메뉴 건너뛰기




Volumn 93, Issue 1, 1999, Pages 376-384

Evaluation of biochemical changes during in vivo erythrocyte senescence in the dog

Author keywords

[No Author keywords available]

Indexed keywords

ERYTHROCYTE BAND 3 PROTEIN; IMMUNOGLOBULIN G; INTEGRAL MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 0032939337     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v93.1.376     Document Type: Article
Times cited : (93)

References (76)
  • 1
    • 0002063739 scopus 로고
    • Destruction of erythrocytes
    • Lee GR, Bithell TC, Foerster J, Athens JW, Lukens JN (eds): Philadelphia, PA, Lea & Febiger
    • Deiss A: Destruction of erythrocytes, in Lee GR, Bithell TC, Foerster J, Athens JW, Lukens JN (eds): Wintrobe's Clinical Hematology, Philadelphia, PA, Lea & Febiger, 1993, p 195
    • (1993) Wintrobe's Clinical Hematology , pp. 195
    • Deiss, A.1
  • 2
    • 0023943252 scopus 로고
    • Senescence of red blood cells: Progress and problems
    • Clark MR: Senescence of red blood cells: Progress and problems. Physiol Rev 68:503, 1988
    • (1988) Physiol Rev , vol.68 , pp. 503
    • Clark, M.R.1
  • 3
    • 0014890186 scopus 로고
    • 51Cr-half life of heavy and ligh human erythrocytes
    • 51Cr-half life of heavy and ligh human erythrocytes. Scand J Haematol 7:336, 1970
    • (1970) Scand J Haematol , vol.7 , pp. 336
    • Ten Brinke, M.1    De Regt, J.2
  • 6
    • 0025251722 scopus 로고
    • Density fractionation of erythrocytes by Percoll/hypaque results in only a slight enrichment for aged cells
    • Dale GL, Norenberg SL: Density fractionation of erythrocytes by Percoll/hypaque results in only a slight enrichment for aged cells. Biochim Biophys Acta 1036:183, 1990
    • (1990) Biochim Biophys Acta , vol.1036 , pp. 183
    • Dale, G.L.1    Norenberg, S.L.2
  • 8
    • 0023550669 scopus 로고
    • Biotinylated erythrocytes: In vivo survival and in vitro recovery
    • Suzuki T, Dale GL: Biotinylated erythrocytes: In vivo survival and in vitro recovery. Blood 70:791, 1987
    • (1987) Blood , vol.70 , pp. 791
    • Suzuki, T.1    Dale, G.L.2
  • 10
    • 0023971165 scopus 로고
    • Senescent erythrocytes: Isolation of in vivo aged cells and their biochemical characteristics
    • Suzuki T, Dale GL: Senescent erythrocytes: Isolation of in vivo aged cells and their biochemical characteristics. Proc Natl Acad Sci USA 85:1647, 1988
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1647
    • Suzuki, T.1    Dale, G.L.2
  • 11
    • 0024537861 scopus 로고
    • Membrane proteins in senescent erythrocytes
    • Suzuki T, Dale GL: Membrane proteins in senescent erythrocytes. Biochem J 257:37, 1989
    • (1989) Biochem J , vol.257 , pp. 37
    • Suzuki, T.1    Dale, G.L.2
  • 12
    • 0024457850 scopus 로고
    • Time-dependent loss of adenosine 5′-monophosphate deaminase activity may explain elevated adenosine 5′-triphosphate levels in senescent erythrocytes
    • Dale GL, Norenburg SL: Time-dependent loss of adenosine 5′-monophosphate deaminase activity may explain elevated adenosine 5′-triphosphate levels in senescent erythrocytes. Blood 74:2157, 1989
    • (1989) Blood , vol.74 , pp. 2157
    • Dale, G.L.1    Norenburg, S.L.2
  • 13
    • 0025254048 scopus 로고
    • In vivo aging of red cell enzymes: Study of biotinylated red blood cells in rabbits
    • Zimran A, Forman L, Suzuki T, Dale GL, Beutler E: In vivo aging of red cell enzymes: Study of biotinylated red blood cells in rabbits. Am J Hematol 33:249, 1990
    • (1990) Am J Hematol , vol.33 , pp. 249
    • Zimran, A.1    Forman, L.2    Suzuki, T.3    Dale, G.L.4    Beutler, E.5
  • 14
    • 0026081713 scopus 로고
    • Quantitation of immunoglobulir associated with senescent erythrocytes from the rabbit
    • Dale GL, Daniels RB: Quantitation of immunoglobulir associated with senescent erythrocytes from the rabbit. Blood 77:1096, 1991
    • (1991) Blood , vol.77 , pp. 1096
    • Dale, G.L.1    Daniels, R.B.2
  • 15
    • 0026503909 scopus 로고
    • Rheologic properties of senescent erythrocytes: Loss of surface area and volume with red blood cell age
    • Waugh RE, Narla M, Jackson CW, Mueller TJ, Suzuki T, Dale GL: Rheologic properties of senescent erythrocytes: Loss of surface area and volume with red blood cell age. Blood 79:1351, 1992
    • (1992) Blood , vol.79 , pp. 1351
    • Waugh, R.E.1    Narla, M.2    Jackson, C.W.3    Mueller, T.J.4    Suzuki, T.5    Dale, G.L.6
  • 16
    • 0029794021 scopus 로고    scopus 로고
    • Specific loss of protein kinase activities in senescent erythrocytes
    • Jindal HK, Ai Z, Gascard P, Horton C, Cohen CM: Specific loss of protein kinase activities in senescent erythrocytes. Blood 88:1479, 1996
    • (1996) Blood , vol.88 , pp. 1479
    • Jindal, H.K.1    Ai, Z.2    Gascard, P.3    Horton, C.4    Cohen, C.M.5
  • 17
    • 0032539931 scopus 로고    scopus 로고
    • Phosphatidylserine exposure and red cell viability in red cell aging and in hemolytic anemia
    • Boas FE, Forman L, Beutler E: Phosphatidylserine exposure and red cell viability in red cell aging and in hemolytic anemia. Proc Natl Acad Sci USA 95:3077, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3077
    • Boas, F.E.1    Forman, L.2    Beutler, E.3
  • 18
    • 0345484329 scopus 로고
    • An analytical study of in vivo survival of limited populations of animal red blood cells tagged with radioiron
    • Brown IW Jr, Eadie GS: An analytical study of in vivo survival of limited populations of animal red blood cells tagged with radioiron. J Gen Physiol 36:327, 1953
    • (1953) J Gen Physiol , vol.36 , pp. 327
    • Brown I.W., Jr.1    Eadie, G.S.2
  • 19
    • 84958684981 scopus 로고
    • Erythrocyte life span in small animals, comparison of two methods employing radioiron
    • Burwell EL, Brickley BA, Finch CA: Erythrocyte life span in small animals, comparison of two methods employing radioiron. Am J Physiol 172:718, 1953
    • (1953) Am J Physiol , vol.172 , pp. 718
    • Burwell, E.L.1    Brickley, B.A.2    Finch, C.A.3
  • 20
    • 0030053469 scopus 로고    scopus 로고
    • Methodologic considerations for the use of canine in vivo aged biotinylated erythrocytes to study RBC senescence
    • Christian JA, Rebar AH, Boon GD, Low PS: Methodologic considerations for the use of canine in vivo aged biotinylated erythrocytes to study RBC senescence. Exp Hematol 24:82, 1996
    • (1996) Exp Hematol , vol.24 , pp. 82
    • Christian, J.A.1    Rebar, A.H.2    Boon, G.D.3    Low, P.S.4
  • 22
    • 0344622113 scopus 로고
    • Quantitative measurement of erythropoiesis in the dog
    • Weissman SM, Waldmann TA, Berlin NI: Quantitative measurement of erythropoiesis in the dog. Am J Physiol 198:183, 1960
    • (1960) Am J Physiol , vol.198 , pp. 183
    • Weissman, S.M.1    Waldmann, T.A.2    Berlin, N.I.3
  • 23
    • 0021969804 scopus 로고
    • The role of hemoglobin denaturation and band 3 clustering in red blood cell aging
    • Low PS, Waugh SM, Zinke K, Drenckhahn D: The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science 227:531, 1985
    • (1985) Science , vol.227 , pp. 531
    • Low, P.S.1    Waugh, S.M.2    Zinke, K.3    Drenckhahn, D.4
  • 24
    • 0026343738 scopus 로고
    • Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis
    • Turrini F, Arese P, Yuan J, Low PS: Clustering of integral membrane proteins of the human erythrocyte membrane stimulates autologous IgG binding, complement deposition, and phagocytosis. J Biol Chem 266:23611, 1991
    • (1991) J Biol Chem , vol.266 , pp. 23611
    • Turrini, F.1    Arese, P.2    Yuan, J.3    Low, P.S.4
  • 25
    • 0013331166 scopus 로고
    • Interaction of native and denatured hemoglobins with band 3: Consequences for erythrocyte structure and function
    • Agre P, Parker JC (eds): New York, NY, Dekker
    • Low PS: Interaction of native and denatured hemoglobins with band 3: Consequences for erythrocyte structure and function., in Agre P, Parker JC (eds): Red Blood Cell Membranes: Structure, Function and Clinical Implications. New York, NY, Dekker, 1989, p 237
    • (1989) Red Blood Cell Membranes: Structure, Function and Clinical Implications , pp. 237
    • Low, P.S.1
  • 26
    • 0031106036 scopus 로고    scopus 로고
    • Induction of band 3 aggregation in erythrocytes results in anti-band 3 autoantibody binding to the carbohydrate epitopes of band 3
    • Ando K, Kikugawa K, Beppu M: Induction of band 3 aggregation in erythrocytes results in anti-band 3 autoantibody binding to the carbohydrate epitopes of band 3. Arch Biochem Biophys 339:250, 1997
    • (1997) Arch Biochem Biophys , vol.339 , pp. 250
    • Ando, K.1    Kikugawa, K.2    Beppu, M.3
  • 27
    • 0346079412 scopus 로고
    • Naturally occuring anti-band 3 antibodies and complement together mediate phagocytosis of oxidatively stressed human erythrocytes
    • Lutz HU, Bussolino F, Flepp R, Flaser S, Stammler P, Kazatchkine MD, Arese P: Naturally occuring anti-band 3 antibodies and complement together mediate phagocytosis of oxidatively stressed human erythrocytes. Proc Natl Acad Sci USA 84:7368, 1987
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7368
    • Lutz, H.U.1    Bussolino, F.2    Flepp, R.3    Flaser, S.4    Stammler, P.5    Kazatchkine, M.D.6    Arese, P.7
  • 28
    • 0020923029 scopus 로고
    • Senescent red cell-bound IgG is attached to band 3 protein
    • Lutz HU, Stringaro-Wipf G: Senescent red cell-bound IgG is attached to band 3 protein. Biomed Biochim Acta 42:S117, 1983 (suppl)
    • (1983) Biomed Biochim Acta , vol.42 , Issue.SUPPL.
    • Lutz, H.U.1    Stringaro-Wipf, G.2
  • 29
    • 0041524601 scopus 로고
    • Co-clustering of denatured hemoglobin with band 3: Its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes
    • Schluter K, Drenckhahn D: Co-clustering of denatured hemoglobin with band 3: Its role in binding of autoantibodies against band 3 to abnormal and aged erythrocytes. Proc Natl Acad Sci USA 83:6137, 1986
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6137
    • Schluter, K.1    Drenckhahn, D.2
  • 30
    • 0019419617 scopus 로고
    • Aggregation of intramembrane particles in erythrocyte membranes treated with diamide
    • Kurantsin-Mills J, Lessin LS: Aggregation of intramembrane particles in erythrocyte membranes treated with diamide. Biochim Biophys Acta 641:129, 1981
    • (1981) Biochim Biophys Acta , vol.641 , pp. 129
    • Kurantsin-Mills, J.1    Lessin, L.S.2
  • 31
    • 0027288165 scopus 로고
    • Characterization of the autologous antibodies that opsonize erythrocytes with clustered integral membrane proteins
    • Turrini F, Mannu F, Arese P, Yuan J, Low PS: Characterization of the autologous antibodies that opsonize erythrocytes with clustered integral membrane proteins. Blood 81:3146, 1993
    • (1993) Blood , vol.81 , pp. 3146
    • Turrini, F.1    Mannu, F.2    Arese, P.3    Yuan, J.4    Low, P.S.5
  • 32
    • 0023814970 scopus 로고
    • Isolation and characterization of the hemichrome-stablized membrane protein aggregates from sickle erythrocytes
    • Kannan R, Labotka R, Low PS: Isolation and characterization of the hemichrome-stablized membrane protein aggregates from sickle erythrocytes. J Biol Chem 263:13766, 1988
    • (1988) J Biol Chem , vol.263 , pp. 13766
    • Kannan, R.1    Labotka, R.2    Low, P.S.3
  • 33
    • 0025862306 scopus 로고
    • Isolation and partial characterization of antibody-and globin-enriched complexes from membranes of dense human erythrocytes
    • Kannan R, Yuan J, Low PS: Isolation and partial characterization of antibody-and globin-enriched complexes from membranes of dense human erythrocytes. Biochem J 278:57, 1991
    • (1991) Biochem J , vol.278 , pp. 57
    • Kannan, R.1    Yuan, J.2    Low, P.S.3
  • 34
    • 0026704541 scopus 로고
    • Isolation, characterization, and immunoprecipitation studies of immune complexes from membranes of B-thalassemic erythrocytes
    • Yuan J, Kannan R, Shinar E, Rachmilewitz EA, Low PS: Isolation, characterization, and immunoprecipitation studies of immune complexes from membranes of B-thalassemic erythrocytes. Blood 79:3007, 1992
    • (1992) Blood , vol.79 , pp. 3007
    • Yuan, J.1    Kannan, R.2    Shinar, E.3    Rachmilewitz, E.A.4    Low, P.S.5
  • 35
    • 0027933629 scopus 로고
    • Involvement of sialylated poly-N-acetyllactosaminyl sugar chains of band 3 glycoprotein on senescent erythrocytes in anti-band 3 autoantibody binding
    • Ando K, Kikugawa K, Beppu M: Involvement of sialylated poly-N-acetyllactosaminyl sugar chains of band 3 glycoprotein on senescent erythrocytes in anti-band 3 autoantibody binding. J Biol Chem 269:19394, 1994
    • (1994) J Biol Chem , vol.269 , pp. 19394
    • Ando, K.1    Kikugawa, K.2    Beppu, M.3
  • 36
    • 0027493863 scopus 로고
    • Naturally occurring anti-band 3 antibodies bind to protein rather than to carbohydrate on band 3
    • Lutz HU, Gianora O, Nater M, Schweizer E, Stammler P: Naturally occurring anti-band 3 antibodies bind to protein rather than to carbohydrate on band 3. J Biol Chem 268:23562, 1993
    • (1993) J Biol Chem , vol.268 , pp. 23562
    • Lutz, H.U.1    Gianora, O.2    Nater, M.3    Schweizer, E.4    Stammler, P.5
  • 37
    • 0027453622 scopus 로고
    • Naturally occuring anti-band 3 antibodies have a unique affinity for C3
    • Lutz HU, Nater M, Stammler P: Naturally occuring anti-band 3 antibodies have a unique affinity for C3. Immunology 80:191, 1993
    • (1993) Immunology , vol.80 , pp. 191
    • Lutz, H.U.1    Nater, M.2    Stammler, P.3
  • 38
    • 0027183205 scopus 로고
    • Preferential formation of C3b-IgG complexes in vitro and in vivo from nascent C3b and naturally occurring anti-band 3 antibodies
    • Lutz HU, Stammler P, Fasler S: Preferential formation of C3b-IgG complexes in vitro and in vivo from nascent C3b and naturally occurring anti-band 3 antibodies. J Biol Chem 268:17418, 1993
    • (1993) J Biol Chem , vol.268 , pp. 17418
    • Lutz, H.U.1    Stammler, P.2    Fasler, S.3
  • 39
    • 0002909964 scopus 로고
    • Erythrocyte clearance
    • Harris JR (ed): New York, NY, Plenum
    • Lutz HU: Erythrocyte clearance, in Harris JR (ed): Blood Cell Biochemistry, vol 1. New York, NY, Plenum, 1990, p 81
    • (1990) Blood Cell Biochemistry , vol.1 , pp. 81
    • Lutz, H.U.1
  • 40
    • 0002571623 scopus 로고
    • Mechanism of removal of senescent cells by human macrophages in situ
    • Kay MMB: Mechanism of removal of senescent cells by human macrophages in situ. Proc Natl Acad Sci USA 72:3521, 1975
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3521
    • Kay, M.M.B.1
  • 41
    • 0027381031 scopus 로고
    • Senescence of canine biotinylated erythrocytes: Increased autologous immunoglobulin binding occurs on erythrocytes aged in vivo for 104 to 110 days
    • Christian JA, Rebar AH, Boon DG, Low PS: Senescence of canine biotinylated erythrocytes: Increased autologous immunoglobulin binding occurs on erythrocytes aged in vivo for 104 to 110 days. Blood 82:3469, 1993
    • (1993) Blood , vol.82 , pp. 3469
    • Christian, J.A.1    Rebar, A.H.2    Boon, D.G.3    Low, P.S.4
  • 42
    • 73649194769 scopus 로고
    • Improved method for the determination of blood glutathione
    • Beutler E, Duron O, Kelly BM: Improved method for the determination of blood glutathione. J Lab Clin Med 61:882, 1963
    • (1963) J Lab Clin Med , vol.61 , pp. 882
    • Beutler, E.1    Duron, O.2    Kelly, B.M.3
  • 43
    • 50549175610 scopus 로고
    • The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
    • Dodge JT, Mitchell C, Hanahan DJ: The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys 100:119, 1963
    • (1963) Arch Biochem Biophys , vol.100 , pp. 119
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 44
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350, 1979
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 45
    • 0027938023 scopus 로고
    • Molecular maps of red cell deformation: Hidden elasticity and in situ connectivity
    • Discher DE, Mohandas N, Evans EA: Molecular maps of red cell deformation: Hidden elasticity and in situ connectivity. Science 266: 1032, 1994
    • (1994) Science , vol.266 , pp. 1032
    • Discher, D.E.1    Mohandas, N.2    Evans, E.A.3
  • 46
    • 0029818016 scopus 로고    scopus 로고
    • Kinematics of red cell aspiration by fluorescence-imaged microdeformation
    • Discher DE, Mohandas N: Kinematics of red cell aspiration by fluorescence-imaged microdeformation. Biophys J 71:1680, 1996
    • (1996) Biophys J , vol.71 , pp. 1680
    • Discher, D.E.1    Mohandas, N.2
  • 47
    • 0020380627 scopus 로고
    • A new solid state reagent to iodinate proteins 1. Conditions for the efficient labeling of antisera
    • Markwell MAK: A new solid state reagent to iodinate proteins 1. Conditions for the efficient labeling of antisera. Anal Biochem 125:427, 1982
    • (1982) Anal Biochem , vol.125 , pp. 427
    • Markwell, M.A.K.1
  • 48
    • 0020081562 scopus 로고
    • Membrane-bound hemichrome in density-separated cohorts of normal (AA) and sickled (SS) cells
    • Campwala HQ, Desforges JF: Membrane-bound hemichrome in density-separated cohorts of normal (AA) and sickled (SS) cells. J Lab Clin Med 99:25, 1982
    • (1982) J Lab Clin Med , vol.99 , pp. 25
    • Campwala, H.Q.1    Desforges, J.F.2
  • 50
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography
    • Casey JR, Reithmeier RAF: Analysis of the oligomeric state of band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. J Biol Chem 266:15726, 1991
    • (1991) J Biol Chem , vol.266 , pp. 15726
    • Casey, J.R.1    Reithmeier, R.A.F.2
  • 51
    • 0030806488 scopus 로고    scopus 로고
    • Red cell membranes of ankyrin-deficient nb/nb mice lack band 3 tetramers but contain normal membrane skeletons
    • Yi SJ, Liu SC, Derick LH, Murray J, Barker JE, Cho MR, Palek J, Golan DE: Red cell membranes of ankyrin-deficient nb/nb mice lack band 3 tetramers but contain normal membrane skeletons. Biochemistry 36:9596, 1997
    • (1997) Biochemistry , vol.36 , pp. 9596
    • Yi, S.J.1    Liu, S.C.2    Derick, L.H.3    Murray, J.4    Barker, J.E.5    Cho, M.R.6    Palek, J.7    Golan, D.E.8
  • 52
    • 0026338299 scopus 로고
    • Role of hemoglobin denaturation and band 3 clustering in initiating red cell removal
    • Magnani M, DeFlora A (eds): New York, NY, Plenum
    • Low PS: Role of hemoglobin denaturation and band 3 clustering in initiating red cell removal, in Magnani M, DeFlora A (eds): Red Blood Cell Aging. New York, NY, Plenum, 1991, p 173
    • (1991) Red Blood Cell Aging , pp. 173
    • Low, P.S.1
  • 53
    • 0018320527 scopus 로고
    • Measurement of immunoglobulin binding to synovial fibroblast monolayer: Comparison of staphylococcal protein A binding to cytotoxic assay methods
    • Gruhn WB, McDuffie FC: Measurement of immunoglobulin binding to synovial fibroblast monolayer: Comparison of staphylococcal protein A binding to cytotoxic assay methods. J Immunol Methods 29:227, 1979
    • (1979) J Immunol Methods , vol.29 , pp. 227
    • Gruhn, W.B.1    McDuffie, F.C.2
  • 55
    • 0026466977 scopus 로고
    • The critical role of asparagine 502 in post-translational alteration of protein 4.1
    • Inaba M, Maede Y: The critical role of asparagine 502 in post-translational alteration of protein 4.1. Comp Biochem Physiol 103B:523, 1992
    • (1992) Comp Biochem Physiol , vol.103 B , pp. 523
    • Inaba, M.1    Maede, Y.2
  • 56
    • 0023681418 scopus 로고
    • Correlation between protein 4.1a/4.1b ratio and erythrocyte life span
    • Inaba M, Maede Y: Correlation between protein 4.1a/4.1b ratio and erythrocyte life span. Biochim Biophys Acta 944:256, 1988
    • (1988) Biochim Biophys Acta , vol.944 , pp. 256
    • Inaba, M.1    Maede, Y.2
  • 57
    • 0021914417 scopus 로고
    • Hemichrome binding to band 3: Nucleation of heinz bodies on the erythrocyte membrane
    • Waugh SM, Low PS: Hemichrome binding to band 3: Nucleation of heinz bodies on the erythrocyte membrane. Biochemistry 24:34, 1985
    • (1985) Biochemistry , vol.24 , pp. 34
    • Waugh, S.M.1    Low, P.S.2
  • 58
    • 0022993811 scopus 로고
    • Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes
    • Waugh SM, Willardson BM, Kannan R, Labotka RJ, Low PS: Heinz bodies induce clustering of band 3, glycophorin, and ankyrin in sickle cell erythrocytes. J Clin Invest 78:1155, 1986
    • (1986) J Clin Invest , vol.78 , pp. 1155
    • Waugh, S.M.1    Willardson, B.M.2    Kannan, R.3    Labotka, R.J.4    Low, P.S.5
  • 59
    • 0023110167 scopus 로고
    • Partial characterization of the copolymerization reaction of erythrocyte membrane band 3 with hemichromes
    • Waugh SM, Walder JA, Low PS: Partial characterization of the copolymerization reaction of erythrocyte membrane band 3 with hemichromes. Biochemistry 26:1777, 1987
    • (1987) Biochemistry , vol.26 , pp. 1777
    • Waugh, S.M.1    Walder, J.A.2    Low, P.S.3
  • 61
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals: I. General aspects
    • Davies KJA: Protein damage and degradation by oxygen radicals: I. General aspects. J Biol Chem 262:9895, 1987
    • (1987) J Biol Chem , vol.262 , pp. 9895
    • Davies, K.J.A.1
  • 62
    • 0027414020 scopus 로고
    • Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19 S) proteasome
    • Giulivi C, Davies KJA: Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19 S) proteasome. J Biol Chem 268:8752, 1993
    • (1993) J Biol Chem , vol.268 , pp. 8752
    • Giulivi, C.1    Davies, K.J.A.2
  • 63
    • 0028796836 scopus 로고
    • Oxidation state of glulathione and membrane proteins in human red cells of different age
    • Piccinini G, Minetti G, Balduini C, Brovelli A: Oxidation state of glulathione and membrane proteins in human red cells of different age. Mech Aging Dev 78:15, 1995
    • (1995) Mech Aging Dev , vol.78 , pp. 15
    • Piccinini, G.1    Minetti, G.2    Balduini, C.3    Brovelli, A.4
  • 64
    • 0013787425 scopus 로고
    • Erythrocyte catalase and detoxication of hydrogen peroxide
    • Panicker NV, Iyer GYN: Erythrocyte catalase and detoxication of hydrogen peroxide. Can J Biochem 43:1029, 1965
    • (1965) Can J Biochem , vol.43 , pp. 1029
    • Panicker, N.V.1    Iyer, G.Y.N.2
  • 65
    • 0024418244 scopus 로고
    • The redox state of cysteines 201 and 317 of the erythrocyte anion exchanger is critical for ankyrin binding
    • Thevenin BJM, Willardson BM, Low PS: The redox state of cysteines 201 and 317 of the erythrocyte anion exchanger is critical for ankyrin binding. J Biol Chem 264:15886, 1989
    • (1989) J Biol Chem , vol.264 , pp. 15886
    • Thevenin, B.J.M.1    Willardson, B.M.2    Low, P.S.3
  • 67
    • 0026033290 scopus 로고
    • Effect of cell-bound proteins on the in vivo survival of circulating blood cells
    • Garratty G: Effect of cell-bound proteins on the in vivo survival of circulating blood cells. Gerontology 37:68, 1991
    • (1991) Gerontology , vol.37 , pp. 68
    • Garratty, G.1
  • 68
    • 0018568046 scopus 로고
    • Ionocyte-mediated destruction in the presence of serum of red cells coated with antibody
    • Kurlander RJ, Rosse WF: Ionocyte-mediated destruction in the presence of serum of red cells coated with antibody. Blood 14:1131, 1979
    • (1979) Blood , vol.14 , pp. 1131
    • Kurlander, R.J.1    Rosse, W.F.2
  • 69
    • 0023244778 scopus 로고
    • Phagocytosis of erythrocytes sensitized with known amounts of IgG1 and IgG3 anti-Rh antibodies
    • Zupanska B, Thompson E, Brojer E, Merry AH: Phagocytosis of erythrocytes sensitized with known amounts of IgG1 and IgG3 anti-Rh antibodies. Vox Sang 53:96, 1987
    • (1987) Vox Sang , vol.53 , pp. 96
    • Zupanska, B.1    Thompson, E.2    Brojer, E.3    Merry, A.H.4
  • 70
    • 0022346823 scopus 로고
    • Some quantitative aspects of the human monocyte erythrophagocytosis and rosette assays
    • Douglas R, Rowthorne NV, Schneider JV: Some quantitative aspects of the human monocyte erythrophagocytosis and rosette assays. Transfusion 25:535, 1985
    • (1985) Transfusion , vol.25 , pp. 535
    • Douglas, R.1    Rowthorne, N.V.2    Schneider, J.V.3
  • 71
    • 0018962991 scopus 로고
    • Clustered IgG on human red blood cell membranes may promote human lymphocyte antibody-dependent cell-mediated cytotoxicity
    • Shaw GM, Aminoff D, Balcerzak SP, LoBuglio AF: Clustered IgG on human red blood cell membranes may promote human lymphocyte antibody-dependent cell-mediated cytotoxicity. J Immunol 125:501, 1980
    • (1980) J Immunol , vol.125 , pp. 501
    • Shaw, G.M.1    Aminoff, D.2    Balcerzak, S.P.3    LoBuglio, A.F.4
  • 72
    • 0024551404 scopus 로고
    • Pathobiology of heme interaction with the erythrocyte membrane
    • Hebbel RP, Eaton JW: Pathobiology of heme interaction with the erythrocyte membrane. Semin Hematol 26:136, 1989
    • (1989) Semin Hematol , vol.26 , pp. 136
    • Hebbel, R.P.1    Eaton, J.W.2
  • 73
    • 0024600910 scopus 로고
    • Oxidative hemoglobin denaturation and RBC destruction: The effect of heme on red cell membranes
    • Chiu D, Lubin B: Oxidative hemoglobin denaturation and RBC destruction: The effect of heme on red cell membranes. Semin Hematol 26:128, 1989
    • (1989) Semin Hematol , vol.26 , pp. 128
    • Chiu, D.1    Lubin, B.2
  • 75
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides
    • Geiger T, Clarke S: Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. J Biol Chem 262:785, 1987
    • (1987) J Biol Chem , vol.262 , pp. 785
    • Geiger, T.1    Clarke, S.2
  • 76
    • 0016360069 scopus 로고
    • Deamidation of glutaminyl and asparaginyl residues in peptides and proteins
    • Robinson AB, Rudd CJ: Deamidation of glutaminyl and asparaginyl residues in peptides and proteins. Curr Top Cell Regul 8:247, 1974
    • (1974) Curr Top Cell Regul , vol.8 , pp. 247
    • Robinson, A.B.1    Rudd, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.