메뉴 건너뛰기




Volumn 8, Issue 7, 2013, Pages

An Insight into the Changes in Human Plasma Proteome on Adaptation to Hypobaric Hypoxia

Author keywords

[No Author keywords available]

Indexed keywords

ALBUMIN; ALPHA 1 ANTITRYPSIN; AMYLOID; APOLIPOPROTEIN A1; COMPLEMENT COMPONENT 4A; COMPLEMENT COMPONENT C3; COMPLEMENT COMPONENT C4; HAPTOGLOBIN; HEMOGLOBIN BETA CHAIN; HEMOPEXIN; IMMUNOGLOBULIN G; PLASMA PROTEIN; PREALBUMIN; RETINOL BINDING PROTEIN; TRANSFERRIN; UNCLASSIFIED DRUG; VITAMIN D BINDING PROTEIN;

EID: 84879757255     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0067548     Document Type: Article
Times cited : (50)

References (97)
  • 1
    • 0016427491 scopus 로고
    • Functional adaptation to high altitude hypoxia
    • Frisancho AR, (1975) Functional adaptation to high altitude hypoxia. Science 187: 313-319.
    • (1975) Science , vol.187 , pp. 313-319
    • Frisancho, A.R.1
  • 2
    • 0026095651 scopus 로고
    • Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering
    • Jessen TH, Weber RE, Fermi G, Tame J, Braunitzer G, (1991) Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering. Proc Natl Acad Sci U S A 88: 6519-6522.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 6519-6522
    • Jessen, T.H.1    Weber, R.E.2    Fermi, G.3    Tame, J.4    Braunitzer, G.5
  • 3
    • 70149102931 scopus 로고    scopus 로고
    • Evolutionary and functional insights into the mechanism underlying high-altitude adaptation of deer mouse hemoglobin
    • Storz JF, Runck AM, Sabatino SJ, Kelly JK, Ferrand N, et al. (2009) Evolutionary and functional insights into the mechanism underlying high-altitude adaptation of deer mouse hemoglobin. Proc Natl Acad Sci U S A 106: 14450-14455.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14450-14455
    • Storz, J.F.1    Runck, A.M.2    Sabatino, S.J.3    Kelly, J.K.4    Ferrand, N.5
  • 4
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
    • Jiang BH, Rue E, Wang GL, Roe R, Semenza GL, (1996) Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. J Biol Chem 271: 17771-17778.
    • (1996) J Biol Chem , vol.271 , pp. 17771-17778
    • Jiang, B.H.1    Rue, E.2    Wang, G.L.3    Roe, R.4    Semenza, G.L.5
  • 5
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang GL, Jiang BH, Rue EA, Semenza GL, (1995) Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci U S A 92: 5510-5514.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 6
    • 0030792094 scopus 로고    scopus 로고
    • Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1
    • Rolfs A, Kvietikova I, Gassmann M, Wenger RH, (1997) Oxygen-regulated transferrin expression is mediated by hypoxia-inducible factor-1. J Biol Chem 272: 20055-20062.
    • (1997) J Biol Chem , vol.272 , pp. 20055-20062
    • Rolfs, A.1    Kvietikova, I.2    Gassmann, M.3    Wenger, R.H.4
  • 7
    • 0032581277 scopus 로고    scopus 로고
    • Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
    • Carmeliet P, Dor Y, Herbert JM, Fukumura D, Brusselmans K, et al. (1998) Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis. Nature 394: 485-490.
    • (1998) Nature , vol.394 , pp. 485-490
    • Carmeliet, P.1    Dor, Y.2    Herbert, J.M.3    Fukumura, D.4    Brusselmans, K.5
  • 8
    • 0029761644 scopus 로고    scopus 로고
    • Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
    • Forsythe JA, Jiang BH, Iyer NV, Agani F, Leung SW, et al. (1996) Activation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1. Mol Cell Biol 16: 4604-4613.
    • (1996) Mol Cell Biol , vol.16 , pp. 4604-4613
    • Forsythe, J.A.1    Jiang, B.H.2    Iyer, N.V.3    Agani, F.4    Leung, S.W.5
  • 9
    • 0028786601 scopus 로고
    • A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter
    • Melillo G, Musso T, Sica A, Taylor LS, Cox GW, et al. (1995) A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter. J Exp Med 182: 1683-1693.
    • (1995) J Exp Med , vol.182 , pp. 1683-1693
    • Melillo, G.1    Musso, T.2    Sica, A.3    Taylor, L.S.4    Cox, G.W.5
  • 10
    • 15444342958 scopus 로고    scopus 로고
    • Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha
    • Iyer NV, Kotch LE, Agani F, Leung SW, Laughner E, et al. (1998) Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha. Genes Dev 12: 149-162.
    • (1998) Genes Dev , vol.12 , pp. 149-162
    • Iyer, N.V.1    Kotch, L.E.2    Agani, F.3    Leung, S.W.4    Laughner, E.5
  • 11
    • 0027210562 scopus 로고
    • General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia
    • Wang GL, Semenza GL, (1993) General involvement of hypoxia-inducible factor 1 in transcriptional response to hypoxia. Proc Natl Acad Sci U S A 90: 4304-4308.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 4304-4308
    • Wang, G.L.1    Semenza, G.L.2
  • 13
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi SP, Rochon Y, Franza BR, Aebersold R, (1999) Correlation between protein and mRNA abundance in yeast. Mol Cell Biol 19: 1720-1730.
    • (1999) Mol Cell Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 14
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: functions, mysteries, uses
    • Varshavsky A, (1996) The N-end rule: functions, mysteries, uses. Proc Natl Acad Sci U S A 93: 12142-12149.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 15
    • 4344576101 scopus 로고    scopus 로고
    • An Investigation of Plasma Collection, Stabilization, and Storage Procedures for Proteomic Analysis of Clinical Samples
    • Hulmes JD, Bethea D, Ho K, Huang S-P, Ricci DL, et al. (2004) An Investigation of Plasma Collection, Stabilization, and Storage Procedures for Proteomic Analysis of Clinical Samples. Clinical Proteomics 1: 017-032.
    • (2004) Clinical Proteomics , vol.1 , pp. 017-032
    • Hulmes, J.D.1    Bethea, D.2    Ho, K.3    Huang, S.-P.4    Ricci, D.L.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 73649148426 scopus 로고    scopus 로고
    • An Effective Method for the Analysis of Human Plasma Proteome using Two-dimensional Gel Electrophoresis
    • Ahmad Y, Sharma N, (2009) An Effective Method for the Analysis of Human Plasma Proteome using Two-dimensional Gel Electrophoresis. Journal of Proteomics & Bioinformatics 02: 495-499.
    • (2009) Journal of Proteomics & Bioinformatics , vol.2 , pp. 495-499
    • Ahmad, Y.1    Sharma, N.2
  • 18
    • 0346887179 scopus 로고    scopus 로고
    • Analysis of proteins expressed in rat plasma exposed to dioxin using 2-dimensional gel electrophoresis
    • Son WK, Lee DY, Lee SH, Joo WA, Kim CW, (2003) Analysis of proteins expressed in rat plasma exposed to dioxin using 2-dimensional gel electrophoresis. Proteomics 3: 2393-2401.
    • (2003) Proteomics , vol.3 , pp. 2393-2401
    • Son, W.K.1    Lee, D.Y.2    Lee, S.H.3    Joo, W.A.4    Kim, C.W.5
  • 19
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • Yan JX, Wait R, Berkelman T, Harry RA, Westbrook JA, et al. (2000) A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry. Electrophoresis 21: 3666-3672.
    • (2000) Electrophoresis , vol.21 , pp. 3666-3672
    • Yan, J.X.1    Wait, R.2    Berkelman, T.3    Harry, R.A.4    Westbrook, J.A.5
  • 20
    • 0042316795 scopus 로고    scopus 로고
    • Quantitative protein profiling in heart mitochondria from diabetic rats
    • Turko IV, Murad F, (2003) Quantitative protein profiling in heart mitochondria from diabetic rats. J Biol Chem 278: 35844-35849.
    • (2003) J Biol Chem , vol.278 , pp. 35844-35849
    • Turko, I.V.1    Murad, F.2
  • 21
    • 80053972002 scopus 로고    scopus 로고
    • Identification of haptoglobin and apolipoprotein A-I as biomarkers for high altitude pulmonary edema
    • Ahmad Y, Shukla D, Garg I, Sharma NK, Saxena S, et al. (2011) Identification of haptoglobin and apolipoprotein A-I as biomarkers for high altitude pulmonary edema. Funct Integr Genomics 11: 407-417.
    • (2011) Funct Integr Genomics , vol.11 , pp. 407-417
    • Ahmad, Y.1    Shukla, D.2    Garg, I.3    Sharma, N.K.4    Saxena, S.5
  • 22
    • 67849130563 scopus 로고    scopus 로고
    • ToppGene Suite for gene list enrichment analysis and candidate gene prioritization
    • Chen J, Bardes EE, Aronow BJ, Jegga AG, (2009) ToppGene Suite for gene list enrichment analysis and candidate gene prioritization. Nucleic Acids Res 37: W305-311.
    • (2009) Nucleic Acids Res , vol.37
    • Chen, J.1    Bardes, E.E.2    Aronow, B.J.3    Jegga, A.G.4
  • 23
    • 0029763762 scopus 로고    scopus 로고
    • Molecular oxygen modulates cytochrome c oxidase function
    • Chandel NS, Budinger GR, Schumacker PT, (1996) Molecular oxygen modulates cytochrome c oxidase function. J Biol Chem 271: 18672-18677.
    • (1996) J Biol Chem , vol.271 , pp. 18672-18677
    • Chandel, N.S.1    Budinger, G.R.2    Schumacker, P.T.3
  • 24
    • 0027379174 scopus 로고
    • Oxygen conformance of cellular respiration in hepatocytes
    • Schumacker PT, Chandel N, Agusti AG, (1993) Oxygen conformance of cellular respiration in hepatocytes. Am J Physiol 265: L395-402.
    • (1993) Am J Physiol , vol.265
    • Schumacker, P.T.1    Chandel, N.2    Agusti, A.G.3
  • 25
    • 34547838835 scopus 로고    scopus 로고
    • Ischemic pre-conditioning in deceased donor liver transplantation: a prospective randomized clinical trial
    • Amador A, Grande L, Marti J, Deulofeu R, Miquel R, et al. (2007) Ischemic pre-conditioning in deceased donor liver transplantation: a prospective randomized clinical trial. Am J Transplant 7: 2180-2189.
    • (2007) Am J Transplant , vol.7 , pp. 2180-2189
    • Amador, A.1    Grande, L.2    Marti, J.3    Deulofeu, R.4    Miquel, R.5
  • 27
    • 0033960898 scopus 로고    scopus 로고
    • Oxygen: modulator of metabolic zonation and disease of the liver
    • Jungermann K, Kietzmann T, (2000) Oxygen: modulator of metabolic zonation and disease of the liver. Hepatology 31: 255-260.
    • (2000) Hepatology , vol.31 , pp. 255-260
    • Jungermann, K.1    Kietzmann, T.2
  • 29
    • 33847725552 scopus 로고    scopus 로고
    • Hypoxic conformance of metabolism in primary rat hepatocytes: a model of hepatic hibernation
    • Subramanian RM, Chandel N, Budinger GR, Schumacker PT, (2007) Hypoxic conformance of metabolism in primary rat hepatocytes: a model of hepatic hibernation. Hepatology 45: 455-464.
    • (2007) Hepatology , vol.45 , pp. 455-464
    • Subramanian, R.M.1    Chandel, N.2    Budinger, G.R.3    Schumacker, P.T.4
  • 30
    • 0029917973 scopus 로고    scopus 로고
    • Metabolic adaptations supporting anoxia tolerance in reptiles: recent advances
    • Storey KB, (1996) Metabolic adaptations supporting anoxia tolerance in reptiles: recent advances. Comp Biochem Physiol B Biochem Mol Biol 113: 23-35.
    • (1996) Comp Biochem Physiol B Biochem Mol Biol , vol.113 , pp. 23-35
    • Storey, K.B.1
  • 31
    • 0025918420 scopus 로고
    • Vitamin D3 binding protein required for in vitro activation of macrophages after alkylglycerol treatment of mouse peritoneal cells
    • Yamamoto N, Homma S, Haddad JG, Kowalski MA, (1991) Vitamin D3 binding protein required for in vitro activation of macrophages after alkylglycerol treatment of mouse peritoneal cells. Immunology 74: 420-424.
    • (1991) Immunology , vol.74 , pp. 420-424
    • Yamamoto, N.1    Homma, S.2    Haddad, J.G.3    Kowalski, M.A.4
  • 32
    • 3042784114 scopus 로고    scopus 로고
    • Therapeutic potential of vitamin D-binding protein
    • Gomme PT, Bertolini J, (2004) Therapeutic potential of vitamin D-binding protein. Trends Biotechnol 22: 340-345.
    • (2004) Trends Biotechnol , vol.22 , pp. 340-345
    • Gomme, P.T.1    Bertolini, J.2
  • 33
    • 0023751926 scopus 로고
    • Depression of gelsolin levels and detection of gelsolin-actin complexes in plasma of patients with acute lung injury
    • Lind SE, Smith DB, Janmey PA, Stossel TP, (1988) Depression of gelsolin levels and detection of gelsolin-actin complexes in plasma of patients with acute lung injury. Am Rev Respir Dis 138: 429-434.
    • (1988) Am Rev Respir Dis , vol.138 , pp. 429-434
    • Lind, S.E.1    Smith, D.B.2    Janmey, P.A.3    Stossel, T.P.4
  • 34
    • 33747854680 scopus 로고    scopus 로고
    • Biological and clinical aspects of the vitamin D binding protein (Gc-globulin) and its polymorphism
    • Speeckaert M, Huang G, Delanghe JR, Taes YE, (2006) Biological and clinical aspects of the vitamin D binding protein (Gc-globulin) and its polymorphism. Clin Chim Acta 372: 33-42.
    • (2006) Clin Chim Acta , vol.372 , pp. 33-42
    • Speeckaert, M.1    Huang, G.2    Delanghe, J.R.3    Taes, Y.E.4
  • 38
    • 0031008641 scopus 로고    scopus 로고
    • Immunotherapy of BALB/c mice bearing Ehrlich ascites tumor with vitamin D-binding protein-derived macrophage activating factor
    • Yamamoto N, Naraparaju VR, (1997) Immunotherapy of BALB/c mice bearing Ehrlich ascites tumor with vitamin D-binding protein-derived macrophage activating factor. Cancer Res 57: 2187-2192.
    • (1997) Cancer Res , vol.57 , pp. 2187-2192
    • Yamamoto, N.1    Naraparaju, V.R.2
  • 39
    • 65549152427 scopus 로고    scopus 로고
    • Heme-hemopexin complex attenuates neuronal cell death and stroke damage
    • Li RC, Saleem S, Zhen G, Cao W, Zhuang H, et al. (2009) Heme-hemopexin complex attenuates neuronal cell death and stroke damage. J Cereb Blood Flow Metab 29: 953-964.
    • (2009) J Cereb Blood Flow Metab , vol.29 , pp. 953-964
    • Li, R.C.1    Saleem, S.2    Zhen, G.3    Cao, W.4    Zhuang, H.5
  • 40
    • 37249083416 scopus 로고    scopus 로고
    • Comparison of the effects of serpin A1, a recombinant serpin A1-IGF chimera and serpin A1 C-terminal peptide on wound healing
    • Congote LF, Temmel N, Sadvakassova G, Dobocan MC, (2008) Comparison of the effects of serpin A1, a recombinant serpin A1-IGF chimera and serpin A1 C-terminal peptide on wound healing. Peptides 29: 39-46.
    • (2008) Peptides , vol.29 , pp. 39-46
    • Congote, L.F.1    Temmel, N.2    Sadvakassova, G.3    Dobocan, M.C.4
  • 41
  • 43
    • 0016684254 scopus 로고
    • alpha1-Antitrypsin deficiency and skin abnormalities
    • Ledoux-Corbusier M, Achten G, (1975) alpha1-Antitrypsin deficiency and skin abnormalities. J Cutan Pathol 2: 25-29.
    • (1975) J Cutan Pathol , vol.2 , pp. 25-29
    • Ledoux-Corbusier, M.1    Achten, G.2
  • 44
    • 85047684827 scopus 로고    scopus 로고
    • Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy
    • Lomas DA, Mahadeva R, (2002) Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. J Clin Invest 110: 1585-1590.
    • (2002) J Clin Invest , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 45
    • 0034126770 scopus 로고    scopus 로고
    • Complete reversal of fatal pulmonary hypertension in rats by a serine elastase inhibitor
    • Cowan KN, Heilbut A, Humpl T, Lam C, Ito S, et al. (2000) Complete reversal of fatal pulmonary hypertension in rats by a serine elastase inhibitor. Nat Med 6: 698-702.
    • (2000) Nat Med , vol.6 , pp. 698-702
    • Cowan, K.N.1    Heilbut, A.2    Humpl, T.3    Lam, C.4    Ito, S.5
  • 46
    • 34248658381 scopus 로고    scopus 로고
    • alpha-1 antitrypsin inhibits caspase-3 activity, preventing lung endothelial cell apoptosis
    • Petrache I, Fijalkowska I, Medler TR, Skirball J, Cruz P, et al. (2006) alpha-1 antitrypsin inhibits caspase-3 activity, preventing lung endothelial cell apoptosis. Am J Pathol 169: 1155-1166.
    • (2006) Am J Pathol , vol.169 , pp. 1155-1166
    • Petrache, I.1    Fijalkowska, I.2    Medler, T.R.3    Skirball, J.4    Cruz, P.5
  • 47
    • 33644865928 scopus 로고    scopus 로고
    • Bone morphogenetic protein receptor-2 signaling promotes pulmonary arterial endothelial cell survival: implications for loss-of-function mutations in the pathogenesis of pulmonary hypertension
    • Teichert-Kuliszewska K, Kutryk MJ, Kuliszewski MA, Karoubi G, Courtman DW, et al. (2006) Bone morphogenetic protein receptor-2 signaling promotes pulmonary arterial endothelial cell survival: implications for loss-of-function mutations in the pathogenesis of pulmonary hypertension. Circ Res 98: 209-217.
    • (2006) Circ Res , vol.98 , pp. 209-217
    • Teichert-Kuliszewska, K.1    Kutryk, M.J.2    Kuliszewski, M.A.3    Karoubi, G.4    Courtman, D.W.5
  • 48
    • 14844360656 scopus 로고    scopus 로고
    • Rescue of monocrotaline-induced pulmonary arterial hypertension using bone marrow-derived endothelial-like progenitor cells: efficacy of combined cell and eNOS gene therapy in established disease
    • Zhao YD, Courtman DW, Deng Y, Kugathasan L, Zhang Q, et al. (2005) Rescue of monocrotaline-induced pulmonary arterial hypertension using bone marrow-derived endothelial-like progenitor cells: efficacy of combined cell and eNOS gene therapy in established disease. Circ Res 96: 442-450.
    • (2005) Circ Res , vol.96 , pp. 442-450
    • Zhao, Y.D.1    Courtman, D.W.2    Deng, Y.3    Kugathasan, L.4    Zhang, Q.5
  • 50
    • 1942510459 scopus 로고    scopus 로고
    • Nitric oxide and other novel therapies for pulmonary hypertension
    • Napoli C, Loscalzo J, (2004) Nitric oxide and other novel therapies for pulmonary hypertension. J Cardiovasc Pharmacol Ther 9: 1-8.
    • (2004) J Cardiovasc Pharmacol Ther , vol.9 , pp. 1-8
    • Napoli, C.1    Loscalzo, J.2
  • 51
    • 17144460129 scopus 로고
    • Haptoglobin: the evolutionary product of duplication, unequal crossing over, and point mutation
    • Bowman BH, Kurosky A (1982) Haptoglobin: the evolutionary product of duplication, unequal crossing over, and point mutation. Adv Hum Genet 12: 189-261, 453-184.
    • (1982) Adv Hum Genet , vol.12
    • Bowman, B.H.1    Kurosky, A.2
  • 52
    • 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
  • 54
    • 2942542718 scopus 로고    scopus 로고
    • Haptoglobin polymorphisms and iron homeostasis in health and in disease
    • Van Vlierberghe H, Langlois M, Delanghe J, (2004) Haptoglobin polymorphisms and iron homeostasis in health and in disease. Clin Chim Acta 345: 35-42.
    • (2004) Clin Chim Acta , vol.345 , pp. 35-42
    • Van Vlierberghe, H.1    Langlois, M.2    Delanghe, J.3
  • 55
    • 0032530341 scopus 로고    scopus 로고
    • Increased susceptibility in Hp knockout mice during acute hemolysis
    • Lim SK, Kim H, bin Ali A, Lim YK, Wang Y, et al. (1998) Increased susceptibility in Hp knockout mice during acute hemolysis. Blood 92: 1870-1877.
    • (1998) Blood , vol.92 , pp. 1870-1877
    • Lim, S.K.1    Kim, H.2    Bin Ali, A.3    Lim, Y.K.4    Wang, Y.5
  • 56
    • 0022261994 scopus 로고
    • A novel proteolytic activity in serum processes rat prohaptoglobin
    • Hanley JM, Heath EC, (1985) A novel proteolytic activity in serum processes rat prohaptoglobin. Arch Biochem Biophys 239: 404-419.
    • (1985) Arch Biochem Biophys , vol.239 , pp. 404-419
    • Hanley, J.M.1    Heath, E.C.2
  • 57
    • 0033840280 scopus 로고    scopus 로고
    • Haptoglobin is a natural regulator of Langerhans cell function in the skin
    • Xie Y, Li Y, Zhang Q, Stiller MJ, Wang CL, et al. (2000) Haptoglobin is a natural regulator of Langerhans cell function in the skin. J Dermatol Sci 24: 25-37.
    • (2000) J Dermatol Sci , vol.24 , pp. 25-37
    • Xie, Y.1    Li, Y.2    Zhang, Q.3    Stiller, M.J.4    Wang, C.L.5
  • 58
    • 0023264947 scopus 로고
    • An analogy between fetal haptoglobin and a potent immunosuppressant in cancer
    • Oh SK, Very DL, Walker J, Raam S, Ju ST, (1987) An analogy between fetal haptoglobin and a potent immunosuppressant in cancer. Cancer Res 47: 5120-5126.
    • (1987) Cancer Res , vol.47 , pp. 5120-5126
    • Oh, S.K.1    Very, D.L.2    Walker, J.3    Raam, S.4    Ju, S.T.5
  • 59
    • 0027399278 scopus 로고
    • Identification of haptoglobin as an angiogenic factor in sera from patients with systemic vasculitis
    • Cid MC, Grant DS, Hoffman GS, Auerbach R, Fauci AS, et al. (1993) Identification of haptoglobin as an angiogenic factor in sera from patients with systemic vasculitis. J Clin Invest 91: 977-985.
    • (1993) J Clin Invest , vol.91 , pp. 977-985
    • Cid, M.C.1    Grant, D.S.2    Hoffman, G.S.3    Auerbach, R.4    Fauci, A.S.5
  • 60
    • 0019467841 scopus 로고
    • Haptoglobin. A novel mode of biosynthesis of a liver secretory glycoprotein
    • Haugen TH, Hanley JM, Heath EC, (1981) Haptoglobin. A novel mode of biosynthesis of a liver secretory glycoprotein. J Biol Chem 256: 1055-1057.
    • (1981) J Biol Chem , vol.256 , pp. 1055-1057
    • Haugen, T.H.1    Hanley, J.M.2    Heath, E.C.3
  • 61
    • 0017721398 scopus 로고
    • High resolution two-dimensional electrophoresis of human plasma proteins
    • Anderson L, Anderson NG, (1977) High resolution two-dimensional electrophoresis of human plasma proteins. Proc Natl Acad Sci U S A 74: 5421-5425.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 5421-5425
    • Anderson, L.1    Anderson, N.G.2
  • 62
    • 23844456707 scopus 로고    scopus 로고
    • Serum levels of leptin, insulin, and lipids in relation to breast cancer in china
    • Han C, Zhang HT, Du L, Liu X, Jing J, et al. (2005) Serum levels of leptin, insulin, and lipids in relation to breast cancer in china. Endocrine 26: 19-24.
    • (2005) Endocrine , vol.26 , pp. 19-24
    • Han, C.1    Zhang, H.T.2    Du, L.3    Liu, X.4    Jing, J.5
  • 63
    • 34548439900 scopus 로고    scopus 로고
    • Structural requirements for antioxidative and anti-inflammatory properties of apolipoprotein A-I mimetic peptides
    • Anantharamaiah GM, Mishra VK, Garber DW, Datta G, Handattu SP, et al. (2007) Structural requirements for antioxidative and anti-inflammatory properties of apolipoprotein A-I mimetic peptides. J Lipid Res 48: 1915-1923.
    • (2007) J Lipid Res , vol.48 , pp. 1915-1923
    • Anantharamaiah, G.M.1    Mishra, V.K.2    Garber, D.W.3    Datta, G.4    Handattu, S.P.5
  • 65
    • 77956861083 scopus 로고    scopus 로고
    • Genetic deletion of apolipoprotein A-I increases airway hyperresponsiveness, inflammation, and collagen deposition in the lung
    • Wang W, Xu H, Shi Y, Nandedkar S, Zhang H, et al. (2010) Genetic deletion of apolipoprotein A-I increases airway hyperresponsiveness, inflammation, and collagen deposition in the lung. J Lipid Res 51: 2560-2570.
    • (2010) J Lipid Res , vol.51 , pp. 2560-2570
    • Wang, W.1    Xu, H.2    Shi, Y.3    Nandedkar, S.4    Zhang, H.5
  • 66
    • 0027998527 scopus 로고
    • Transthyretin (prealbumin) in health and disease: nutritional implications
    • Ingenbleek Y, Young V, (1994) Transthyretin (prealbumin) in health and disease: nutritional implications. Annu Rev Nutr 14: 495-533.
    • (1994) Annu Rev Nutr , vol.14 , pp. 495-533
    • Ingenbleek, Y.1    Young, V.2
  • 67
    • 0036910380 scopus 로고    scopus 로고
    • Transthyretin as a thyroid hormone carrier: function revisited
    • Palha JA, (2002) Transthyretin as a thyroid hormone carrier: function revisited. Clin Chem Lab Med 40: 1292-1300.
    • (2002) Clin Chem Lab Med , vol.40 , pp. 1292-1300
    • Palha, J.A.1
  • 68
    • 4544363879 scopus 로고    scopus 로고
    • Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation
    • Chang MH, Hua CT, Isaac EL, Litjens T, Hodge G, et al. (2004) Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulation. Biochem J 382: 481-489.
    • (2004) Biochem J , vol.382 , pp. 481-489
    • Chang, M.H.1    Hua, C.T.2    Isaac, E.L.3    Litjens, T.4    Hodge, G.5
  • 69
    • 0036915485 scopus 로고    scopus 로고
    • Protein status in pancreatitis-transthyretin is a sensitive biomarker of malnutrition in acute and chronic pancreatitis
    • Lasztity N, Biro L, Nemeth E, Pap A, Antal M, (2002) Protein status in pancreatitis-transthyretin is a sensitive biomarker of malnutrition in acute and chronic pancreatitis. Clin Chem Lab Med 40: 1320-1324.
    • (2002) Clin Chem Lab Med , vol.40 , pp. 1320-1324
    • Lasztity, N.1    Biro, L.2    Nemeth, E.3    Pap, A.4    Antal, M.5
  • 70
    • 4143067096 scopus 로고    scopus 로고
    • Three biomarkers identified from serum proteomic analysis for the detection of early stage ovarian cancer
    • Zhang Z, Bast RC Jr, Yu Y, Li J, Sokoll LJ, et al. (2004) Three biomarkers identified from serum proteomic analysis for the detection of early stage ovarian cancer. Cancer Res 64: 5882-5890.
    • (2004) Cancer Res , vol.64 , pp. 5882-5890
    • Zhang, Z.1    Bast Jr., R.C.2    Yu, Y.3    Li, J.4    Sokoll, L.J.5
  • 71
    • 13444271567 scopus 로고    scopus 로고
    • Transthyretin, a biomarker for nutritional status and ovarian cancer
    • author reply 1114
    • Schweigert FJ, Sehouli J (2005) Transthyretin, a biomarker for nutritional status and ovarian cancer. Cancer Res 65: 1114; author reply 1114.
    • (2005) Cancer Res , vol.65 , pp. 1114
    • Schweigert, F.J.1    Sehouli, J.2
  • 72
  • 73
    • 0036915486 scopus 로고    scopus 로고
    • The prognostic value of nutritional and inflammatory indices in critically ill patients with acute respiratory failure
    • Schlossmacher P, Hasselmann M, Meyer N, Kara F, Delabranche X, et al. (2002) The prognostic value of nutritional and inflammatory indices in critically ill patients with acute respiratory failure. Clin Chem Lab Med 40: 1339-1343.
    • (2002) Clin Chem Lab Med , vol.40 , pp. 1339-1343
    • Schlossmacher, P.1    Hasselmann, M.2    Meyer, N.3    Kara, F.4    Delabranche, X.5
  • 74
    • 0037304903 scopus 로고    scopus 로고
    • Molecular characterization of hemoglobin alpha-D chains from Geochelone carbonaria and Geochelone denticulata land turtles
    • Melo MB, Bordin S, Duarte AS, Ogo SH, Torsoni MA, et al. (2003) Molecular characterization of hemoglobin alpha-D chains from Geochelone carbonaria and Geochelone denticulata land turtles. Comp Biochem Physiol B Biochem Mol Biol 134: 389-395.
    • (2003) Comp Biochem Physiol B Biochem Mol Biol , vol.134 , pp. 389-395
    • Melo, M.B.1    Bordin, S.2    Duarte, A.S.3    Ogo, S.H.4    Torsoni, M.A.5
  • 75
    • 0028127972 scopus 로고
    • Red blood cell function in hypoxia at altitude and exercise
    • Mairbaurl H, (1994) Red blood cell function in hypoxia at altitude and exercise. Int J Sports Med 15: 51-63.
    • (1994) Int J Sports Med , vol.15 , pp. 51-63
    • Mairbaurl, H.1
  • 77
    • 43749090222 scopus 로고    scopus 로고
    • Iron and anemia in human biology: a review of mechanisms
    • Handelman GJ, Levin NW, (2008) Iron and anemia in human biology: a review of mechanisms. Heart Fail Rev 13: 393-404.
    • (2008) Heart Fail Rev , vol.13 , pp. 393-404
    • Handelman, G.J.1    Levin, N.W.2
  • 78
    • 0000655498 scopus 로고    scopus 로고
    • Identification of a hypoxia response element in the transferrin receptor gene
    • Lok CN, Ponka P, (1999) Identification of a hypoxia response element in the transferrin receptor gene. J Biol Chem 274: 24147-24152.
    • (1999) J Biol Chem , vol.274 , pp. 24147-24152
    • Lok, C.N.1    Ponka, P.2
  • 79
    • 0033588021 scopus 로고    scopus 로고
    • Transferrin receptor induction by hypoxia. HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation
    • Tacchini L, Bianchi L, Bernelli-Zazzera A, Cairo G, (1999) Transferrin receptor induction by hypoxia. HIF-1-mediated transcriptional activation and cell-specific post-transcriptional regulation. J Biol Chem 274: 24142-24146.
    • (1999) J Biol Chem , vol.274 , pp. 24142-24146
    • Tacchini, L.1    Bianchi, L.2    Bernelli-Zazzera, A.3    Cairo, G.4
  • 80
    • 0030739637 scopus 로고    scopus 로고
    • Transport of iron in the blood-brain-cerebrospinal fluid system
    • Bradbury MW, (1997) Transport of iron in the blood-brain-cerebrospinal fluid system. J Neurochem 69: 443-454.
    • (1997) J Neurochem , vol.69 , pp. 443-454
    • Bradbury, M.W.1
  • 82
    • 0023713738 scopus 로고
    • A pentameric form of human serum amyloid P component. Crystallization, X-ray diffraction and neutron scattering studies
    • Wood SP, Oliva G, O'Hara BP, White HE, Blundell TL, et al. (1988) A pentameric form of human serum amyloid P component. Crystallization, X-ray diffraction and neutron scattering studies. J Mol Biol 202: 169-173.
    • (1988) J Mol Biol , vol.202 , pp. 169-173
    • Wood, S.P.1    Oliva, G.2    O'Hara, B.P.3    White, H.E.4    Blundell, T.L.5
  • 83
    • 0023617937 scopus 로고
    • Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum
    • Pepys MB, Butler PJ, (1987) Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum. Biochem Biophys Res Commun 148: 308-313.
    • (1987) Biochem Biophys Res Commun , vol.148 , pp. 308-313
    • Pepys, M.B.1    Butler, P.J.2
  • 84
    • 0034687703 scopus 로고    scopus 로고
    • Role of serum amyloid P component in bacterial infection: protection of the host or protection of the pathogen
    • Noursadeghi M, Bickerstaff MC, Gallimore JR, Herbert J, Cohen J, et al. (2000) Role of serum amyloid P component in bacterial infection: protection of the host or protection of the pathogen. Proc Natl Acad Sci U S A 97: 14584-14589.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 14584-14589
    • Noursadeghi, M.1    Bickerstaff, M.C.2    Gallimore, J.R.3    Herbert, J.4    Cohen, J.5
  • 85
    • 0029010736 scopus 로고
    • Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis
    • Tennent GA, Lovat LB, Pepys MB, (1995) Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc Natl Acad Sci U S A 92: 4299-4303.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 4299-4303
    • Tennent, G.A.1    Lovat, L.B.2    Pepys, M.B.3
  • 86
    • 0030757182 scopus 로고    scopus 로고
    • Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene
    • Botto M, Hawkins PN, Bickerstaff MC, Herbert J, Bygrave AE, et al. (1997) Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Nat Med 3: 855-859.
    • (1997) Nat Med , vol.3 , pp. 855-859
    • Botto, M.1    Hawkins, P.N.2    Bickerstaff, M.C.3    Herbert, J.4    Bygrave, A.E.5
  • 87
    • 0037118028 scopus 로고    scopus 로고
    • Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
    • Pepys MB, Herbert J, Hutchinson WL, Tennent GA, Lachmann HJ, et al. (2002) Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature 417: 254-259.
    • (2002) Nature , vol.417 , pp. 254-259
    • Pepys, M.B.1    Herbert, J.2    Hutchinson, W.L.3    Tennent, G.A.4    Lachmann, H.J.5
  • 88
    • 33744945033 scopus 로고    scopus 로고
    • Mechanisms of Disease: the complement system and the pathogenesis of systemic lupus erythematosus
    • Cook HT, Botto M, (2006) Mechanisms of Disease: the complement system and the pathogenesis of systemic lupus erythematosus. Nat Clin Pract Rheumatol 2: 330-337.
    • (2006) Nat Clin Pract Rheumatol , vol.2 , pp. 330-337
    • Cook, H.T.1    Botto, M.2
  • 89
    • 37349066319 scopus 로고    scopus 로고
    • Complement deficiencies and systemic lupus erythematosus
    • Truedsson L, Bengtsson AA, Sturfelt G, (2007) Complement deficiencies and systemic lupus erythematosus. Autoimmunity 40: 560-566.
    • (2007) Autoimmunity , vol.40 , pp. 560-566
    • Truedsson, L.1    Bengtsson, A.A.2    Sturfelt, G.3
  • 90
    • 33645686069 scopus 로고    scopus 로고
    • Identification of plasma protein biomarkers associated with idiopathic pulmonary arterial hypertension
    • Abdul-Salam VB, Paul GA, Ali JO, Gibbs SR, Rahman D, et al. (2006) Identification of plasma protein biomarkers associated with idiopathic pulmonary arterial hypertension. Proteomics 6: 2286-2294.
    • (2006) Proteomics , vol.6 , pp. 2286-2294
    • Abdul-Salam, V.B.1    Paul, G.A.2    Ali, J.O.3    Gibbs, S.R.4    Rahman, D.5
  • 91
    • 70449523330 scopus 로고    scopus 로고
    • Potential diagnostic biomarkers in serum of idiopathic pulmonary arterial hypertension
    • Zhang J, Zhang Y, Li N, Liu Z, Xiong C, et al. (2009) Potential diagnostic biomarkers in serum of idiopathic pulmonary arterial hypertension. Respir Med 103: 1801-1806.
    • (2009) Respir Med , vol.103 , pp. 1801-1806
    • Zhang, J.1    Zhang, Y.2    Li, N.3    Liu, Z.4    Xiong, C.5
  • 92
    • 83355176600 scopus 로고    scopus 로고
    • Complement C3 deficiency attenuates chronic hypoxia-induced pulmonary hypertension in mice
    • Bauer EM, Zheng H, Comhair S, Erzurum S, Billiar TR, et al. (2011) Complement C3 deficiency attenuates chronic hypoxia-induced pulmonary hypertension in mice. PLoS One 6: e28578.
    • (2011) PLoS One , vol.6
    • Bauer, E.M.1    Zheng, H.2    Comhair, S.3    Erzurum, S.4    Billiar, T.R.5
  • 93
    • 0030022473 scopus 로고    scopus 로고
    • Retinol binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells
    • Bellovino D, Morimoto T, Tosetti F, Gaetani S, (1996) Retinol binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells. Exp Cell Res 222: 77-83.
    • (1996) Exp Cell Res , vol.222 , pp. 77-83
    • Bellovino, D.1    Morimoto, T.2    Tosetti, F.3    Gaetani, S.4
  • 94
    • 22944434929 scopus 로고    scopus 로고
    • Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes
    • Yang Q, Graham TE, Mody N, Preitner F, Peroni OD, et al. (2005) Serum retinol binding protein 4 contributes to insulin resistance in obesity and type 2 diabetes. Nature 436: 356-362.
    • (2005) Nature , vol.436 , pp. 356-362
    • Yang, Q.1    Graham, T.E.2    Mody, N.3    Preitner, F.4    Peroni, O.D.5
  • 95
    • 34347208708 scopus 로고    scopus 로고
    • Serum retinol-binding protein: a link between obesity, insulin resistance, and type 2 diabetes
    • Wolf G, (2007) Serum retinol-binding protein: a link between obesity, insulin resistance, and type 2 diabetes. Nutr Rev 65: 251-256.
    • (2007) Nutr Rev , vol.65 , pp. 251-256
    • Wolf, G.1
  • 96
    • 84861403641 scopus 로고    scopus 로고
    • Retinol-binding protein 4 inhibits insulin signaling in adipocytes by inducing proinflammatory cytokines in macrophages through a c-Jun N-terminal kinase- and toll-like receptor 4-dependent and retinol-independent mechanism
    • Norseen J, Hosooka T, Hammarstedt A, Yore MM, Kant S, et al. (2012) Retinol-binding protein 4 inhibits insulin signaling in adipocytes by inducing proinflammatory cytokines in macrophages through a c-Jun N-terminal kinase- and toll-like receptor 4-dependent and retinol-independent mechanism. Mol Cell Biol 32: 2010-2019.
    • (2012) Mol Cell Biol , vol.32 , pp. 2010-2019
    • Norseen, J.1    Hosooka, T.2    Hammarstedt, A.3    Yore, M.M.4    Kant, S.5
  • 97
    • 0033198844 scopus 로고    scopus 로고
    • Impaired retinal function and vitamin A availability in mice lacking retinol-binding protein
    • Quadro L, Blaner WS, Salchow DJ, Vogel S, Piantedosi R, et al. (1999) Impaired retinal function and vitamin A availability in mice lacking retinol-binding protein. EMBO J 18: 4633-4644.
    • (1999) EMBO J , vol.18 , pp. 4633-4644
    • Quadro, L.1    Blaner, W.S.2    Salchow, D.J.3    Vogel, S.4    Piantedosi, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.