메뉴 건너뛰기




Volumn 69, Issue 1, 2005, Pages 73-85

Changes in spectrin organisation in leukaemic and lymphoid cells upon chemotherapy

Author keywords

ALL; Apoptosis; Chemotherapy; nHL; Nonerythroid spectrin (fodrin); PKC

Indexed keywords

BUFFER; CELL EXTRACT; CHLORAMBUCIL; CYCLOPHOSPHAMIDE; CYTOSTATIC AGENT; DEXAMETHASONE; DOXORUBICIN; FLUDARABINE; MERCAPTOPURINE; MITOXANTRONE; PHOSPHATIDYLSERINE; PREDNISONE; PROTEIN KINASE C; SPECTRIN; TRITON X 100; VINCRISTINE;

EID: 9944235041     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2004.08.031     Document Type: Article
Times cited : (17)

References (37)
  • 1
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • K. Djinovic-Carugo, M. Gautel, J. Ylanne, and P. Young The spectrin repeat: a structural platform for cytoskeletal protein assemblies FEBS Lett 20 2002 119 123
    • (2002) FEBS Lett , vol.20 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 2
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • V. Bennett, and A.J. Baines Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues Physiol Rev 81 2001 1353 1392
    • (2001) Physiol Rev , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 3
    • 0032577702 scopus 로고    scopus 로고
    • Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton
    • D. Ziemnicka-Kotula, J. Xu, H. Gu, A. Potempska, K.S. Kim, and E.C. Jenkins Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton J Biol Chem 273 1998 13681 13692
    • (1998) J Biol Chem , vol.273 , pp. 13681-13692
    • Ziemnicka-Kotula, D.1    Xu, J.2    Gu, H.3    Potempska, A.4    Kim, K.S.5    Jenkins, E.C.6
  • 4
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • M.A. De Matteis, and J.S. Morrow Spectrin tethers and mesh in the biosynthetic pathway J Cell Sci 113 2000 2331 2343
    • (2000) J Cell Sci , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 5
    • 0035853269 scopus 로고    scopus 로고
    • Monoclonal antibodies to alpha I spectrin Src homology 3 domain associate with macropinocytic vesicles in nonerythroid cells
    • J. Hu, D. Ziemnicka, J. Scalia, and L. Kotula Monoclonal antibodies to alpha I spectrin Src homology 3 domain associate with macropinocytic vesicles in nonerythroid cells Brain Res 898 2001 171 177
    • (2001) Brain Res , vol.898 , pp. 171-177
    • Hu, J.1    Ziemnicka, D.2    Scalia, J.3    Kotula, L.4
  • 6
    • 0033693858 scopus 로고    scopus 로고
    • Human spectrin Src homology 3 domain binding protein 1 regulates macropinocytosis in NIH 3T3 cells
    • J. Xu, D. Ziemnicka, G.S. Merz, and L. Kotula Human spectrin Src homology 3 domain binding protein 1 regulates macropinocytosis in NIH 3T3 cells J Cell Sci 21 2000 3805 3814
    • (2000) J Cell Sci , vol.21 , pp. 3805-3814
    • Xu, J.1    Ziemnicka, D.2    Merz, G.S.3    Kotula, L.4
  • 7
    • 0031457622 scopus 로고    scopus 로고
    • Signalling through scaffold, anchoring, and adaptor proteins
    • T. Pawson, and J.D. Scott Signalling through scaffold, anchoring, and adaptor proteins Science 278 1997 2075 2080
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 8
    • 0027288910 scopus 로고
    • A putative modular domain present in diverse signalling proteins
    • B.J. Mayer, R. Ren, K.L. Clark, and D. Baltimore A putative modular domain present in diverse signalling proteins Cell 73 1993 629 630
    • (1993) Cell , vol.73 , pp. 629-630
    • Mayer, B.J.1    Ren, R.2    Clark, K.L.3    Baltimore, D.4
  • 10
    • 0022629302 scopus 로고
    • Immunofluorescent patterns of spectrin in lymphocyte cell lines
    • J.L. Pauly, R.B. Bankert, and E.A. Repasky Immunofluorescent patterns of spectrin in lymphocyte cell lines J Immunol 136 1986 246 253
    • (1986) J Immunol , vol.136 , pp. 246-253
    • Pauly, J.L.1    Bankert, R.B.2    Repasky, E.A.3
  • 11
    • 0024276519 scopus 로고
    • Activation induces a rapid reorganisation of spectrin in lymphocytes
    • J.K. Lee, J.D. Black, E.A. Repasky, R.T. Kubo, and R.B. Bankert Activation induces a rapid reorganisation of spectrin in lymphocytes Cell 55 1988 807 816
    • (1988) Cell , vol.55 , pp. 807-816
    • Lee, J.K.1    Black, J.D.2    Repasky, E.A.3    Kubo, R.T.4    Bankert, R.B.5
  • 12
    • 0026773055 scopus 로고
    • Translocation of spectrin and protein kinase C to a cytoplasmic aggregate upon lymphocyte activation
    • C.C. Gregorio, R.T. Kubo, B.R. Bankert, and E.A. Repasky Translocation of spectrin and protein kinase C to a cytoplasmic aggregate upon lymphocyte activation Proc Natl Acad Sci USA 89 1992 4947 4951
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4947-4951
    • Gregorio, C.C.1    Kubo, R.T.2    Bankert, B.R.3    Repasky, E.A.4
  • 13
    • 0026770096 scopus 로고
    • Relationship between membrane lipid mobility and spectrin distribution in lymphocytes
    • M. Langner, E.A. Repasky, and S.W. Hui Relationship between membrane lipid mobility and spectrin distribution in lymphocytes FEBS Lett 305 1992 197 202
    • (1992) FEBS Lett , vol.305 , pp. 197-202
    • Langner, M.1    Repasky, E.A.2    Hui, S.W.3
  • 14
    • 0030741077 scopus 로고    scopus 로고
    • Distribution of HSP70, protein kinase C, and spectrin is altered in lymphocytes during a fever-like hyperthermia exposure
    • Y. Di, E.A. Repasky, and J.R. Subjeck Distribution of HSP70, protein kinase C, and spectrin is altered in lymphocytes during a fever-like hyperthermia exposure J Cell Physiol 172 1997 44 54
    • (1997) J Cell Physiol , vol.172 , pp. 44-54
    • Di, Y.1    Repasky, E.A.2    Subjeck, J.R.3
  • 15
    • 0033559490 scopus 로고    scopus 로고
    • Effect of fever like whole-body hyperthermia on lymphocyte spectrin distribution, protein kinase C activity, and uropod formation
    • X.Y. Wang, J.R. Ostberg, and E.A. Repasky Effect of fever like whole-body hyperthermia on lymphocyte spectrin distribution, protein kinase C activity, and uropod formation J Immunol 162 1999 3378 3389
    • (1999) J Immunol , vol.162 , pp. 3378-3389
    • Wang, X.Y.1    Ostberg, J.R.2    Repasky, E.A.3
  • 16
    • 0031595974 scopus 로고    scopus 로고
    • New perspectives on PKC θ, a member of the novel subfamily of protein kinase C
    • N. Meller, A. Altman, and N. Isakov New perspectives on PKC θ, a member of the novel subfamily of protein kinase C Stem Cells 16 1998 178 192
    • (1998) Stem Cells , vol.16 , pp. 178-192
    • Meller, N.1    Altman, A.2    Isakov, N.3
  • 17
    • 0034637536 scopus 로고    scopus 로고
    • Synergistic activation of NF-κB by functional cooperation between Vav and PKC θ in T lymphocytes
    • O. Dienz, S.P. Hehner, W. Droge, and M.L. Schmitz Synergistic activation of NF-κB by functional cooperation between Vav and PKC θ in T lymphocytes J Biol Chem 275 2000 24547 24551
    • (2000) J Biol Chem , vol.275 , pp. 24547-24551
    • Dienz, O.1    Hehner, S.P.2    Droge, W.3    Schmitz, M.L.4
  • 18
    • 0034644505 scopus 로고    scopus 로고
    • Signalling takes shape in the immune system
    • M. Dustin, and A. Chan Signalling takes shape in the immune system Cell 103 2000 283 294
    • (2000) Cell , vol.103 , pp. 283-294
    • Dustin, M.1    Chan, A.2
  • 19
    • 0034005120 scopus 로고    scopus 로고
    • Cytoskeletal polarization and redistribution of cell-surface molecules during T-cell antigen recognition
    • P.A. Merwe, S.J. Davis, A.S. Shaw, and M.L. Dustin Cytoskeletal polarization and redistribution of cell-surface molecules during T-cell antigen recognition Sem Immunol 12 2000 5 21
    • (2000) Sem Immunol , vol.12 , pp. 5-21
    • Merwe, P.A.1    Davis, S.J.2    Shaw, A.S.3    Dustin, M.L.4
  • 20
    • 0033998793 scopus 로고    scopus 로고
    • The role of lipid rafts in T-cell antigen receptor (TCR) signalling
    • P.W. Janes, S.C. Ley, A.I. Magee, and P.S. Kabouridis The role of lipid rafts in T-cell antigen receptor (TCR) signalling Semin Immunol 12 2000 23 34
    • (2000) Semin Immunol , vol.12 , pp. 23-34
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3    Kabouridis, P.S.4
  • 21
    • 0037716812 scopus 로고    scopus 로고
    • Lymphocyte lipid rafts: Structure and function
    • P. Pizzo, and A. Viola Lymphocyte lipid rafts: structure and function Curr Opin Immunol 15 2003 255 260
    • (2003) Curr Opin Immunol , vol.15 , pp. 255-260
    • Pizzo, P.1    Viola, A.2
  • 22
    • 0036604936 scopus 로고    scopus 로고
    • Protein kinase C θ: sssignaling from the center of the T-cell synapse
    • C.W. Arendt, B. Albrecht, T.J. Soos, and D.R. Littman Protein kinase C θ: signaling from the center of the T-cell synapse Curr Opin Immunol 14 2002 323 330
    • (2002) Curr Opin Immunol , vol.14 , pp. 323-330
    • Arendt, C.W.1    Albrecht, B.2    Soos, T.J.3    Littman, D.R.4
  • 23
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T-cell activation
    • A. Grakoui, S.K. Bromley, C. Sumen, M.M. Davis, A.S. Shaw, and P.M. Allen The immunological synapse: a molecular machine controlling T-cell activation Science 285 1999 221 227
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1    Bromley, S.K.2    Sumen, C.3    Davis, M.M.4    Shaw, A.S.5    Allen, P.M.6
  • 24
    • 0033551804 scopus 로고    scopus 로고
    • Protein kinase C and calcineurin synergize to activate IκB kinase and NF-κB in T lymphocytes
    • S.A. Trushin, K.N. Pennington, A. Algecira-Schimnich, and C.V. Paya Protein kinase C and calcineurin synergize to activate IκB kinase and NF-κB in T lymphocytes J Biol Chem 274 1999 22923 22931
    • (1999) J Biol Chem , vol.274 , pp. 22923-22931
    • Trushin, S.A.1    Pennington, K.N.2    Algecira-Schimnich, A.3    Paya, C.V.4
  • 25
    • 0032587013 scopus 로고    scopus 로고
    • Protein kinase C θ, a selective upstream regulator of JNK/SAPK and IL-2 promoter activation in Jurkat T cells
    • N. Ghaffari-Tabrizi, B. Bauer, A. Villunger, G. Baier-Bitterlich, A. Altman, and G. Utermann Protein kinase C θ, a selective upstream regulator of JNK/SAPK and IL-2 promoter activation in Jurkat T cells Eur J Immunol 29 1999 132 142
    • (1999) Eur J Immunol , vol.29 , pp. 132-142
    • Ghaffari-Tabrizi, N.1    Bauer, B.2    Villunger, A.3    Baier-Bitterlich, G.4    Altman, A.5    Utermann, G.6
  • 26
    • 0037462502 scopus 로고    scopus 로고
    • Disruption of transforming growth factor-β signalling in ELF-β spectrin-deficient mice
    • Y. Tang, V. Katuri, A. Dillner, B. Mishra, C. Deng, and L. Mishra Disruption of transforming growth factor-β signalling in ELF-β spectrin-deficient mice Science 299 2003 574 577
    • (2003) Science , vol.299 , pp. 574-577
    • Tang, Y.1    Katuri, V.2    Dillner, A.3    Mishra, B.4    Deng, C.5    Mishra, L.6
  • 27
    • 0033551772 scopus 로고    scopus 로고
    • Transforming growth factor β induces caspase 3-independent cleavage of αiI-spectrin (α-fodrin) coincident with apoptosis
    • T.L. Brown, S. Patil, C.D. Cianci, J.S. Morrow, and P.H. Howe Transforming growth factor β induces caspase 3-independent cleavage of αII-spectrin (α-fodrin) coincident with apoptosis J Biol Chem 274 1999 23256 23262
    • (1999) J Biol Chem , vol.274 , pp. 23256-23262
    • Brown, T.L.1    Patil, S.2    Cianci, C.D.3    Morrow, J.S.4    Howe, P.H.5
  • 28
    • 0032779866 scopus 로고    scopus 로고
    • The effect of caspase-inhibitors on radiation induced apoptosis in human peripheral blood lymphocytes: An electron microscopic approach
    • M. Cornelissen, A. Vral, H. Thierens, and L. De Ridder The effect of caspase-inhibitors on radiation induced apoptosis in human peripheral blood lymphocytes: an electron microscopic approach Apoptosis 4 1999 449 454
    • (1999) Apoptosis , vol.4 , pp. 449-454
    • Cornelissen, M.1    Vral, A.2    Thierens, H.3    De Ridder, L.4
  • 29
    • 0032575377 scopus 로고    scopus 로고
    • Simultaneous degradation of αiI- and βiI-spectrin by caspase 3 (CPP32) in apoptotic cells
    • K.K. Wang, R. Posmantur, R. Nath, K. McGinnis, M. Whitton, and R.V. Talanian Simultaneous degradation of αII- and βII-spectrin by caspase 3 (CPP32) in apoptotic cells J Biol Chem 273 1998 22490 22497
    • (1998) J Biol Chem , vol.273 , pp. 22490-22497
    • Wang, K.K.1    Posmantur, R.2    Nath, R.3    McGinnis, K.4    Whitton, M.5    Talanian, R.V.6
  • 31
    • 0035827604 scopus 로고    scopus 로고
    • Caspase remodelling of the spectrin membrane skeleton during lens development and aging
    • A. Lee, J.S. Morrow, and V.M. Fowler Caspase remodelling of the spectrin membrane skeleton during lens development and aging J Biol Chem 276 2001 20735 20742
    • (2001) J Biol Chem , vol.276 , pp. 20735-20742
    • Lee, A.1    Morrow, J.S.2    Fowler, V.M.3
  • 32
    • 0042167442 scopus 로고    scopus 로고
    • Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis
    • S.T. William, A.N. Smith, C.D. Cianci, J.S. Morrow, and T.L. Brown Identification of the primary caspase 3 cleavage site in alpha II-spectrin during apoptosis Apoptosis 8 2003 353 361
    • (2003) Apoptosis , vol.8 , pp. 353-361
    • William, S.T.1    Smith, A.N.2    Cianci, C.D.3    Morrow, J.S.4    Brown, T.L.5
  • 33
    • 0032193209 scopus 로고    scopus 로고
    • Caspase-independent cell death induced by anti-CD2 and staurosporine in activated human peripheral T lymphocytes
    • O. Deas, C. Dumon, and M. Mac Farlane Caspase-independent cell death induced by anti-CD2 and staurosporine in activated human peripheral T lymphocytes J Immunol 161 1998 3375 3383
    • (1998) J Immunol , vol.161 , pp. 3375-3383
    • Deas, O.1    Dumon, C.2    Mac Farlane, M.3
  • 34
    • 0033047235 scopus 로고    scopus 로고
    • Apoptosis without caspases: An inefficient molecular guillotine?
    • C. Borner, and L. Monney Apoptosis without caspases: an inefficient molecular guillotine? Cell Death Differ 6 1999 497 507
    • (1999) Cell Death Differ , vol.6 , pp. 497-507
    • Borner, C.1    Monney, L.2
  • 35
    • 0034801843 scopus 로고    scopus 로고
    • Caspase-independent apoptotic pathways in T lymphocytes: A minireview
    • N. Bidere, and A. Senik Caspase-independent apoptotic pathways in T lymphocytes: a minireview Apoptosis 6 2001 371 375
    • (2001) Apoptosis , vol.6 , pp. 371-375
    • Bidere, N.1    Senik, A.2
  • 36
    • 0027497573 scopus 로고
    • Interferon-alpha alters spectrin organisation in normal and leukemic human B lymphocytes
    • S.S. Evans, W.C. Wang, C.C. Gregorio, T. Han, and E.A. Repasky Interferon-alpha alters spectrin organisation in normal and leukemic human B lymphocytes Blood 81 1993 759 766
    • (1993) Blood , vol.81 , pp. 759-766
    • Evans, S.S.1    Wang, W.C.2    Gregorio, C.C.3    Han, T.4    Repasky, E.A.5
  • 37
    • 0032832351 scopus 로고    scopus 로고
    • Polarized expression of immunoglobulin, spectrin, and protein kinase C beta II occurs in B cells from normal BALB/c, autoimmune lpr, and anti-ssDNA transgenic, tolerant mice
    • P.A. Masso-Welch, J.D. Black, J. Erikson, and E.A. Repasky Polarized expression of immunoglobulin, spectrin, and protein kinase C beta II occurs in B cells from normal BALB/c, autoimmune lpr, and anti-ssDNA transgenic, tolerant mice J Leukoc Biol 66 1999 617 624
    • (1999) J Leukoc Biol , vol.66 , pp. 617-624
    • Masso-Welch, P.A.1    Black, J.D.2    Erikson, J.3    Repasky, E.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.