011) Host fibrinogen stably bound to hemozoin rapidly activates monocytes via TLR-4 and CD11b/CD18-integrin: a new paradigm of hemozoin action. Blood 117:5674-5682
    • (2011) Blood , vol.117 , pp. 5674-5682
    • Barrera, V.1    Skorokhod, O.A.2    Baci, D.3    Gremo, G.4    Arese, P.5    Schwarzer, E.6
  • 2
    • 77952531839 scopus 로고    scopus 로고
    • Concentration-dependent effect fibrinogen on IgG-specific antigen binding and phagocytosis
    • 20303075 10.1016/j.cellimm.2010.02.014 1:CAS:528:DC%2BC3cXlsVOms74%3D
    • Boehm TK, Sojar H, DeNardin E (2010) Concentration-dependent effect fibrinogen on IgG-specific antigen binding and phagocytosis. Cell Immunol 263:41-48
    • (2010) Cell Immunol , vol.263 , pp. 41-48
    • Boehm, T.K.1    Sojar, H.2    Denardin, E.3
  • 3
    • 0019860211 scopus 로고
    • Zinc transport proteins in plasma
    • 6167283 10.1079/BJN19810014 1:CAS:528:DyaL3MXlvVamtL4%3D
    • Chesters JK, Will M (1981) Zinc transport proteins in plasma. Br J Nutr 46:111-118
    • (1981) Br J Nutr , vol.46 , pp. 111-118
    • Chesters, J.K.1    Will, M.2
  • 4
    • 0024396651 scopus 로고
    • The normal and morbid biology of fibrinogen
    • 2683767 10.1016/S0002-9343(89)80616-3 1:STN:280:DyaK3c%2FltlKguw%3D%3D
    • Dang CV, Bell WR, Shuman M (1989) The normal and morbid biology of fibrinogen. Am J Med 87:567-576
    • (1989) Am J Med , vol.87 , pp. 567-576
    • Dang, C.V.1    Bell, W.R.2    Shuman, M.3
  • 5
    • 0001490181 scopus 로고
    • Prevention of neonatal hyperbilirubinemia by tin protoporphyrin IX, a potent competitive inhibitor of heme oxidation
    • 6947237 10.1073/pnas.78.10.6466 1:CAS:528:DyaL38XhsFWhsg%3D%3D
    • Drummond GS, Kappas A (1981) Prevention of neonatal hyperbilirubinemia by tin protoporphyrin IX, a potent competitive inhibitor of heme oxidation. Proc Natl Acad Sci USA 78:6466-6470
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6466-6470
    • Drummond, G.S.1    Kappas, A.2
  • 6
    • 0024356383 scopus 로고
    • High molecular weight kininogen inhibits fibrinogen binding to cytoadhesins of neutrophils and platelets
    • 2526132 10.1083/jcb.109.1.377 1:CAS:528:DyaL1MXksFCrsrY%3D
    • Gustafson EJ, Lukasiewicz H, Wachtfogel YT, Norton KJ, Schmaier AH, Niewirowski S, Colman RW (1989) High molecular weight kininogen inhibits fibrinogen binding to cytoadhesins of neutrophils and platelets. J Cell Biol 109:377-387
    • (1989) J Cell Biol , vol.109 , pp. 377-387
    • Gustafson, E.J.1    Lukasiewicz, H.2    Wachtfogel, Y.T.3    Norton, K.J.4    Schmaier, A.H.5    Niewirowski, S.6    Colman, R.W.7
  • 7
    • 0021233532 scopus 로고
    • Quantification of the three normally occurring plasma fibrinogen in health and during so-cold acute phase by SDS electro-phoresis of fibrin obtained from EDTA-plasma
    • 6431629 10.1016/0049-3848(84)90359-1 1:CAS:528:DyaL2cXkvVygur8%3D
    • Holm B, Godal HC (1984) Quantification of the three normally occurring plasma fibrinogen in health and during so-cold acute phase by SDS electro-phoresis of fibrin obtained from EDTA-plasma. Thromb Res 35:279-290
    • (1984) Thromb Res , vol.35 , pp. 279-290
    • Holm, B.1    Godal, H.C.2
  • 8
    • 23944484733 scopus 로고    scopus 로고
    • An improved method for quantification of heme using tetramethylbenzidine as substrate
    • 16091279 10.1016/j.ab.2005.06.022 1:CAS:528:DC%2BD2MXpslynu7k%3D
    • Huy NT, Trang DTX, Uyen DT, Sasai M, Harada S, Kamei K (2005) An improved method for quantification of heme using tetramethylbenzidine as substrate. Anal Biochem 344:289-291
    • (2005) Anal Biochem , vol.344 , pp. 289-291
    • Huy, N.T.1    Trang, D.T.X.2    Uyen, D.T.3    Sasai, M.4    Harada, S.5    Kamei, K.6
  • 9
    • 0033956343 scopus 로고    scopus 로고
    • Speciation of protein-binding zinc and copper in human blood serum by chelating resin pre-treatment and inductively coupled plasma mass spectrometry
    • 10885075 10.1039/a907088e 1:CAS:528:DC%2BD3cXhtlGhsg%3D%3D
    • Inagaki K, Mikuriya N, Morita S, Haraguchi H, Nakahara Y, Hattori M, Kinoshita T, Saito H (2000) Speciation of protein-binding zinc and copper in human blood serum by chelating resin pre-treatment and inductively coupled plasma mass spectrometry. Analyst 125:197-203
    • (2000) Analyst , vol.125 , pp. 197-203
    • Inagaki, K.1    Mikuriya, N.2    Morita, S.3    Haraguchi, H.4    Nakahara, Y.5    Hattori, M.6    Kinoshita, T.7    Saito, H.8
  • 10
    • 0032710987 scopus 로고    scopus 로고
    • Zinc protoporphyrin: A metabolite with a mission
    • 10585337
    • Labbè RF, Vreman HJ, Stevenson DK (1999) Zinc protoporphyrin: a metabolite with a mission. Clin Chem 45:2060-2072
    • (1999) Clin Chem , vol.45 , pp. 2060-2072
    • Labbè, R.F.1    Vreman, H.J.2    Stevenson, D.K.3
  • 11
    • 4444373278 scopus 로고    scopus 로고
    • Regulated de novo biosynthesis of fibrinogen in extrahepatic epithelial cells in response to inflammation
    • 15269818 1:CAS:528:DC%2BD2cXmvVert7w%3D
    • Lawrence SO, Simpson-Haidaris PJ (2004) Regulated de novo biosynthesis of fibrinogen in extrahepatic epithelial cells in response to inflammation. Thromb Haemost 92:234-243
    • (2004) Thromb Haemost , vol.92 , pp. 234-243
    • Lawrence, S.O.1    Simpson-Haidaris, P.J.2
  • 12
    • 0023679995 scopus 로고
    • Zinc binding to fibrinogen and fibrin
    • 10.1016/0003-9861(88)90260-3
    • Mark G (1988) Zinc binding to fibrinogen and fibrin. Arch Biochem Biophys 266:285-288
    • (1988) Arch Biochem Biophys , vol.266 , pp. 285-288
    • Mark, G.1
  • 13
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and functions
    • 16102057 10.1111/j.1538-7836.2005.01365.x 1:CAS:528:DC%2BD2MXpsFKjsL8%3D
    • Mosesson MW (2005) Fibrinogen and fibrin structure and functions. J Thromb Haemost 3:1894-1904
    • (2005) J Thromb Haemost , vol.3 , pp. 1894-1904
    • Mosesson, M.W.1
  • 14
    • 68149089854 scopus 로고    scopus 로고
    • Carbon monoxide releasing molecule-2 increases the velocity of thrombus growth and strength in human plasma
    • 19417630 10.1097/MBC.0b013e32832ca3a3 1:CAS:528:DC%2BD1MXnsFOqsbc%3D
    • Nielsen VG, Kirklin JK, George JF (2009) Carbon monoxide releasing molecule-2 increases the velocity of thrombus growth and strength in human plasma. Blood Coagul Fibrinolysis 20:377-380
    • (2009) Blood Coagul Fibrinolysis , vol.20 , pp. 377-380
    • Nielsen, V.G.1    Kirklin, J.K.2    George, J.F.3
  • 15
    • 79960697365 scopus 로고    scopus 로고
    • Fibrinogen is a heme-associated, carbon monoxide sensing molecule: A preliminary report
    • 21451399 10.1097/MBC.0b013e328345c069 1:CAS:528:DC%2BC3MXos1ejsbk%3D
    • Nielsen VG, Cohen JB, Malayaman SN, Nowak M, Vosseller K (2011) Fibrinogen is a heme-associated, carbon monoxide sensing molecule: a preliminary report. Blood Coagul Fibrinolysis 22:443-447
    • (2011) Blood Coagul Fibrinolysis , vol.22 , pp. 443-447
    • Nielsen, V.G.1    Cohen, J.B.2    Malayaman, S.N.3    Nowak, M.4    Vosseller, K.5
  • 16
    • 36249027053 scopus 로고    scopus 로고
    • Different vulnerability of fibrinogen subunits to oxidative stress/nitrative modifications induced by peroxynitrite: Functional consequences
    • 17467041 10.1016/j.thromres.2007.03.017 1:CAS:528:DC%2BD2sXhtlGns7vK
    • Nowak P, Zbikowska HM, Ponczek M, Kolodziejczyk J, Wachowicz B (2007) Different vulnerability of fibrinogen subunits to oxidative stress/nitrative modifications induced by peroxynitrite: functional consequences. Thromb Res 121:163-174
    • (2007) Thromb Res , vol.121 , pp. 163-174
    • Nowak, P.1    Zbikowska, H.M.2    Ponczek, M.3    Kolodziejczyk, J.4    Wachowicz, B.5
  • 17
    • 0035090120 scopus 로고    scopus 로고
    • Fibrinogen is an efficient antioxidant
    • 11257465 10.1016/S0955-2863(00)00147-9 1:CAS:528:DC%2BD3MXitVOmsbY%3D
    • Olinescu RM, Kummerow FA (2001) Fibrinogen is an efficient antioxidant. J Nutr Biochem 12:162-169
    • (2001) J Nutr Biochem , vol.12 , pp. 162-169
    • Olinescu, R.M.1    Kummerow, F.A.2
  • 18
    • 70350126591 scopus 로고    scopus 로고
    • Zinc: Role in immunity, oxidative stress and chronic inflammation
    • 19710611 10.1097/MCO.0b013e3283312956 1:CAS:528:DC%2BD1MXht1Kju7jL
    • Prasad AS (2009) Zinc: role in immunity, oxidative stress and chronic inflammation. Curr Opin Clin Nutr Metab Care 12:646-652
    • (2009) Curr Opin Clin Nutr Metab Care , vol.12 , pp. 646-652
    • Prasad, A.S.1
  • 19
    • 79551624917 scopus 로고    scopus 로고
    • Fibrinopeptides A and B release in the process of surface fibrin formation
    • 21106983 10.1182/blood-2010-08-300301 1:CAS:528:DC%2BC3MXit1Kktrw%3D
    • Riedel T, Suttnar J, Brynda E, Houska M, Medved L, Dyr JE (2011) Fibrinopeptides A and B release in the process of surface fibrin formation. Blood 117:1700-1706
    • (2011) Blood , vol.117 , pp. 1700-1706
    • Riedel, T.1    Suttnar, J.2    Brynda, E.3    Houska, M.4    Medved, L.5    Dyr, J.E.6
  • 20
    • 67849121525 scopus 로고    scopus 로고
    • Fibrinogen signal transduction in the nervous system
    • 19630789 10.1111/j.1538-7836.2009.03438.x 1:CAS:528:DC%2BD1MXpvV2isr0%3D
    • Ryu JK, Davalos D, Akassoglou K (2009) Fibrinogen signal transduction in the nervous system. J Thromb Haemost 7:151-154
    • (2009) J Thromb Haemost , vol.7 , pp. 151-154
    • Ryu, J.K.1    Davalos, D.2    Akassoglou, K.3
  • 21
    • 33646809045 scopus 로고    scopus 로고
    • Biological implications of heme metabolism
    • 10.3164/jcbn.38.138 1:CAS:528:DC%2BD28XlsFamurg%3D
    • Sassa S (2006) Biological implications of heme metabolism. J Clin Biochem Nutr 38:138-155
    • (2006) J Clin Biochem Nutr , vol.38 , pp. 138-155
    • Sassa, S.1
  • 23
    • 57649107157 scopus 로고    scopus 로고
    • Bacterial heme-transport proteins and their heme-coordination modes
    • 18977196 10.1016/j.abb.2008.10.013 1:CAS:528:DC%2BD1cXhsFagtb7F
    • Tong Y, Guo M (2009) Bacterial heme-transport proteins and their heme-coordination modes. Arch Biochem Biophys 481:1-15
    • (2009) Arch Biochem Biophys , vol.481 , pp. 1-15
    • Tong, Y.1    Guo, M.2
  • 24
    • 83555165130 scopus 로고    scopus 로고
    • Heme-mediated binding of α-casein to ferritin: Evidence for preferential α-casein to ferrous iron
    • 21732136 10.1007/s10534-011-9470-1 1:CAS:528:DC%2BC3MXhsVKhsrbI
    • Usami A, Tanaka M, Yoshikawa Y, Watanabe K, Ohtsuka H, Orino K (2011) Heme-mediated binding of α-casein to ferritin: evidence for preferential α-casein to ferrous iron. Biometals 24:1217-1224
    • (2011) Biometals , vol.24 , pp. 1217-1224
    • Usami, A.1    Tanaka, M.2    Yoshikawa, Y.3    Watanabe, K.4    Ohtsuka, H.5    Orino, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.