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Volumn 103, Issue 8, 2008, Pages 779-781

Cardiac cytoskeleton and arrhythmia: An unexpected role for protein 4.1R in cardiac excitability

Author keywords

Arrhythmia; Cytoskeleton; Na Ca exchanger; Protein 4.1R; Spectrin

Indexed keywords

ERYTHROCYTE BAND 4.1 PROTEIN; GLYCOPHORIN C; PROTEIN 4.1R; PROTEIN P55; UNCLASSIFIED DRUG; 4.1R PROTEIN, MOUSE; CALCIUM; PLASMA PROTEIN; SODIUM CALCIUM EXCHANGE PROTEIN; SODIUM CHANNEL; VOLTAGE GATED NA+ CHANNEL NA(V)1.5A; VOLTAGE-GATED NA+ CHANNEL NA(V)1.5A;

EID: 54449091500     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.108.186460     Document Type: Editorial
Times cited : (5)

References (23)
  • 1
    • 0037452054 scopus 로고    scopus 로고
    • The cytoskeleton, cellular motility and the reductionist agenda
    • Pollard TD. The cytoskeleton, cellular motility and the reductionist agenda. Nature. 2003;422:741-745.
    • (2003) Nature , vol.422 , pp. 741-745
    • Pollard, T.D.1
  • 2
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • Bennett V, Baines AJ. Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues. Physiol Rev. 2001;81: 1353-1392.
    • (2001) Physiol Rev , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 3
    • 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 EP, Chui DH, Bennett V. A molecular defect in two families with hemolytic poikilocytic anemia: reduction of high affinity membrane binding sites for ankyrin. J Clin Invest. 1981;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
  • 4
    • 0020083327 scopus 로고
    • Deficient red-cell spectrin in severe, recessively inherited spherocytosis
    • Agre P, Orringer EP, Bennett V. Deficient red-cell spectrin in severe, recessively inherited spherocytosis. N Engl J Med. 1982;306:1155-1161.
    • (1982) N Engl J Med , vol.306 , pp. 1155-1161
    • Agre, P.1    Orringer, E.P.2    Bennett, V.3
  • 7
    • 43049129979 scopus 로고    scopus 로고
    • X-linked nonsyndromic sinus node dysfunction and atrial fibrillation caused by emerin mutation
    • Karst ML, Herron KJ, Olson TM. X-linked nonsyndromic sinus node dysfunction and atrial fibrillation caused by emerin mutation. J Car-diovasc Electrophysiol. 2008;19:510-515.
    • (2008) J Car-diovasc Electrophysiol , vol.19 , pp. 510-515
    • Karst, M.L.1    Herron, K.J.2    Olson, T.M.3
  • 9
    • 0011727270 scopus 로고
    • Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton
    • Conboy J, Kan YW, Shohet SB, Mohandas N. Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton. Proc Natl Acad Sci U S A. 1986;83:9512-9516.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 9512-9516
    • Conboy, J.1    Kan, Y.W.2    Shohet, S.B.3    Mohandas, N.4
  • 10
    • 0027512335 scopus 로고
    • Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells
    • Conboy JG. Structure, function, and molecular genetics of erythroid membrane skeletal protein 4.1 in normal and abnormal red blood cells. Semin Hematol. 1993;30:58-73.
    • (1993) Semin Hematol , vol.30 , pp. 58-73
    • Conboy, J.G.1
  • 11
    • 0034637458 scopus 로고    scopus 로고
    • Regulation of protein 4.1R, p55, and glycophorin C ternary complex in human erythrocyte membrane
    • Nunomura W, Takakuwa Y, Parra M, Conboy J, Mohandas N. Regulation of protein 4.1R, p55, and glycophorin C ternary complex in human erythrocyte membrane. J Biol Chem. 2000;275:24540-24546.
    • (2000) J Biol Chem , vol.275 , pp. 24540-24546
    • Nunomura, W.1    Takakuwa, Y.2    Parra, M.3    Conboy, J.4    Mohandas, N.5
  • 12
    • 0022494195 scopus 로고
    • Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiency
    • Conboy J, Mohandas N, Tchernia G, Kan YW. Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiency. N Engl J Med. 1986;315:680-685.
    • (1986) N Engl J Med , vol.315 , pp. 680-685
    • Conboy, J.1    Mohandas, N.2    Tchernia, G.3    Kan, Y.W.4
  • 13
    • 42049115740 scopus 로고    scopus 로고
    • Disorders of red cell membrane
    • An X, Mohandas N. Disorders of red cell membrane. Br J Haematol. 2008;141:367-375.
    • (2008) Br J Haematol , vol.141 , pp. 367-375
    • An, X.1    Mohandas, N.2
  • 15
    • 0027391114 scopus 로고
    • An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells
    • Conboy JG, Chasis JA, Winardi R, Tchernia G, Kan YW, Mohandas N. An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells. J Clin Invest. 1993;91:77-82.
    • (1993) J Clin Invest , vol.91 , pp. 77-82
    • Conboy, J.G.1    Chasis, J.A.2    Winardi, R.3    Tchernia, G.4    Kan, Y.W.5    Mohandas, N.6
  • 16
    • 33750727697 scopus 로고    scopus 로고
    • Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily
    • Diakowski W, Grzybek M, Sikorski AF. Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily. Folia Histochem Cytobiol. 2006;44:231-248.
    • (2006) Folia Histochem Cytobiol , vol.44 , pp. 231-248
    • Diakowski, W.1    Grzybek, M.2    Sikorski, A.F.3
  • 18
    • 17644413588 scopus 로고    scopus 로고
    • Cardiac muscle cell cytoskeletal protein 4.1: Analysis of transcripts and subcellular location-relevance to membrane integrity, microstructure, and possible role in heart failure
    • Taylor-Harris PM, Keating LA, Maggs AM, Phillips GW, Birks EJ, Franklin RC, Yacoub MH, Baines AJ, Pinder JC. Cardiac muscle cell cytoskeletal protein 4.1: analysis of transcripts and subcellular location-relevance to membrane integrity, microstructure, and possible role in heart failure. Mamm Genome. 2005;16:137-151.
    • (2005) Mamm Genome , vol.16 , pp. 137-151
    • Taylor-Harris, P.M.1    Keating, L.A.2    Maggs, A.M.3    Phillips, G.W.4    Birks, E.J.5    Franklin, R.C.6    Yacoub, M.H.7    Baines, A.J.8    Pinder, J.C.9
  • 20
    • 15744405775 scopus 로고    scopus 로고
    • Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Nav1.5 on the surface of cardio-myocytes
    • Mohler PJ, Rivolta I, Napolitano C, Lemaillet G, Lambert S, Priori SG, Bennett V. Nav1.5 E1053K mutation causing Brugada syndrome blocks binding to ankyrin-G and expression of Nav1.5 on the surface of cardio-myocytes. Proc Natl Acad Sci U S A. 2004;101:17533-17538.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17533-17538
    • Mohler, P.J.1    Rivolta, I.2    Napolitano, C.3    Lemaillet, G.4    Lambert, S.5    Priori, S.G.6    Bennett, V.7
  • 21
    • 35348996106 scopus 로고    scopus 로고
    • Mechanisms of human arrhythmia syndromes: Abnormal cardiac macromolecular interactions
    • Mohler PJ, Wehrens XH. Mechanisms of human arrhythmia syndromes: abnormal cardiac macromolecular interactions. Physiology (Bethesda, MD). 2007;22:342-350.
    • (2007) Physiology (Bethesda, MD) , vol.22 , pp. 342-350
    • Mohler, P.J.1    Wehrens, X.H.2
  • 22
    • 33847314248 scopus 로고    scopus 로고
    • Ankyrin-G and beta2-spectrin collaborate in biogenesis of lateral membrane of human bronchial epithelial cells
    • Kizhatil K, Yoon W, Mohler PJ, Davis LH, Hoffman JA, Bennett V. Ankyrin-G and beta2-spectrin collaborate in biogenesis of lateral membrane of human bronchial epithelial cells. J Biol Chem. 2007;282: 2029-2037.
    • (2007) J Biol Chem , vol.282 , pp. 2029-2037
    • Kizhatil, K.1    Yoon, W.2    Mohler, P.J.3    Davis, L.H.4    Hoffman, J.A.5    Bennett, V.6
  • 23
    • 39449083242 scopus 로고    scopus 로고
    • Adducin promotes micrometer-scale organization of {beta}2-spectrin in lateral membranes of bronchial epithelial cells
    • Abdi KM, Bennett V. Adducin promotes micrometer-scale organization of {beta}2-spectrin in lateral membranes of bronchial epithelial cells. Mol Biol Cell. 2008;19:536-545
    • (2008) Mol Biol Cell , vol.19 , pp. 536-545
    • Abdi, K.M.1    Bennett, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.