메뉴 건너뛰기




Volumn 49, Issue 21, 2010, Pages 4516-4523

Control of erythrocyte membrane-skeletal cohesion by the spectrin-membrane linkage

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; ERYTHROCYTE MEMBRANE; FUNCTIONAL DIMER; NATIVE MEMBRANES; NONCOVALENT; PHYSIOLOGICAL STATE; RED CELLS; SELF-ASSOCIATIONS; SPECTRIN; TETRAMERS; THIOL REAGENTS;

EID: 77952819298     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1003684     Document Type: Article
Times cited : (34)

References (39)
  • 1
    • 0022510339 scopus 로고
    • Erythrocyte membrane deformability and stability: Two distinct membrane properties that are independently regulated by skeletal protein associations
    • Chasis, J. A. and Mohandas, N. (1986) Erythrocyte membrane deformability and stability: Two distinct membrane properties that are independently regulated by skeletal protein associations J. Cell Biol. 103, 343-350
    • (1986) J. Cell Biol. , vol.103 , pp. 343-350
    • Chasis, J.A.1    Mohandas, N.2
  • 2
    • 58149158216 scopus 로고    scopus 로고
    • Red cell membrane: Past, present, and future
    • Mohandas, N. and Gallagher, P. G. (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
  • 4
    • 0021047024 scopus 로고
    • Sulfhydryl reagents induce altered spectrin self-association, skeletal instability, and increased thermal sensitivity of red cells
    • Smith, D. K. and 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
  • 5
    • 0017899233 scopus 로고
    • Selective alteration of erythrocyte deformabiliby by SH-reagents: Evidence for an involvement of spectrin in membrane shear elasticity
    • Fischer, T. M., Haest, C. W., Stöhr, M., Kamp, D., and Deuticke, B. (1978) Selective alteration of erythrocyte deformabiliby by SH-reagents: Evidence for an involvement of spectrin in membrane shear elasticity Biochim. Biophys. Acta 510, 270-282
    • (1978) Biochim. Biophys. Acta , vol.510 , pp. 270-282
    • Fischer, T.M.1    Haest, C.W.2    Stöhr, M.3    Kamp, D.4    Deuticke, B.5
  • 7
    • 0037200093 scopus 로고    scopus 로고
    • Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane
    • An, X., Lecomte, M. C., Chasis, J. A., Mohandas, N., and Gratzer, W. (2002) Shear-response of the spectrin dimer-tetramer equilibrium in the red blood cell membrane J. Biol. Chem. 277, 31796-31800
    • (2002) J. Biol. Chem. , vol.277 , pp. 31796-31800
    • An, X.1    Lecomte, M.C.2    Chasis, J.A.3    Mohandas, N.4    Gratzer, W.5
  • 8
    • 31444453626 scopus 로고    scopus 로고
    • Mammalian αi-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytes
    • Salomao, M., An, X., Guo, X., Gratzer, W. B., Mohandas, N., and Baines, A. J. (2006) Mammalian αI-spectrin is a neofunctionalized polypeptide adapted to small highly deformable erythrocytes Proc. Natl. Acad. Sci. U.S.A. 103, 643-648
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 643-648
    • Salomao, M.1    An, X.2    Guo, X.3    Gratzer, W.B.4    Mohandas, N.5    Baines, A.J.6
  • 9
    • 0023019557 scopus 로고
    • Analysis of the self-association of human red cell spectrin
    • Shahbakhti, F. and Gratzer, W. B. (1986) Analysis of the self-association of human red cell spectrin Biochemistry 25, 5969-5975
    • (1986) Biochemistry , vol.25 , pp. 5969-5975
    • Shahbakhti, F.1    Gratzer, W.B.2
  • 10
    • 0020080930 scopus 로고
    • A technique to detect reduced mechanical stability of red cell membranes: Relevance to elliptocytic disorders
    • Mohandas, N., Clark, M. R., Health, B. P., Rossi, M., Wolfe, L. C., Lux, S. E., and Shohet, S. B. (1982) A technique to detect reduced mechanical stability of red cell membranes: Relevance to elliptocytic disorders Blood 59, 768-774
    • (1982) Blood , vol.59 , pp. 768-774
    • Mohandas, N.1    Clark, M.R.2    Health, B.P.3    Rossi, M.4    Wolfe, L.C.5    Lux, S.E.6    Shohet, S.B.7
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes
    • DOI 10.1038/280468a0
    • Bennett, V. and Stenbuck, P. J. (1979) The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes Nature 280, 468-473 (Pubitemid 9234557)
    • (1979) Nature , vol.280 , Issue.5722 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.J.2
  • 13
    • 0030966961 scopus 로고    scopus 로고
    • Oxidative damage does not alter membrane phospholipid asymmetry in human erythrocytes
    • de Jong, K., Geldwerth, D., and Kuypers, F. A. (1997) Oxidative damage does not alter membrane phospholipid asymmetry in human erythrocytes Biochemistry 36, 6768-6776
    • (1997) Biochemistry , vol.36 , pp. 6768-6776
    • De Jong, K.1    Geldwerth, D.2    Kuypers, F.A.3
  • 14
    • 0026470325 scopus 로고
    • Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides
    • DeSilva, T. M., Peng, K. C., Speicher, K. D., and Speicher, D. W. (1992) Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides Biochemistry 31, 10872-10878
    • (1992) Biochemistry , vol.31 , pp. 10872-10878
    • Desilva, T.M.1    Peng, K.C.2    Speicher, K.D.3    Speicher, D.W.4
  • 15
    • 0018099901 scopus 로고
    • Self-association of human spectrin. A thermodynamic and kinetic study
    • Ungewickell, E. and Gratzer, W. (1978) Self-association of human spectrin. A thermodynamic and kinetic study Eur. J. Biochem. 88, 379-385
    • (1978) Eur. J. Biochem. , vol.88 , pp. 379-385
    • Ungewickell, E.1    Gratzer, W.2
  • 16
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • Bennett, V. and Baines, A. J. (2001) Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues Physiol. Rev. 81, 1353-1392
    • (2001) Physiol. Rev. , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 17
    • 0018075434 scopus 로고
    • Triton shells of intact erythrocytes
    • Sheetz, M. P. and Sawyer, D. (1978) Triton shells of intact erythrocytes J. Supramol. Struct. 8, 399-412
    • (1978) J. Supramol. Struct. , vol.8 , pp. 399-412
    • Sheetz, M.P.1    Sawyer, D.2
  • 18
    • 0026671203 scopus 로고
    • Conformation and elasticity of the isolated red blood cell membrane skeleton
    • Svoboda, K., Schmidt, C. F., Branton, D., and Block, S. M. (1992) Conformation and elasticity of the isolated red blood cell membrane skeleton Biophys. J. 63, 784-793
    • (1992) Biophys. J. , vol.63 , pp. 784-793
    • Svoboda, K.1    Schmidt, C.F.2    Branton, D.3    Block, S.M.4
  • 19
    • 0024561407 scopus 로고
    • Elasticity of the human red cell membrane skeleton. Effects of temperature and denaturants
    • Vertessy, B. G. and Steck, T. L. (1989) Elasticity of the human red cell membrane skeleton. Effects of temperature and denaturants Biophys. J. 55, 255-262
    • (1989) Biophys. J. , vol.55 , pp. 255-262
    • Vertessy, B.G.1    Steck, T.L.2
  • 20
    • 0022998463 scopus 로고
    • Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes
    • Cohen, A. M., Liu, S. C., Derick, L. H., and Palek, J. (1986) Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes Blood 68, 920-926
    • (1986) Blood , vol.68 , pp. 920-926
    • Cohen, A.M.1    Liu, S.C.2    Derick, L.H.3    Palek, J.4
  • 21
    • 0027179353 scopus 로고
    • Temperature and ionic effects on the interaction of erythroid spectrin with phosphatidylserine membranes
    • MacDonald, R. I. (1993) Temperature and ionic effects on the interaction of erythroid spectrin with phosphatidylserine membranes Biochemistry 32, 6957-6964
    • (1993) Biochemistry , vol.32 , pp. 6957-6964
    • MacDonald, R.I.1
  • 22
    • 0023270477 scopus 로고
    • Electrostatic coupling of spectrin dimers to phosphatidylserine containing lipid lamellae
    • Maksymiw, R., Sui, S. F., Gaub, H., and Sackmann, E. (1987) Electrostatic coupling of spectrin dimers to phosphatidylserine containing lipid lamellae Biochemistry 26, 2983-2990
    • (1987) Biochemistry , vol.26 , pp. 2983-2990
    • Maksymiw, R.1    Sui, S.F.2    Gaub, H.3    Sackmann, E.4
  • 23
  • 24
    • 0023642603 scopus 로고
    • Interaction of spectrin with phospholipids. Quenching of spectrin intrinsic fluorescence by phospholipid suspensions
    • Sikorski, A. F., Michalak, K., and Bobrowska, M. (1987) Interaction of spectrin with phospholipids. Quenching of spectrin intrinsic fluorescence by phospholipid suspensions Biochim. Biophys. Acta 904, 55-60
    • (1987) Biochim. Biophys. Acta , vol.904 , pp. 55-60
    • Sikorski, A.F.1    Michalak, K.2    Bobrowska, M.3
  • 25
    • 0037133206 scopus 로고    scopus 로고
    • Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability
    • Manno, S., Takakuwa, Y., and Mohandas, N. (2002) Identification of a functional role for lipid asymmetry in biological membranes: Phosphatidylserine-skeletal protein interactions modulate membrane stability Proc. Natl. Acad. Sci. U.S.A. 99, 1943-1948
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1943-1948
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 26
    • 0024566916 scopus 로고
    • Aminophospholipid translocase of human erythrocytes: Phospholipid substrate specificity and effect of cholesterol
    • Morrot, G., Hervé, P., Zachowski, A., Fellmann, P., and Devaux, P. F. (1989) Aminophospholipid translocase of human erythrocytes: Phospholipid substrate specificity and effect of cholesterol Biochemistry 28, 3456-3462
    • (1989) Biochemistry , vol.28 , pp. 3456-3462
    • Morrot, G.1    Hervé, P.2    Zachowski, A.3    Fellmann, P.4    Devaux, P.F.5
  • 27
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid β-spectrin
    • Kennedy, S. P., Warren, S. L., Forget, B. G., and Morrow, J. S. (1991) Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid β-spectrin J. Cell Biol. 115, 267-277
    • (1991) J. Cell Biol. , vol.115 , pp. 267-277
    • Kennedy, S.P.1    Warren, S.L.2    Forget, B.G.3    Morrow, J.S.4
  • 28
    • 0019858830 scopus 로고
    • A molecular defect in two families with hemolytic poikilocytic anemia: Reduction of high affinity membrane binding sites for ankyrin
    • Agre, P., Orringer, E. P., Chui, D. H., and Bennett, V. (1981) A molecular defect in two families with hemolytic poikilocytic anemia: Reduction of high affinity membrane binding sites for ankyrin J. Clin. Invest. 68, 1566-1576
    • (1981) J. Clin. Invest. , vol.68 , pp. 1566-1576
    • Agre, P.1    Orringer, E.P.2    Chui, D.H.3    Bennett, V.4
  • 29
    • 0032189026 scopus 로고    scopus 로고
    • Reduced spectrin-ankyrin binding in a South African hereditary elliptocytosis kindred homozygous for spectrin St Claude
    • Burke, J. P., Van Zyl, D., Zail, S. S., and Coetzer, T. L. (1998) Reduced spectrin-ankyrin binding in a South African hereditary elliptocytosis kindred homozygous for spectrin St Claude Blood 92, 2591-2592
    • (1998) Blood , vol.92 , pp. 2591-2592
    • Burke, J.P.1    Van Zyl, D.2    Zail, S.S.3    Coetzer, T.L.4
  • 30
    • 0021169748 scopus 로고
    • Defective binding of spectrin to ankyrin in a kindred with recessively inherited hereditary elliptocytosis
    • Zail, S. S. and Coetzer, T. L. (1984) Defective binding of spectrin to ankyrin in a kindred with recessively inherited hereditary elliptocytosis J. Clin. Invest. 74, 753-762
    • (1984) J. Clin. Invest. , vol.74 , pp. 753-762
    • Zail, S.S.1    Coetzer, T.L.2
  • 31
    • 0034974157 scopus 로고    scopus 로고
    • Spectrin oligomerization is cooperatively coupled to membrane assembly: A linkage targeted by many hereditary hemolytic anemias?
    • Giorgi, M., Cianci, C. D., Gallagher, P. G., and Morrow, J. S. (2001) Spectrin oligomerization is cooperatively coupled to membrane assembly: A linkage targeted by many hereditary hemolytic anemias? Exp. Mol. Pathol. 70, 215-230
    • (2001) Exp. Mol. Pathol. , vol.70 , pp. 215-230
    • Giorgi, M.1    Cianci, C.D.2    Gallagher, P.G.3    Morrow, J.S.4
  • 32
    • 0032510959 scopus 로고    scopus 로고
    • Effect of band 3 subunit equilibrium on the kinetics and affinity of ankyrin binding to erythrocyte membrane vesicles
    • Van Dort, H. M., Moriyama, R., and Low, P. S. (1998) Effect of band 3 subunit equilibrium on the kinetics and affinity of ankyrin binding to erythrocyte membrane vesicles J. Biol. Chem. 273, 14819-14826
    • (1998) J. Biol. Chem. , vol.273 , pp. 14819-14826
    • Van Dort, H.M.1    Moriyama, R.2    Low, P.S.3
  • 33
    • 0021940465 scopus 로고
    • Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton
    • Pasternack, G. R., Anderson, R. A., Leto, T. L., and Marchesi, V. T. (1985) Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton J. Biol. Chem. 260, 3676-3683
    • (1985) J. Biol. Chem. , vol.260 , pp. 3676-3683
    • Pasternack, G.R.1    Anderson, R.A.2    Leto, T.L.3    Marchesi, V.T.4
  • 34
    • 70349254604 scopus 로고    scopus 로고
    • Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion
    • Anong, W. A., Franco, T., Chu, H., Weis, T. L., Devlin, E. E., Bodine, D. M., An, X., Mohandas, N., and Low, P. S. (2009) Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion Blood 114, 1904-1912
    • (2009) Blood , vol.114 , pp. 1904-1912
    • Anong, W.A.1    Franco, T.2    Chu, H.3    Weis, T.L.4    Devlin, E.E.5    Bodine, D.M.6    An, X.7    Mohandas, N.8    Low, P.S.9
  • 36
    • 0024583918 scopus 로고
    • Viscoelastic properties of red cell membrane in hereditary elliptocytosis
    • Chabanel, A., Sung, K. L., Rapiejko, J., Prchal, J. T., Palek, J., Liu, S. C., and Chien, S. (1989) Viscoelastic properties of red cell membrane in hereditary elliptocytosis Blood 73, 592-595
    • (1989) Blood , vol.73 , pp. 592-595
    • Chabanel, A.1    Sung, K.L.2    Rapiejko, J.3    Prchal, J.T.4    Palek, J.5    Liu, S.C.6    Chien, S.7
  • 37
    • 34147151815 scopus 로고    scopus 로고
    • Pathogenic proline mutation in the linker between spectrin repeats: Disease caused by spectrin unfolding
    • Johnson, C. P., Gaetani, M., Ortiz, V., Bhasin, N., Harper, S., Gallagher, P. G., Speicher, D. W., and Discher, D. E. (2007) Pathogenic proline mutation in the linker between spectrin repeats: Disease caused by spectrin unfolding Blood 109, 3538-3543
    • (2007) Blood , vol.109 , pp. 3538-3543
    • Johnson, C.P.1    Gaetani, M.2    Ortiz, V.3    Bhasin, N.4    Harper, S.5    Gallagher, P.G.6    Speicher, D.W.7    Discher, D.E.8
  • 38
    • 0022966969 scopus 로고
    • Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: Dependence on spectrin association state
    • Tsuji, A. and Ohnishi, S. (1986) Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: Dependence on spectrin association state Biochemistry 25, 6133-6139
    • (1986) Biochemistry , vol.25 , pp. 6133-6139
    • Tsuji, A.1    Ohnishi, S.2
  • 39
    • 47249140034 scopus 로고    scopus 로고
    • Molecular epitopes of the ankyrin-spectrin interaction
    • Ipsaro, J. J., Huang, L., Gutierrez, L., and MacDonald, R. I. (2008) Molecular epitopes of the ankyrin-spectrin interaction Biochemistry 47, 7452-7464
    • (2008) Biochemistry , vol.47 , pp. 7452-7464
    • Ipsaro, J.J.1    Huang, L.2    Gutierrez, L.3    MacDonald, R.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.