메뉴 건너뛰기




Volumn 246, Issue 8, 2013, Pages 591-607

Erratum: Identification of human erythrocyte cytosolic proteins associated with plasma membrane during thermal stress (The Journal of Membrane Biology DOI: 10.1007/s00232-013-9569-0);Identification of human erythrocyte cytosolic proteins associated with plasma membrane during thermal stress

Author keywords

Electrophoresis; Erythrocyte; Heat stress; Mass spectrometry; Membrane skeleton

Indexed keywords

ALPHA ENOLASE; CARBONATE DEHYDRATASE I; CARBONATE DEHYDRATASE II; CATALASE; CELL PROTEIN; CYTOSOLIC PROTEIN; FLAVIN REDUCTASE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90ALPHA; OXIDOREDUCTASE; PEPTIDYLPROLYL ISOMERASE; PEPTIDYLPROLYL ISOMERASE A; PEROXIREDOXIN 2; PEROXIREDOXIN 6; UNCLASSIFIED DRUG;

EID: 84881317697     PISSN: 00222631     EISSN: 14321424     Source Type: Journal    
DOI: 10.1007/s00232-013-9581-4     Document Type: Erratum
Times cited : (9)

References (39)
  • 1
    • 40649086619 scopus 로고    scopus 로고
    • Oxidative status of red blood cells, neutrophils, and platelets in paroxysmal nocturnal hemoglobinuria
    • 18261835 10.1016/j.exphem.2007.12.003 1:CAS:528:DC%2BD1cXjtl2lu7o%3D
    • Amer J, Zelig O, Fibach E (2008) Oxidative status of red blood cells, neutrophils, and platelets in paroxysmal nocturnal hemoglobinuria. Exp Hematol 36:369-377
    • (2008) Exp Hematol , vol.36 , pp. 369-377
    • Amer, J.1    Zelig, O.2    Fibach, E.3
  • 2
    • 0023008883 scopus 로고
    • The effect of mild diamide oxidation on the structure and function of human erythrocyte spectrin
    • 3957910 1:CAS:528:DyaL28XitVamtrY%3D
    • Becker PS, Cohen CM, Lux SE (1986) The effect of mild diamide oxidation on the structure and function of human erythrocyte spectrin. J Biol Chem 261:4620-4628
    • (1986) J Biol Chem , vol.261 , pp. 4620-4628
    • Becker, P.S.1    Cohen, C.M.2    Lux, S.E.3
  • 3
    • 0024990463 scopus 로고
    • Spectrin-based membrane skeleton: A multipotential adaptor between plasma membrane and cytoplasm
    • 2271059 1:CAS:528:DyaK3MXhs1Wmtr4%3D
    • Bennett V (1990) Spectrin-based membrane skeleton: a multipotential adaptor between plasma membrane and cytoplasm. Physiol Rev 70:1029-1065
    • (1990) Physiol Rev , vol.70 , pp. 1029-1065
    • Bennett, V.1
  • 4
    • 44649095166 scopus 로고    scopus 로고
    • Heat-shock protein-27, -70 and peroxiredoxin-II show molecular chaperone function in sickle red cells: Evidence from transgenic sickle cell mouse model
    • 21136868 10.1002/prca.200780058 1:CAS:528:DC%2BD1cXms1emtb0%3D
    • Biondani A, Franco T, Franco C, Alessandro M, Alida F, Angela S, Yves B, Lucia De F (2008) Heat-shock protein-27, -70 and peroxiredoxin-II show molecular chaperone function in sickle red cells: evidence from transgenic sickle cell mouse model. Proteomics Clin Appl 2:706-719
    • (2008) Proteomics Clin Appl , vol.2 , pp. 706-719
    • Biondani, A.1    Franco, T.2    Franco, C.3    Alessandro, M.4    Alida, F.5    Angela, S.6    Yves, B.7    De, L.F.8
  • 5
    • 0017411709 scopus 로고
    • Calorimetric studies of the structural transitions of the human erythrocyte membrane. The involvement of spectrin in the A transition
    • 889805 10.1021/bi00634a024 1:CAS:528:DyaE2sXkvVSis70%3D
    • Brandts JF, Erickson L, Lysko K, Schwartz AT, Taverna RD (1977) Calorimetric studies of the structural transitions of the human erythrocyte membrane. The involvement of spectrin in the A transition. Biochemistry 16:3450-3454
    • (1977) Biochemistry , vol.16 , pp. 3450-3454
    • Brandts, J.F.1    Erickson, L.2    Lysko, K.3    Schwartz, A.T.4    Taverna, R.D.5
  • 6
    • 0018744050 scopus 로고
    • Morphological changes, haemolysis and microvesicularization of heated human erythrocytes
    • 10.1016/0306-4565(79)90051-2 1:CAS:528:DyaE1MXitVWnu7o%3D
    • Coakley WT, Bater AJ, Crum LA, Deeley JO (1979) Morphological changes, haemolysis and microvesicularization of heated human erythrocytes. J Therm Biol 4:85-93
    • (1979) J Therm Biol , vol.4 , pp. 85-93
    • Coakley, W.T.1    Bater, A.J.2    Crum, L.A.3    Deeley, J.O.4
  • 7
    • 34548181867 scopus 로고    scopus 로고
    • Proteomic analysis of RBC membrane protein degradation during blood storage
    • 17585793 10.1021/pr070179d
    • D'Amici GM, Rinalducci S, Zolla L (2007) Proteomic analysis of RBC membrane protein degradation during blood storage. J Proteome Res 6:3242-3255
    • (2007) J Proteome Res , vol.6 , pp. 3242-3255
    • D'Amici, G.M.1    Rinalducci, S.2    Zolla, L.3
  • 8
    • 0034971472 scopus 로고    scopus 로고
    • Lipid peroxidation, osmotic fragility and antioxidant status in children with acute post-streptococcal glomerulonephritis
    • 11412828 10.1016/S0009-8981(01)00482-X 1:CAS:528:DC%2BD3MXksVyls7Y%3D
    • Devasena T, Lalitha S, Padma K (2001) Lipid peroxidation, osmotic fragility and antioxidant status in children with acute post-streptococcal glomerulonephritis. Clin Chim Acta 308:155-161
    • (2001) Clin Chim Acta , vol.308 , pp. 155-161
    • Devasena, T.1    Lalitha, S.2    Padma, K.3
  • 9
    • 0022366275 scopus 로고
    • Thermal denaturation of the erythrocyte cytoskeleton alters the morphological changes associated with osmotic swelling
    • 10.1016/0306-4565(85)90038-5
    • Eskelinen S, Coakley WT, Tilley D (1985) Thermal denaturation of the erythrocyte cytoskeleton alters the morphological changes associated with osmotic swelling. J Therm Biol 10:187-190
    • (1985) J Therm Biol , vol.10 , pp. 187-190
    • Eskelinen, S.1    Coakley, W.T.2    Tilley, D.3
  • 10
    • 36849061166 scopus 로고    scopus 로고
    • The human red blood cell proteome and interactome
    • 10.3181/0706-MR-156 1:CAS:528:DC%2BD2sXhsVahsbjP
    • Goodman SR, Kurdia A, Ammann L, Kakhniashvili D, Daescu O (2007) The human red blood cell proteome and interactome. Exp Biol Med 232:1391-1408
    • (2007) Exp Biol Med , vol.232 , pp. 1391-1408
    • Goodman, S.R.1    Kurdia, A.2    Ammann, L.3    Kakhniashvili, D.4    Daescu, O.5
  • 11
    • 0027493422 scopus 로고
    • Hsp 70-like protein in rhesus erythrocyte cytosol and its interactions with membrane skeleton under heat and pathologic stress
    • 8407973 1:CAS:528:DyaK3sXlsFOltr8%3D
    • Gudi T, Gupta CM (1993) Hsp 70-like protein in rhesus erythrocyte cytosol and its interactions with membrane skeleton under heat and pathologic stress. J Biol Chem 268:21344-21350
    • (1993) J Biol Chem , vol.268 , pp. 21344-21350
    • Gudi, T.1    Gupta, C.M.2
  • 12
    • 0025343440 scopus 로고
    • Membrane skeleton-bilayer interaction is not the major determinant of membrane phospholipid asymmetry in human erythrocytes
    • 2317498 10.1016/0005-2736(90)90010-L 1:CAS:528:DyaK3cXhvFGrt7g%3D
    • Gudi SRP, Kumar A, Bhakuni V, Gokhale SM, Gupta CM (1990) Membrane skeleton-bilayer interaction is not the major determinant of membrane phospholipid asymmetry in human erythrocytes. Biochim Biophys Acta 1023:63-72
    • (1990) Biochim Biophys Acta , vol.1023 , pp. 63-72
    • Gudi, S.R.P.1    Kumar, A.2    Bhakuni, V.3    Gokhale, S.M.4    Gupta, C.M.5
  • 13
    • 0022529172 scopus 로고
    • Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts
    • 3010861 10.1016/0003-9861(86)90305-X 1:CAS:528:DyaL28Xhs1Khsr4%3D
    • Halliwell B, Gutteridge JMC (1986) Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts. Arch Biochem Biophys 246:501-514
    • (1986) Arch Biochem Biophys , vol.246 , pp. 501-514
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 14
    • 0016355004 scopus 로고
    • The preparation of red cell ghosts (membranes)
    • 4278921 10.1016/0076-6879(74)31018-X 1:STN:280:DyaE2M%2FjtFekug%3D%3D
    • Hanahan DJ, Ekholm JE (1974) The preparation of red cell ghosts (membranes). Methods Enzymol 31:168-172
    • (1974) Methods Enzymol , vol.31 , pp. 168-172
    • Hanahan, D.J.1    Ekholm, J.E.2
  • 15
    • 0026071319 scopus 로고
    • 2O, glycerol, and anisotonic saline
    • 1986397 10.2307/3577977 1:CAS:528:DyaK3MXhsVSlt7g%3D
    • 2O, glycerol, and anisotonic saline. Radiat Res 125:20-27
    • (1991) Radiat Res , vol.125 , pp. 20-27
    • Ho, K.C.1    Lin, P.S.2
  • 16
    • 0018438765 scopus 로고
    • Temperature-related changes in the erythrocytic carbonic anhydrase (actazolamide-sensitive estrase) activity of goldfish, Carassius auratus
    • 108353 1:CAS:528:DyaE1MXhvVenu7Y%3D
    • Houston H, Mearow KM (1979) Temperature-related changes in the erythrocytic carbonic anhydrase (actazolamide-sensitive estrase) activity of goldfish, Carassius auratus. J Exp Biol 78:255-264
    • (1979) J Exp Biol , vol.78 , pp. 255-264
    • Houston, H.1    Mearow, K.M.2
  • 17
    • 0036910048 scopus 로고    scopus 로고
    • Blood pressure, hematologic and erythrocyte fragility changes in children suffering from sickle cell anemia following ascorbic acid supplementation
    • 12521281 10.1093/tropej/48.6.366 1:STN:280:DC%2BD3s%2FhsVygsA%3D%3D
    • Jaja SI, Ikotum AR, Gbenebitse S, Temiye EO (2002) Blood pressure, hematologic and erythrocyte fragility changes in children suffering from sickle cell anemia following ascorbic acid supplementation. J Trop Pediatr 48:366-370
    • (2002) J Trop Pediatr , vol.48 , pp. 366-370
    • Jaja, S.I.1    Ikotum, A.R.2    Gbenebitse, S.3    Temiye, E.O.4
  • 18
    • 0026035970 scopus 로고
    • The response of pig erythrocytes to thermal stress
    • 1671697 10.1080/09553009114550431 1:STN:280:DyaK3M7ktVWitQ%3D%3D
    • Jozwiak Z, Palecz D, Leyko W (1991) The response of pig erythrocytes to thermal stress. Int J Radiat Biol 59:479-487
    • (1991) Int J Radiat Biol , vol.59 , pp. 479-487
    • Jozwiak, Z.1    Palecz, D.2    Leyko, W.3
  • 19
    • 2642551423 scopus 로고    scopus 로고
    • The human erythrocyte proteome: Analysis by ion trap mass spectrometry
    • 14963112 10.1074/mcp.M300132-MCP200 1:CAS:528:DC%2BD2cXktFChsLs%3D
    • Kakhniashvili DG, Bulla LA Jr, Goodman SR (2004) The human erythrocyte proteome: analysis by ion trap mass spectrometry. Mol Cell Proteomics 3:501-509
    • (2004) Mol Cell Proteomics , vol.3 , pp. 501-509
    • Kakhniashvili, D.G.1    Bulla, Jr.L.A.2    Goodman, S.R.3
  • 21
    • 33947328401 scopus 로고    scopus 로고
    • Progressive oxidation of cytoskeletal proteins and accumulation of denatured hemoglobin in stored red cells
    • 17367509 10.1111/j.1582-4934.2007.00008.x 1:CAS:528:DC%2BD2sXlvFCltrY%3D
    • Kriebardis AG, Antonelou MH, Stamoulis KS, Economou-Petersen E, Margaritis LH, Papassideri IS (2007) Progressive oxidation of cytoskeletal proteins and accumulation of denatured hemoglobin in stored red cells. J Cell Mol Med 11:148-155
    • (2007) J Cell Mol Med , vol.11 , pp. 148-155
    • Kriebardis, A.G.1    Antonelou, M.H.2    Stamoulis, K.S.3    Economou-Petersen, E.4    Margaritis, L.H.5    Papassideri, I.S.6
  • 22
    • 0025204710 scopus 로고
    • Heat-induced alterations in monkey erythrocyte membrane phospholipid organization and skeletal protein structure and interactions
    • 2261489 10.1016/0005-2736(90)90303-6 1:CAS:528:DyaK3MXlvFKjsw%3D%3D
    • Kumar A, Gudi SR, Gokhale SM, Bhakuni V, Gupta CM (1990) Heat-induced alterations in monkey erythrocyte membrane phospholipid organization and skeletal protein structure and interactions. Biochim Biophys Acta 1030:269-278
    • (1990) Biochim Biophys Acta , vol.1030 , pp. 269-278
    • Kumar, A.1    Gudi, S.R.2    Gokhale, S.M.3    Bhakuni, V.4    Gupta, C.M.5
  • 23
    • 0014949207 scopus 로고
    • 4
    • 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • 4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0024968834 scopus 로고
    • Relationship of hyperthermia-induced hemolysis of human erythrocytes to the thermal denaturation of membrane proteins
    • Lepock JR, Frey HE, Bayne H, Markus J (1989) Relationship of hyperthermia-induced hemolysis of human erythrocytes to the thermal denaturation of membrane proteins. Biochim Biophys Acta 14:191-201
    • (1989) Biochim Biophys Acta , vol.14 , pp. 191-201
    • Lepock, J.R.1    Frey, H.E.2    Bayne, H.3    Markus, J.4
  • 25
    • 0030797220 scopus 로고    scopus 로고
    • Protein thiol modifications of human red blood cells treated with t-butyl hydroperoxide
    • 9305784 10.1016/S0304-4165(97)00020-2 1:CAS:528:DyaK2sXks12hs7c%3D
    • Lii CK, Hung CN (1997) Protein thiol modifications of human red blood cells treated with t-butyl hydroperoxide. Biochim Biophys Acta 1336:147-156
    • (1997) Biochim Biophys Acta , vol.1336 , pp. 147-156
    • Lii, C.K.1    Hung, C.N.2
  • 26
    • 71849104860 scopus 로고
    • Protein measurement with the Folin-phenol reagent
    • 14907713 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin-phenol reagent. J Biol Chem 193:265-275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 27
    • 0019843898 scopus 로고
    • Protein involvement in structural transitions of erythrocyte ghosts. Use of thermal gel analysis to detect protein aggregation
    • 7295694 10.1021/bi00522a034 1:CAS:528:DyaL3MXlt1Ort78%3D
    • Lysko KA, Carlson R, Taverna R, Snow J, Brandts JF (1981) Protein involvement in structural transitions of erythrocyte ghosts. Use of thermal gel analysis to detect protein aggregation. Biochemistry 20:5570-5576
    • (1981) Biochemistry , vol.20 , pp. 5570-5576
    • Lysko, K.A.1    Carlson, R.2    Taverna, R.3    Snow, J.4    Brandts, J.F.5
  • 28
    • 0022588386 scopus 로고
    • Spectrin involvement in a 40 C structural transition of the red blood cell membrane
    • 3711154 10.1002/jcb.240300409 1:CAS:528:DyaL28Xit1Wjur8%3D
    • Minetti M, Ceccarini M, Distasi AMM, Petrucci TC, Marchesi VT (1986) Spectrin involvement in a 40 C structural transition of the red blood cell membrane. J Cell Biochem 30:361-370
    • (1986) J Cell Biochem , vol.30 , pp. 361-370
    • Minetti, M.1    Ceccarini, M.2    Distasi, A.M.M.3    Petrucci, T.C.4    Marchesi, V.T.5
  • 29
    • 58149158216 scopus 로고    scopus 로고
    • Red cell membrane: Past, present, and future
    • 18988878 10.1182/blood-2008-07-161166 1:CAS:528:DC%2BD1cXhsVSmsrzP
    • Mohandas N, Gallagher PG (2008) Red cell membrane: past, present, and future. Blood 112:3939-3948
    • (2008) Blood , vol.112 , pp. 3939-3948
    • Mohandas, N.1    Gallagher, P.G.2
  • 30
    • 16744363275 scopus 로고    scopus 로고
    • Age-related changes of antioxidant enzyme activities, glutathione status and lipid peroxidation in rat erythrocytes after heat stress
    • 15261761 10.1016/j.lfs.2004.03.020 1:CAS:528:DC%2BD2cXlsl2mtrs%3D
    • Ozturk O, Gumuslu S (2004) Age-related changes of antioxidant enzyme activities, glutathione status and lipid peroxidation in rat erythrocytes after heat stress. Life Sci 75:1551-1565
    • (2004) Life Sci , vol.75 , pp. 1551-1565
    • Ozturk, O.1    Gumuslu, S.2
  • 31
    • 33746616420 scopus 로고    scopus 로고
    • In-depth analysis of the membrane and cytosolic proteome of red blood cells
    • 16861337 10.1182/blood-2005-11-007799 1:CAS:528:DC%2BD28XnvFajtr0%3D
    • Pasini EM, Kirkegaard M, Mortensen P, Lutz HU (2006) In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 108:791-801
    • (2006) Blood , vol.108 , pp. 791-801
    • Pasini, E.M.1    Kirkegaard, M.2    Mortensen, P.3    Lutz, H.U.4
  • 33
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • 8779443 10.1021/ac950914h 1:CAS:528:DyaK28XntlygtA%3D%3D
    • Shevchenko A, Wilm M, Vorm O, Mann M (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal Chem 68:850-858
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 34
    • 0021047024 scopus 로고
    • Sulfhydryl reagents induce altered spectrin self-association, skeletal instability and increased thermal sensitivity of red cells
    • 6640108 1:CAS:528:DyaL2cXkvFahtQ%3D%3D
    • Smith DK, Palek J (1983) Sulfhydryl reagents induce altered spectrin self-association, skeletal instability and increased thermal sensitivity of red cells. Blood 62:1190-1196
    • (1983) Blood , vol.62 , pp. 1190-1196
    • Smith, D.K.1    Palek, J.2
  • 35
    • 0023740149 scopus 로고
    • Direct involvement of spectrin thiols in maintaining erythrocyte membrane thermal stability and spectrin dimer self-association
    • 3395616 10.1016/0005-2736(88)90035-1 1:CAS:528:DyaL1cXkvFSgsL8%3D
    • Streichman S, Hertz E, Tatarsky I (1988) Direct involvement of spectrin thiols in maintaining erythrocyte membrane thermal stability and spectrin dimer self-association. Biochim Biophys Acta 942:333-340
    • (1988) Biochim Biophys Acta , vol.942 , pp. 333-340
    • Streichman, S.1    Hertz, E.2    Tatarsky, I.3
  • 36
    • 0026446364 scopus 로고
    • Effects of heat on fragility and morphology of human and calf erythrocytes
    • 1472484 10.3109/08941939209012448 1:STN:280:DyaK3s7ht1GrtA%3D%3D
    • Utoh J, Zajkowski B, Joy E, Harasaki H (1992) Effects of heat on fragility and morphology of human and calf erythrocytes. J Invest Surg 5:305-313
    • (1992) J Invest Surg , vol.5 , pp. 305-313
    • Utoh, J.1    Zajkowski, B.2    Joy, E.3    Harasaki, H.4
  • 37
    • 1942533521 scopus 로고    scopus 로고
    • T-complex polypeptide-1 interacts with the erythrocyte cytoskeleton in response to elevated temperatures
    • 14729905 10.1074/jbc.M310730200 1:CAS:528:DC%2BD2cXivF2qsbo%3D
    • Wagner CT, Lu IY, Hoffman MH, Sun WQ, Trent JD, Connor J (2004) T-complex polypeptide-1 interacts with the erythrocyte cytoskeleton in response to elevated temperatures. J Biol Chem 279:16223-16228
    • (2004) J Biol Chem , vol.279 , pp. 16223-16228
    • Wagner, C.T.1    Lu, I.Y.2    Hoffman, M.H.3    Sun, W.Q.4    Trent, J.D.5    Connor, J.6
  • 38
    • 0021279404 scopus 로고
    • Isolation of spectrin subunits and reassociation in vitro. Analysis by fluorescence polarization
    • 6707015 1:CAS:528:DyaL2cXhslShtbY%3D
    • Yoshino H, Marchesi VT (1984) Isolation of spectrin subunits and reassociation in vitro. Analysis by fluorescence polarization. J Biol Chem 259:4496-4500
    • (1984) J Biol Chem , vol.259 , pp. 4496-4500
    • Yoshino, H.1    Marchesi, V.T.2
  • 39
    • 0023475239 scopus 로고
    • Heat induced dissociation of human erythrocyte spectrin dimer into monomers
    • 3676303 10.1016/0005-2736(87)90013-7 1:CAS:528:DyaL1cXovF2gtw%3D%3D
    • Yoshino H, Minari O (1987) Heat induced dissociation of human erythrocyte spectrin dimer into monomers. Biochim Biophys Acta 905:100-108
    • (1987) Biochim Biophys Acta , vol.905 , pp. 100-108
    • Yoshino, H.1    Minari, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.