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Volumn 49, Issue 2, 2012, Pages 129-133

Changes in protein profile of erythrocyte membrane in bronchial asthma

Author keywords

Blood; Bronchial asthma; Erythrocytes; Membrane; Protein profile

Indexed keywords

ADDUCIN; ADDUCIN I; ADDUCIN II; BETA ACTIN; CELL MEMBRANE PROTEIN; ERYTHROCYTE BAND 4.1 PROTEIN; ERYTHROCYTE BAND 4.2 PROTEIN; ERYTHROCYTE BAND 4.9 PROTEIN; ERYTHROCYTE MEMBRANE PROTEIN; GALECTIN 3; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 84856907909     PISSN: 02770903     EISSN: 15324303     Source Type: Journal    
DOI: 10.3109/02770903.2011.649873     Document Type: Article
Times cited : (7)

References (28)
  • 1
    • 0036746499 scopus 로고    scopus 로고
    • Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ ionization-time of flight mass spectrometry
    • Low TY, Seow TK, Chung MC. Separation of human erythrocyte membrane associated proteins with one-dimensional and two-dimensional gel electrophoresis followed by identification with matrix-assisted laser desorption/ ionization-time of flight mass spectrometry. Proteomics 2002; 2:1229-1239.
    • (2002) Proteomics , vol.2 , pp. 1229-1239
    • Low, T.Y.1    Seow, T.K.2    Chung, M.C.3
  • 2
    • 0018140115 scopus 로고
    • Gel electrophoresis of the human erythrocyte membrane proteins: Aberrant patterns in hematological and non-hematological diseases
    • DOI 10.1007/BF00996652
    • Anselstetter V. Gel eleetrophoresis of the human erytbrocyte membrane proteins aberrant patterns in hematological and non-hematological diseases. Blut 1978; 36:135-144. (Pubitemid 8319660)
    • (1978) Blut , vol.36 , Issue.3 , pp. 135-144
    • Anselstetter, V.1
  • 3
    • 33847334329 scopus 로고    scopus 로고
    • Viruses, lipid rafts and signal transduction
    • DOI 10.1002/sita.200600113
    • Rauch S, Fackler OT. Viruses, lipid rafts and signal transduction. Signal Transduct 2007; 7:53-63. (Pubitemid 46326743)
    • (2007) Signal Transduction , vol.7 , Issue.1 , pp. 53-63
    • Rauch, S.1    Fackler, O.T.2
  • 5
    • 0033055564 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae
    • DOI 10.1080/096876899294607
    • Hooper NM. Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae. Mol Membr Biol 1999; 16:145-156. (Pubitemid 29308814)
    • (1999) Molecular Membrane Biology , vol.16 , Issue.2 , pp. 145-156
    • Hooper, N.M.1
  • 6
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • DOI 10.1016/S0167-4889(99)00075-0, PII S0167488999000750
    • Resh MD. Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta 1999; 1451:1-16. (Pubitemid 29364242)
    • (1999) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1451 , Issue.1 , pp. 1-16
    • Resh, M.D.1
  • 7
    • 0033597141 scopus 로고    scopus 로고
    • Association of sterol- and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains
    • Rietveld A, Neutz S, Simons K, Eaton S. Association of sterol- and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains. J Biol Chem 1999; 274:12049-12054.
    • (1999) J Biol Chem , vol.274 , pp. 12049-12054
    • Rietveld, A.1    Neutz, S.2    Simons, K.3    Eaton, S.4
  • 8
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • DOI 10.1083/jcb.141.4.929
    • Harder T, Scheiffele P, Verkade P, Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J Cell Biol 1998; 141:929-942. (Pubitemid 28243961)
    • (1998) Journal of Cell Biology , vol.141 , Issue.4 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 9
    • 0037370756 scopus 로고    scopus 로고
    • Regulation of erythrocyte membrane protein gene expression
    • DOI 10.1097/00062752-200303000-00003
    • Gallagher PG. Regulation of erythrocyte membrane protein gene expression. Curr Opin Hematol 2003; 10:115-122. (Pubitemid 36207965)
    • (2003) Current Opinion in Hematology , vol.10 , Issue.2 , pp. 115-122
    • Gallagher, P.G.1
  • 11
    • 57649129461 scopus 로고    scopus 로고
    • Protective effect of ginsenosides Rg(2) and Rh(1) on oxidation-induced impairment of erythrocyte membrane properties
    • Samukawa K, Suzuki Y, Ohkubo N, Aoto M, Sakanaka M, Mitsuda N. Protective effect of ginsenosides Rg(2) and Rh(1) on oxidation-induced impairment of erythrocyte membrane properties. Biorheology 2008; 45:689-700.
    • (2008) Biorheology , vol.45 , pp. 689-700
    • Samukawa, K.1    Suzuki, Y.2    Ohkubo, N.3    Aoto, M.4    Sakanaka, M.5    Mitsuda, N.6
  • 12
    • 0031892421 scopus 로고    scopus 로고
    • Effect of ethanol and formate radicals on erythrocyte membrane proteins
    • DOI 10.1080/095530098142608
    • Soszynski M, Schuessler H. Effect of ethanol and formate radicals on erythrocyte membrane proteins. Int J Radiat Biol 1998; 73:211-218. (Pubitemid 28104413)
    • (1998) International Journal of Radiation Biology , vol.73 , Issue.2 , pp. 211-218
    • Soszynski, M.1    Schuessler, H.2
  • 13
    • 0018139526 scopus 로고
    • Abnormal erythrocyte membrane protein pattern in severe megaloblastic anemia
    • Ballas SK. Abnormal erythrocyte membrane protein pattern in severe megaloblastic anemia. J Clin Invest 1978; 61:1097-1101. (Pubitemid 8321087)
    • (1978) Journal of Clinical Investigation , vol.61 , Issue.4 , pp. 1097-1101
    • Ballas, S.K.1
  • 18
    • 34248504870 scopus 로고    scopus 로고
    • Chloride channels in normal and cystic fibrosis human erythrocyte membrane
    • DOI 10.1016/j.bcmd.2007.02.014, PII S1079979607000691
    • Decherf G, Bouyer G, Egée S, Thomas SL. Chloride channels in normal and cystic fibrosis human erythrocyte membrane. Blood Cells Mol Dis 2007; 39:24-34. (Pubitemid 46754930)
    • (2007) Blood Cells, Molecules, and Diseases , vol.39 , Issue.1 , pp. 24-34
    • Decherf, G.1    Bouyer, G.2    Egee, S.3    Thomas, S.L.Y.4
  • 19
    • 0004002716 scopus 로고    scopus 로고
    • Expert Panel Report 2. Bethesda: National Institutes of Health, National Heart, Lung and Blood Institute Information Center
    • Guidelines for the Diagnosis and Management of Asthma. Expert Panel Report 2. Bethesda: National Institutes of Health, National Heart, Lung and Blood Institute Information Center, 1997.
    • (1997) Guidelines for the Diagnosis and Management of Asthma
  • 20
    • 0016961001 scopus 로고
    • Isolation of lymphocytes, granulocytes and macrophages
    • Boyum A. Isolation of lymphocytes, granulocytes and macrophages. Scand J Immunol Suppl 1976; 5:9-15.
    • (1976) Scand J Immunol Suppl , vol.5 , pp. 9-15
    • Boyum, A.1
  • 21
    • 0016355004 scopus 로고
    • Methods in enzymology
    • In Colowick SP, Kaplan NO, eds New York Academic Press
    • Hanahan DJ, Ekholm JE. Methods in enzymology. In: Colowick SP, Kaplan NO, eds. The Preparation of Red Cell Ghosts (Membranes). Vol XXXI. New York: Academic Press, 1974:168-172.
    • (1974) The Preparation of Red Cell Ghosts (Membranes) , vol.31 , pp. 168-172
    • Hanahan, D.J.1    Ekholm, J.E.2
  • 23
    • 0023600841 scopus 로고
    • Erythrocyte adducin: A calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding
    • DOI 10.1083/jcb.105.6.2837
    • Mische SM, Mooseker MS, Morrow JS. Erythrocyte adducin: A calmodulin-regulated actin-bundling protein that stimulates spectrinactin binding. J Cell Biol 1987; 105:2837-2845. (Pubitemid 18017714)
    • (1987) Journal of Cell Biology , vol.105 , Issue.6 , pp. 2837-2845
    • Mische, S.M.1    Mooseker, M.S.2    Morrow, J.S.3
  • 24
    • 0026497661 scopus 로고
    • Cytoskeleton-plasma membrane interactions
    • Luna EJ, Hitt AL. Cytoskeleton-plasma membrane interactions. Science 1991; 258:955-964.
    • (1991) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 26
    • 0023867132 scopus 로고
    • Deficiency of protein 4.2 in erythrocytes from a patient with a Coombs negative hemolytic anemia. Evidence for a role of protein 4.2 in stabilizing ankyrin on the membrane
    • Rybicki AC, Heath R, Wolf JL, Lubin B, Schwartz RS. Deficiency of protein 4.2 in erythrocytes from a patient with a coombs negative hemolytic anemia: Evidence for a role of protein 4.2 in stabilizing ankyrin on the membrane.J Clin Invest 1988; 81:893-901. (Pubitemid 18079742)
    • (1988) Journal of Clinical Investigation , vol.81 , Issue.3 , pp. 893-901
    • Rybicki, A.C.1    Heath, R.2    Wolf, J.L.3    Lubin, B.4    Schwartz, R.S.5
  • 27
    • 78651356179 scopus 로고    scopus 로고
    • Regulated expression of galectin-3 a multifunctional glycan-binding protein in haematopoietic and non-haematopoietic tissues
    • Sundblad V, Croci DO, Rabinovich GA. Regulated expression of galectin-3, a multifunctional glycan-binding protein, in haematopoietic and non-haematopoietic tissues. Histol Histopathol 2011; 26(2): 247-265.
    • (2011) Histol Histopathol , vol.26 , Issue.2 , pp. 247-265
    • Sundblad, V.1    Croci, D.O.2    Rabinovich, G.A.3
  • 28
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • DOI 10.1126/science.290.5497.1721
    • Simons K, Ikonen E. How cells handle cholesterol. Science 2000; 290:1721-1726. (Pubitemid 32004797)
    • (2000) Science , vol.290 , Issue.5497 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.