메뉴 건너뛰기




Volumn 73, Issue 3, 2010, Pages 396-402

Comparative proteomics of erythrocyte aging in vivo and in vitro

Author keywords

Aging; Erythrocyte; Membrane; Storage; Vesicles

Indexed keywords

CHAPERONE; ERYTHROCYTE BAND 3 PROTEIN; HEAT SHOCK PROTEIN; HEMOGLOBIN; PHOSPHATIDYLSERINE; PROTEASOME; SCAVENGER RECEPTOR;

EID: 72149086124     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2009.07.010     Document Type: Review
Times cited : (83)

References (54)
  • 1
    • 58149095080 scopus 로고    scopus 로고
    • Erythrocyte aging in vivo and in vitro: structural aspects and implications for transfusion
    • Bosman G.J.C.G.M., Werre J.M., Willekens F.L.A., and Novotný V.M.J. Erythrocyte aging in vivo and in vitro: structural aspects and implications for transfusion. Transfus Med 18 (2008) 1-13
    • (2008) Transfus Med , vol.18 , pp. 1-13
    • Bosman, G.J.C.G.M.1    Werre, J.M.2    Willekens, F.L.A.3    Novotný, V.M.J.4
  • 2
    • 59249098866 scopus 로고    scopus 로고
    • Red cell membrane lipids in hemoglobinopathies
    • Kuypers F.A. Red cell membrane lipids in hemoglobinopathies. Curr Mol Med 8 (2008) 633-638
    • (2008) Curr Mol Med , vol.8 , pp. 633-638
    • Kuypers, F.A.1
  • 4
    • 47749112789 scopus 로고    scopus 로고
    • A role of phosphatidylserine externalization in clearance of erythrocytes exposed to stress but not in eliminating aging populations of erythrocytes in mice
    • Khandelwal S., and Saxena R.K. A role of phosphatidylserine externalization in clearance of erythrocytes exposed to stress but not in eliminating aging populations of erythrocytes in mice. Exp Gerontol 43 (2008) 764-770
    • (2008) Exp Gerontol , vol.43 , pp. 764-770
    • Khandelwal, S.1    Saxena, R.K.2
  • 7
    • 0021969804 scopus 로고
    • The role of hemoglobin denaturation and band 3 clustering in red blood cell aging
    • Low P.S., Waugh S.M., Zinke K., and Drenckhahn D. The role of hemoglobin denaturation and band 3 clustering in red blood cell aging. Science 227 (1985) 531-533
    • (1985) Science , vol.227 , pp. 531-533
    • Low, P.S.1    Waugh, S.M.2    Zinke, K.3    Drenckhahn, D.4
  • 8
    • 32244435726 scopus 로고    scopus 로고
    • Immunoregulation of cellular life span
    • Kay M.M.B. Immunoregulation of cellular life span. Ann NY Acad Sci 1057 (2005) 85-111
    • (2005) Ann NY Acad Sci , vol.1057 , pp. 85-111
    • Kay, M.M.B.1
  • 9
    • 0023720213 scopus 로고
    • Erythrocyte aging: a comparison of model systems for simulating cellular aging in vitro
    • Bosman G.J.C.G.M., and Kay M.M.B. Erythrocyte aging: a comparison of model systems for simulating cellular aging in vitro. Blood Cells 14 (1988) 19-35
    • (1988) Blood Cells , vol.14 , pp. 19-35
    • Bosman, G.J.C.G.M.1    Kay, M.M.B.2
  • 10
  • 11
    • 44849127632 scopus 로고    scopus 로고
    • Prolonged maintenance of 2,3-diphosphoglycerate acid and adenosine triphosphate in red blood cells during storage
    • De Korte D., Kleine M., Korsten H.G., and Verhoeven A.J. Prolonged maintenance of 2,3-diphosphoglycerate acid and adenosine triphosphate in red blood cells during storage. Transfusion 48 (2008) 1081-1089
    • (2008) Transfusion , vol.48 , pp. 1081-1089
    • De Korte, D.1    Kleine, M.2    Korsten, H.G.3    Verhoeven, A.J.4
  • 12
    • 52049121547 scopus 로고    scopus 로고
    • Survival of red blood cells after transfusion: a comparison between red cell concentrates of different storage periods
    • Luten M., Roerdinkholder-Stoelwinder B., Schaap N.P.M., De Grip W.J., Bos H.J., and Bosman G.J.C.G.M. Survival of red blood cells after transfusion: a comparison between red cell concentrates of different storage periods. Transfusion 48 (2008) 1478-1485
    • (2008) Transfusion , vol.48 , pp. 1478-1485
    • Luten, M.1    Roerdinkholder-Stoelwinder, B.2    Schaap, N.P.M.3    De Grip, W.J.4    Bos, H.J.5    Bosman, G.J.C.G.M.6
  • 15
    • 33746616420 scopus 로고    scopus 로고
    • In-depth analysis of the membrane and cytosolic proteome of red blood cells
    • Pasini E.M., Kirkegaard M., Mortensen P., Lutz H.U., Thomas A., and Mann M. In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 108 (2006) 791-801
    • (2006) Blood , vol.108 , pp. 791-801
    • Pasini, E.M.1    Kirkegaard, M.2    Mortensen, P.3    Lutz, H.U.4    Thomas, A.5    Mann, M.6
  • 16
    • 33644838780 scopus 로고    scopus 로고
    • The how and why of exocytic vesicles
    • Greenwalt T.J. The how and why of exocytic vesicles. Transfusion 46 (2006) 143-152
    • (2006) Transfusion , vol.46 , pp. 143-152
    • Greenwalt, T.J.1
  • 18
    • 5144228243 scopus 로고    scopus 로고
    • Erythrocyte aging in sickle cell disease
    • Bosman G.J.C.G.M. Erythrocyte aging in sickle cell disease. Cell Mol Biol 50 (2004) 81-86
    • (2004) Cell Mol Biol , vol.50 , pp. 81-86
    • Bosman, G.J.C.G.M.1
  • 19
    • 30644465690 scopus 로고    scopus 로고
    • Storage-related changes in erythrocyte band 3: not a case for the Diego blood group antigens
    • Bosman G.J.C.G.M., Klaarenbeek J.M., Luten M., and Bos H.J. Storage-related changes in erythrocyte band 3: not a case for the Diego blood group antigens. Cell Mol Biol 51 (2005) 195-200
    • (2005) Cell Mol Biol , vol.51 , pp. 195-200
    • Bosman, G.J.C.G.M.1    Klaarenbeek, J.M.2    Luten, M.3    Bos, H.J.4
  • 20
    • 34250675997 scopus 로고    scopus 로고
    • Storage-dependent remodeling of the red blood cell membrane is associated with increased immunoglobulin G binding, lipid raft rearrangement, and caspase activation
    • Kriebardis A.G., Antonelou M.H., Stamoulis K.E., Economou-Petersen E., Margaritis L.H., and Papassideri I.S. Storage-dependent remodeling of the red blood cell membrane is associated with increased immunoglobulin G binding, lipid raft rearrangement, and caspase activation. Transfusion 47 (2007) 1212-1220
    • (2007) Transfusion , vol.47 , pp. 1212-1220
    • Kriebardis, A.G.1    Antonelou, M.H.2    Stamoulis, K.E.3    Economou-Petersen, E.4    Margaritis, L.H.5    Papassideri, I.S.6
  • 21
    • 0030276770 scopus 로고    scopus 로고
    • Implications of aging- and degeneration-related changes in anion exchange proteins for the maintenance of neuronal homeostasis
    • Bosman G.J.C.G.M., Engbersen A., Vollaard C.H., Bartholomeus I.G., Pistorius A.M., Renkawek K., et al. Implications of aging- and degeneration-related changes in anion exchange proteins for the maintenance of neuronal homeostasis. Cell Mol Biol 42 (1996) 905-918
    • (1996) Cell Mol Biol , vol.42 , pp. 905-918
    • Bosman, G.J.C.G.M.1    Engbersen, A.2    Vollaard, C.H.3    Bartholomeus, I.G.4    Pistorius, A.M.5    Renkawek, K.6
  • 22
    • 0023234284 scopus 로고
    • Spectrin oxidation correlates with membrane vesiculation in stored RBCs
    • Wagner G.M., Chiu D.T., Qju J.H., Heath R.H., and Lubin B.H. Spectrin oxidation correlates with membrane vesiculation in stored RBCs. Blood 69 (1987) 1777-1781
    • (1987) Blood , vol.69 , pp. 1777-1781
    • Wagner, G.M.1    Chiu, D.T.2    Qju, J.H.3    Heath, R.H.4    Lubin, B.H.5
  • 25
    • 28844493639 scopus 로고    scopus 로고
    • The N-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function
    • Perrotta S., Borriello A., and Scaloni A. The N-terminal 11 amino acids of human erythrocyte band 3 are critical for aldolase binding and protein phosphorylation: implications for band 3 function. Blood 106 (2005) 4359-4366
    • (2005) Blood , vol.106 , pp. 4359-4366
    • Perrotta, S.1    Borriello, A.2    Scaloni, A.3
  • 26
    • 0037929812 scopus 로고    scopus 로고
    • Molecular and cellullar mechanisms of erythrocyte programmed cell death: impact on blood transfusion
    • Bratosin D., Estaquier J., Ameisen J.C., and Montreuil J. Molecular and cellullar mechanisms of erythrocyte programmed cell death: impact on blood transfusion. Vox Sang 83 (2002) 307-310
    • (2002) Vox Sang , vol.83 , pp. 307-310
    • Bratosin, D.1    Estaquier, J.2    Ameisen, J.C.3    Montreuil, J.4
  • 28
    • 55549129951 scopus 로고    scopus 로고
    • Erythrocyte-derived ectosomes have immunosuppressive properties
    • Sadallah S., Eken C., and Schifferli J.A. Erythrocyte-derived ectosomes have immunosuppressive properties. J Leukoc Biol 84 (2008) 1316-1325
    • (2008) J Leukoc Biol , vol.84 , pp. 1316-1325
    • Sadallah, S.1    Eken, C.2    Schifferli, J.A.3
  • 29
    • 68849102601 scopus 로고    scopus 로고
    • Erythrocyte-derived microvesicles may transfer phosphatidylserine to the surface of nucleated cells and falsely "mark" them as apoptotic
    • R. Liu, I. Klich, J. Ratajczak, M.Z. Ratajczak, E.K. Zuba-Surma, Erythrocyte-derived microvesicles may transfer phosphatidylserine to the surface of nucleated cells and falsely "mark" them as apoptotic. Eur. J. Haematol. 2009;83:220-9.
    • (2009) Eur. J. Haematol , vol.83 , pp. 220-229
    • Liu, R.1    Klich, I.2    Ratajczak, J.3    Ratajczak, M.Z.4    Zuba-Surma, E.K.5
  • 31
    • 33846383092 scopus 로고    scopus 로고
    • Force balance and membrane shedding at the red-blood-cell surface
    • Sens P., and Gov N. Force balance and membrane shedding at the red-blood-cell surface. Phys Rev Lett 98 (2007) 018102
    • (2007) Phys Rev Lett , vol.98 , pp. 018102
    • Sens, P.1    Gov, N.2
  • 32
    • 33846552346 scopus 로고    scopus 로고
    • Active elastic network: cytoskeleton of the red blood cell
    • Gov N.S. Active elastic network: cytoskeleton of the red blood cell. Phys Rev. E 75 (2007) 011921
    • (2007) Phys Rev. E , vol.75 , pp. 011921
    • Gov, N.S.1
  • 33
    • 39749155230 scopus 로고    scopus 로고
    • Vesicles generated during storage of red cell concentrates are rich in the lipid raft marker stomatin
    • Salzer U., Zhu R., Luten M., Isobe H., Pastushenko V., Perkmann T., et al. Vesicles generated during storage of red cell concentrates are rich in the lipid raft marker stomatin. Transfusion 48 (2008) 451-462
    • (2008) Transfusion , vol.48 , pp. 451-462
    • Salzer, U.1    Zhu, R.2    Luten, M.3    Isobe, H.4    Pastushenko, V.5    Perkmann, T.6
  • 35
    • 53849106127 scopus 로고    scopus 로고
    • Microparticles in stored red blood cells: an approach using flow cytometry and proteomic tools
    • Rubin O., Crettaz D., Canellini G., Tissot J.D., and Lion N. Microparticles in stored red blood cells: an approach using flow cytometry and proteomic tools. Vox Sang 95 (2008) 288-297
    • (2008) Vox Sang , vol.95 , pp. 288-297
    • Rubin, O.1    Crettaz, D.2    Canellini, G.3    Tissot, J.D.4    Lion, N.5
  • 36
    • 33748344923 scopus 로고    scopus 로고
    • Prolonged storage of red blood cells affects aminophospholipid translocase activity
    • Verhoeven A.J., Hilarius P.M., Dekkers D.W., Lagerberg J.W., and De Korte D. Prolonged storage of red blood cells affects aminophospholipid translocase activity. Vox Sang 91 (2006) 244-251
    • (2006) Vox Sang , vol.91 , pp. 244-251
    • Verhoeven, A.J.1    Hilarius, P.M.2    Dekkers, D.W.3    Lagerberg, J.W.4    De Korte, D.5
  • 37
    • 0030058569 scopus 로고    scopus 로고
    • Improved red blood cell preservation correlates with decreased loss of bands 3, 4.1, acetylcholinesterase, and lipids in microvesicles
    • Dumaswala U.J., Dumaswala R.U., Levin D.S., and Greenwalt T.J. Improved red blood cell preservation correlates with decreased loss of bands 3, 4.1, acetylcholinesterase, and lipids in microvesicles. Blood 87 (1996) 1612-1616
    • (1996) Blood , vol.87 , pp. 1612-1616
    • Dumaswala, U.J.1    Dumaswala, R.U.2    Levin, D.S.3    Greenwalt, T.J.4
  • 39
    • 0043198426 scopus 로고    scopus 로고
    • Proteomic tools for quantitation by mass spectrometry
    • Lill J. Proteomic tools for quantitation by mass spectrometry. Mass Spectrom Rev 22 (2003) 182-194
    • (2003) Mass Spectrom Rev , vol.22 , pp. 182-194
    • Lill, J.1
  • 40
    • 38649095599 scopus 로고    scopus 로고
    • An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data
    • Mueller L.N., Brusniak M.Y., Mani D.R., and Aebersold R. An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data. J Proteome Res 7 (2008) 51-61
    • (2008) J Proteome Res , vol.7 , pp. 51-61
    • Mueller, L.N.1    Brusniak, M.Y.2    Mani, D.R.3    Aebersold, R.4
  • 41
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong S.E., and Mann M. Mass spectrometry-based proteomics turns quantitative. Nat Chem Biol 1 (2005) 252-262
    • (2005) Nat Chem Biol , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 42
    • 44049105535 scopus 로고    scopus 로고
    • Experimental and computational approaches to quantitative proteomics: status quo and outlook
    • Panchaud A., Affolter M., Moreillon P., and Kussmann M. Experimental and computational approaches to quantitative proteomics: status quo and outlook. J Proteomics 71 (2008) 19-33
    • (2008) J Proteomics , vol.71 , pp. 19-33
    • Panchaud, A.1    Affolter, M.2    Moreillon, P.3    Kussmann, M.4
  • 43
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishimima Y., Oda Y., Tabata T., Sato T., Nagasu T., Rappsilber J., et al. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 4 (2005) 1265-1272
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishimima, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6
  • 46
    • 34547156610 scopus 로고    scopus 로고
    • A platform for accurate mass and time analyses of mass spectrometry data
    • May D., Fitzgibbon M., Liu Y., Holzman T., and Eng J. A platform for accurate mass and time analyses of mass spectrometry data. J Proteome Res 6 (2007) 2685-2694
    • (2007) J Proteome Res , vol.6 , pp. 2685-2694
    • May, D.1    Fitzgibbon, M.2    Liu, Y.3    Holzman, T.4    Eng, J.5
  • 48
    • 0042887140 scopus 로고    scopus 로고
    • Proteome analyses using accurate mass and elution time peptide tags with capillary LC time-of-flight mass spectrometry
    • Strittmatter E.F., Ferguson P.L., Tang K., and Smith R.D. Proteome analyses using accurate mass and elution time peptide tags with capillary LC time-of-flight mass spectrometry. J Am Soc Mass Spectrom 14 (2003) 980-991
    • (2003) J Am Soc Mass Spectrom , vol.14 , pp. 980-991
    • Strittmatter, E.F.1    Ferguson, P.L.2    Tang, K.3    Smith, R.D.4
  • 49
    • 66749114309 scopus 로고    scopus 로고
    • (18)O(2)-labeling in quantitative proteomic strategies: a status report
    • Fenselau C., and Yao X. (18)O(2)-labeling in quantitative proteomic strategies: a status report. J Proteome Res 8 (2009) 2140-2143
    • (2009) J Proteome Res , vol.8 , pp. 2140-2143
    • Fenselau, C.1    Yao, X.2
  • 51
    • 66749156510 scopus 로고    scopus 로고
    • A simple procedure for effective quenching of trypsin activity and prevention of 18O-labeling back-exchange
    • Petritis B, Qian WJ, Camp D, Smith R. A simple procedure for effective quenching of trypsin activity and prevention of 18O-labeling back-exchange. J Proteome Res. 2009;8:2157-63.
    • (2009) J Proteome Res , vol.8 , pp. 2157-2163
    • Petritis, B.1    Qian, W.J.2    Camp, D.3    Smith, R.4
  • 52
    • 81555215409 scopus 로고    scopus 로고
    • Neuroacanthocytosis-related changes in erythrocyte membrane organization and function
    • Walker R.H., Saki S., and Danek A. (Eds), Springer Verlag
    • Bosman G.J.C.G.M., and De Franceschi L. Neuroacanthocytosis-related changes in erythrocyte membrane organization and function. In: Walker R.H., Saki S., and Danek A. (Eds). Neuroacanthocytosis II (2008), Springer Verlag 133-142
    • (2008) Neuroacanthocytosis II , pp. 133-142
    • Bosman, G.J.C.G.M.1    De Franceschi, L.2
  • 53
    • 43149086780 scopus 로고    scopus 로고
    • Extensive analysis of the cytoplasmic proteome of human erythrocytes using the peptide ligand library technology and advanced mass spectrometry
    • Roux-Dalvai F., Gonzalez de Peredo A., Simó C., Guerrier L., Bouyssié D., Zanella A., et al. Extensive analysis of the cytoplasmic proteome of human erythrocytes using the peptide ligand library technology and advanced mass spectrometry. Mol Cell Proteomics 7 (2008) 2254-2269
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2254-2269
    • Roux-Dalvai, F.1    Gonzalez de Peredo, A.2    Simó, C.3    Guerrier, L.4    Bouyssié, D.5    Zanella, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.