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Volumn 45, Issue 1, 2010, Pages 41-45

Altered phosphorylation of cytoskeleton proteins in sickle red blood cells: The role of protein kinase C, Rac GTPases, and reactive oxygen species

Author keywords

Cytoskeleton phosphorylation; Protein kinase C; Rac GTPases; Reactive oxygen species; Sickle cell disease

Indexed keywords

CYTOSKELETON PROTEIN; PROTEIN KINASE C; RAC PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

EID: 77953139384     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcmd.2010.02.006     Document Type: Article
Times cited : (54)

References (60)
  • 1
    • 0035097063 scopus 로고    scopus 로고
    • Pleiotropic and epistatic effects in sickle cell anemia
    • Nagel R.L. Pleiotropic and epistatic effects in sickle cell anemia. Curr. Opin. Hematol. 2001, 8:105-110.
    • (2001) Curr. Opin. Hematol. , vol.8 , pp. 105-110
    • Nagel, R.L.1
  • 2
    • 0033837987 scopus 로고    scopus 로고
    • Sickle cell anemia as an inflammatory disease
    • Platt O.S. Sickle cell anemia as an inflammatory disease. J. Clin. Invest. 2000, 106:337-338.
    • (2000) J. Clin. Invest. , vol.106 , pp. 337-338
    • Platt, O.S.1
  • 3
    • 41349090417 scopus 로고    scopus 로고
    • Hydroxyurea for children with sickle cell disease
    • x
    • Heeney M.M., Ware R.E. Hydroxyurea for children with sickle cell disease. Pediatr. Clin. North Am. 2008, 55:483-501. x.
    • (2008) Pediatr. Clin. North Am. , vol.55 , pp. 483-501
    • Heeney, M.M.1    Ware, R.E.2
  • 4
    • 10244242639 scopus 로고    scopus 로고
    • Sickle red cell microrheology and sickle blood rheology
    • Ballas S.K., Mohandas N. Sickle red cell microrheology and sickle blood rheology. Microcirculation 2004, 11:209-225.
    • (2004) Microcirculation , vol.11 , pp. 209-225
    • Ballas, S.K.1    Mohandas, N.2
  • 6
    • 0022972413 scopus 로고
    • Protein kinase C phosphorylates a recently identified membrane skeleton-associated calmodulin-binding protein in human erythrocytes
    • Ling E., Gardner K., Bennett V. Protein kinase C phosphorylates a recently identified membrane skeleton-associated calmodulin-binding protein in human erythrocytes. J. Biol. Chem. 1986, 261:13875-13878.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13875-13878
    • Ling, E.1    Gardner, K.2    Bennett, V.3
  • 7
    • 0025306103 scopus 로고
    • Identification and protein kinase C-dependent phosphorylation of alpha-adducin in human fibroblasts
    • Waseem A., Palfrey H.C. Identification and protein kinase C-dependent phosphorylation of alpha-adducin in human fibroblasts. J. Cell Sci. 1990, 96(Pt 1):93-98.
    • (1990) J. Cell Sci. , vol.96 , Issue.PART 1 , pp. 93-98
    • Waseem, A.1    Palfrey, H.C.2
  • 8
    • 0032572559 scopus 로고    scopus 로고
    • Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons
    • Matsuoka Y., Li X., Bennett V. Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons. J. Cell Biol. 1998, 142:485-497.
    • (1998) J. Cell Biol. , vol.142 , pp. 485-497
    • Matsuoka, Y.1    Li, X.2    Bennett, V.3
  • 10
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • Larsson C. Protein kinase C and the regulation of the actin cytoskeleton. Cell. Signal. 2006, 18:276-284.
    • (2006) Cell. Signal. , vol.18 , pp. 276-284
    • Larsson, C.1
  • 11
    • 33645285957 scopus 로고    scopus 로고
    • Regulation of NADPH oxidases: the role of Rac proteins
    • Hordijk P.L. Regulation of NADPH oxidases: the role of Rac proteins. Circ. Res. 2006, 98:453-462.
    • (2006) Circ. Res. , vol.98 , pp. 453-462
    • Hordijk, P.L.1
  • 12
    • 58149158216 scopus 로고    scopus 로고
    • Red cell membrane: past, present, and future
    • Mohandas N., Gallagher P.G. Red cell membrane: past, present, and future. Blood 2008, 112:3939-3948.
    • (2008) Blood , vol.112 , pp. 3939-3948
    • Mohandas, N.1    Gallagher, P.G.2
  • 13
    • 0033929093 scopus 로고    scopus 로고
    • Adducin: structure, function and regulation
    • Matsuoka Y., Li X., Bennett V. Adducin: structure, function and regulation. Cell. Mol. Life Sci. 2000, 57:884-895.
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 884-895
    • Matsuoka, Y.1    Li, X.2    Bennett, V.3
  • 14
    • 0030021105 scopus 로고    scopus 로고
    • Regulation of actin filament length in erythrocytes and striated muscle
    • Fowler V.M. Regulation of actin filament length in erythrocytes and striated muscle. Curr. Opin. Cell Biol. 1996, 8:86-96.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 86-96
    • Fowler, V.M.1
  • 16
    • 2342609853 scopus 로고    scopus 로고
    • Update on the clinical spectrum and genetics of red blood cell membrane disorders
    • Gallagher P.G. Update on the clinical spectrum and genetics of red blood cell membrane disorders. Curr. Hematol. Rep. 2004, 3:85-91.
    • (2004) Curr. Hematol. Rep. , vol.3 , pp. 85-91
    • Gallagher, P.G.1
  • 17
    • 0026739575 scopus 로고
    • Regulation and post-translational modification of erythrocyte membrane and membrane-skeletal proteins
    • Cohen C.M., Gascard P. Regulation and post-translational modification of erythrocyte membrane and membrane-skeletal proteins. Semin. Hematol. 1992, 29:244-292.
    • (1992) Semin. Hematol. , vol.29 , pp. 244-292
    • Cohen, C.M.1    Gascard, P.2
  • 18
    • 5144222293 scopus 로고    scopus 로고
    • Ubiquitination of spectrin regulates the erythrocyte spectrin-protein-4.1-actin ternary complex dissociation: implications for the sickle cell membrane skeleton
    • Ghatpande S.S., Goodman S.R. Ubiquitination of spectrin regulates the erythrocyte spectrin-protein-4.1-actin ternary complex dissociation: implications for the sickle cell membrane skeleton. Cell. Mol. Biol. (Noisy-le-grand) 2004, 50:67-74.
    • (2004) Cell. Mol. Biol. (Noisy-le-grand) , vol.50 , pp. 67-74
    • Ghatpande, S.S.1    Goodman, S.R.2
  • 19
    • 72149101507 scopus 로고    scopus 로고
    • Current knowledge about the functional roles of phosphorylative changes of membrane proteins in normal and diseased red cells
    • Pantaleo A., De Franceschi L., Ferru E., Vono R., Turrini F. Current knowledge about the functional roles of phosphorylative changes of membrane proteins in normal and diseased red cells. J. Proteomics 2010, 73:445-455.
    • (2010) J. Proteomics , vol.73 , pp. 445-455
    • Pantaleo, A.1    De Franceschi, L.2    Ferru, E.3    Vono, R.4    Turrini, F.5
  • 21
    • 0029166184 scopus 로고
    • Biochemical characterization of a human band 4.1-related protein-tyrosine phosphatase, PTPH1
    • Zhang S.H., Eckberg W.R., Yang Q., Samatar A.A., Tonks N.K. Biochemical characterization of a human band 4.1-related protein-tyrosine phosphatase, PTPH1. J. Biol. Chem. 1995, 270:20067-20072.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20067-20072
    • Zhang, S.H.1    Eckberg, W.R.2    Yang, Q.3    Samatar, A.A.4    Tonks, N.K.5
  • 22
    • 0032756848 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatases and regulation of K-Cl cotransport in human erythrocytes
    • Bize I., Guvenc B., Robb A., Buchbinder G., Brugnara C. Serine/threonine protein phosphatases and regulation of K-Cl cotransport in human erythrocytes. Am. J. Physiol. 1999, 277:C926-C936.
    • (1999) Am. J. Physiol. , vol.277
    • Bize, I.1    Guvenc, B.2    Robb, A.3    Buchbinder, G.4    Brugnara, C.5
  • 23
    • 0036659906 scopus 로고    scopus 로고
    • Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes
    • Bordin L., Brunati A.M., Donella-Deana A., Baggio B., Toninello A., Clari G. Band 3 is an anchor protein and a target for SHP-2 tyrosine phosphatase in human erythrocytes. Blood 2002, 100:276-282.
    • (2002) Blood , vol.100 , pp. 276-282
    • Bordin, L.1    Brunati, A.M.2    Donella-Deana, A.3    Baggio, B.4    Toninello, A.5    Clari, G.6
  • 24
    • 0031005935 scopus 로고    scopus 로고
    • Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3-associated phosphotyrosine phosphatase
    • Zipser Y., Piade A., Kosower N.S. Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3-associated phosphotyrosine phosphatase. FEBS Lett. 1997, 406:126-130.
    • (1997) FEBS Lett. , vol.406 , pp. 126-130
    • Zipser, Y.1    Piade, A.2    Kosower, N.S.3
  • 25
    • 14844314119 scopus 로고    scopus 로고
    • Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation
    • Manno S., Takakuwa Y., Mohandas N. Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation. J. Biol. Chem. 2005, 280:7581-7587.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7581-7587
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 26
  • 27
    • 1542619344 scopus 로고    scopus 로고
    • Protein kinase C isozymes as potential targets for anticancer therapy
    • Hofmann J. Protein kinase C isozymes as potential targets for anticancer therapy. Curr. Cancer Drug Targets 2004, 4:125-146.
    • (2004) Curr. Cancer Drug Targets , vol.4 , pp. 125-146
    • Hofmann, J.1
  • 28
    • 0034793515 scopus 로고    scopus 로고
    • Protein kinase C isoforms in human erythrocytes
    • Govekar R.B., Zingde S.M. Protein kinase C isoforms in human erythrocytes. Ann. Hematol. 2001, 80:531-534.
    • (2001) Ann. Hematol. , vol.80 , pp. 531-534
    • Govekar, R.B.1    Zingde, S.M.2
  • 30
    • 0032514916 scopus 로고    scopus 로고
    • Evidence of zeta protein kinase C involvement in polymorphonuclear neutrophil integrin-dependent adhesion and chemotaxis
    • Laudanna C., Mochly-Rosen D., Liron T., Constantin G., Butcher E.C. Evidence of zeta protein kinase C involvement in polymorphonuclear neutrophil integrin-dependent adhesion and chemotaxis. J. Biol. Chem. 1998, 273:30306-30315.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30306-30315
    • Laudanna, C.1    Mochly-Rosen, D.2    Liron, T.3    Constantin, G.4    Butcher, E.C.5
  • 31
    • 0022259317 scopus 로고
    • Phosphorylation of the glucose transporter in vitro and in vivo by protein kinase C
    • Witters L.A., Vater C.A., Lienhard G.E. Phosphorylation of the glucose transporter in vitro and in vivo by protein kinase C. Nature 1985, 315:777-778.
    • (1985) Nature , vol.315 , pp. 777-778
    • Witters, L.A.1    Vater, C.A.2    Lienhard, G.E.3
  • 35
    • 0037108083 scopus 로고    scopus 로고
    • Protein kinase C activation induces phosphatidylserine exposure on red blood cells
    • de Jong K., Rettig M.P., Low P.S., Kuypers F.A. Protein kinase C activation induces phosphatidylserine exposure on red blood cells. Biochemistry 2002, 41:12562-12567.
    • (2002) Biochemistry , vol.41 , pp. 12562-12567
    • de Jong, K.1    Rettig, M.P.2    Low, P.S.3    Kuypers, F.A.4
  • 36
    • 0029794021 scopus 로고    scopus 로고
    • Specific loss of protein kinase activities in senescent erythrocytes
    • Jindal H.K., Ai Z., Gascard P., Horton C., Cohen C.M. Specific loss of protein kinase activities in senescent erythrocytes. Blood 1996, 88:1479-1487.
    • (1996) Blood , vol.88 , pp. 1479-1487
    • Jindal, H.K.1    Ai, Z.2    Gascard, P.3    Horton, C.4    Cohen, C.M.5
  • 37
    • 0023874060 scopus 로고
    • Modulation of red cell band 4.1 function by cAMP-dependent kinase and protein kinase C phosphorylation
    • Ling E., Danilov Y.N., Cohen C.M. Modulation of red cell band 4.1 function by cAMP-dependent kinase and protein kinase C phosphorylation. J. Biol. Chem. 1988, 263:2209-2216.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2209-2216
    • Ling, E.1    Danilov, Y.N.2    Cohen, C.M.3
  • 38
    • 0019157151 scopus 로고
    • Membrane protein phosphorylation in intact normal and sickle cell erythrocytes
    • Dzandu J.K., Johnson R.M. Membrane protein phosphorylation in intact normal and sickle cell erythrocytes. J. Biol. Chem. 1980, 255:6382-6386.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6382-6386
    • Dzandu, J.K.1    Johnson, R.M.2
  • 39
    • 0029166725 scopus 로고
    • Inhibition of deoxygenation-induced membrane protein dephosphorylation and cell dehydration by phorbol esters and okadaic acid in sickle cells
    • Fathallah H., Coezy E., de Neef R.S., Hardy-Dessources M.D., Giraud F. Inhibition of deoxygenation-induced membrane protein dephosphorylation and cell dehydration by phorbol esters and okadaic acid in sickle cells. Blood 1995, 86:1999-2007.
    • (1995) Blood , vol.86 , pp. 1999-2007
    • Fathallah, H.1    Coezy, E.2    de Neef, R.S.3    Hardy-Dessources, M.D.4    Giraud, F.5
  • 41
    • 0022931548 scopus 로고
    • 2+-dependent phosphorylation of human red cell membrane skeletal proteins
    • 2+-dependent phosphorylation of human red cell membrane skeletal proteins. J. Biol. Chem. 1986, 261:7701-7709.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7701-7709
    • Cohen, C.M.1    Foley, S.F.2
  • 42
    • 0024413059 scopus 로고
    • Alteration in protein kinase C activity and subcellular distribution in sickle erythrocytes
    • Apovo M., Gascard P., Rhoda M.D., Beuzard Y., Giraud F. Alteration in protein kinase C activity and subcellular distribution in sickle erythrocytes. Biochim. Biophys. Acta 1989, 984:26-32.
    • (1989) Biochim. Biophys. Acta , vol.984 , pp. 26-32
    • Apovo, M.1    Gascard, P.2    Rhoda, M.D.3    Beuzard, Y.4    Giraud, F.5
  • 43
    • 42449091192 scopus 로고    scopus 로고
    • Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family
    • Chen J., Deng F., Li J., Wang Q.J. Selective binding of phorbol esters and diacylglycerol by individual C1 domains of the PKD family. Biochem. J. 2008, 411:333-342.
    • (2008) Biochem. J. , vol.411 , pp. 333-342
    • Chen, J.1    Deng, F.2    Li, J.3    Wang, Q.J.4
  • 46
    • 44949287472 scopus 로고
    • Use of ektacytometry to determine red cell susceptibility to oxidative stress
    • Kuypers F.A., Scott M.D., Schott M.A., Lubin B., Chiu D.T. Use of ektacytometry to determine red cell susceptibility to oxidative stress. J. Lab. Clin. Med. 1990, 116:535-545.
    • (1990) J. Lab. Clin. Med. , vol.116 , pp. 535-545
    • Kuypers, F.A.1    Scott, M.D.2    Schott, M.A.3    Lubin, B.4    Chiu, D.T.5
  • 47
    • 0024989557 scopus 로고
    • Oxidation-induced changes in microrheologic properties of the red blood cell membrane
    • Hebbel R.P., Leung A., Mohandas N. Oxidation-induced changes in microrheologic properties of the red blood cell membrane. Blood 1990, 76:1015-1020.
    • (1990) Blood , vol.76 , pp. 1015-1020
    • Hebbel, R.P.1    Leung, A.2    Mohandas, N.3
  • 48
    • 7244238089 scopus 로고    scopus 로고
    • KCl cotransport mediates abnormal sulfhydryl-dependent volume regulation in sickle reticulocytes
    • Joiner C.H., Rettig R.K., Jiang M., Franco R.S. KCl cotransport mediates abnormal sulfhydryl-dependent volume regulation in sickle reticulocytes. Blood 2004, 104:2954-2960.
    • (2004) Blood , vol.104 , pp. 2954-2960
    • Joiner, C.H.1    Rettig, R.K.2    Jiang, M.3    Franco, R.S.4
  • 49
    • 0032101033 scopus 로고    scopus 로고
    • The efficacy of reducing agents or antioxidants in blocking the formation of dense cells and irreversibly sickled cells in vitro
    • Gibson X.A., Shartava A., McIntyre J., Monteiro C.A., Zhang Y., Shah A., Campbell N.F., Goodman S.R. The efficacy of reducing agents or antioxidants in blocking the formation of dense cells and irreversibly sickled cells in vitro. Blood 1998, 91:4373-4378.
    • (1998) Blood , vol.91 , pp. 4373-4378
    • Gibson, X.A.1    Shartava, A.2    McIntyre, J.3    Monteiro, C.A.4    Zhang, Y.5    Shah, A.6    Campbell, N.F.7    Goodman, S.R.8
  • 50
    • 34447513984 scopus 로고    scopus 로고
    • Sickle cell disease: role of reactive oxygen and nitrogen metabolites
    • Wood K.C., Granger D.N. Sickle cell disease: role of reactive oxygen and nitrogen metabolites. Clin. Exp. Pharmacol. Physiol. 2007, 34:926-932.
    • (2007) Clin. Exp. Pharmacol. Physiol. , vol.34 , pp. 926-932
    • Wood, K.C.1    Granger, D.N.2
  • 53
    • 0842287251 scopus 로고    scopus 로고
    • Reactive oxygen species and phosphatidylserine externalization in murine sickle red cells
    • Banerjee T., Kuypers F.A. Reactive oxygen species and phosphatidylserine externalization in murine sickle red cells. Br. J. Haematol. 2004, 124:391-402.
    • (2004) Br. J. Haematol. , vol.124 , pp. 391-402
    • Banerjee, T.1    Kuypers, F.A.2
  • 54
    • 20444468127 scopus 로고    scopus 로고
    • Endothelial cell NADPH oxidase mediates the cerebral microvascular dysfunction in sickle cell transgenic mice
    • Wood K.C., Hebbel R.P., Granger D.N. Endothelial cell NADPH oxidase mediates the cerebral microvascular dysfunction in sickle cell transgenic mice. FASEB J. 2005, 19:989-991.
    • (2005) FASEB J. , vol.19 , pp. 989-991
    • Wood, K.C.1    Hebbel, R.P.2    Granger, D.N.3
  • 56
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology
    • Bedard K., Krause K.H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 2007, 87:245-313.
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2


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